Recombinant EBOV soluble GP

Description: Peptides & Proteins|Recombinant Proteins

Description: Peptides & Proteins|Recombinant Proteins

Description: Peptides & Proteins|Recombinant Proteins

Description: EBOV GPDTM, recombinant protein from mammalian cells.

Description: Ebola virus (subtype Sudan, strain Gulu) Glycoprotein, recombinant protein.

Description: Ebola virus (subtype Sudan, strain Gulu) Glycoprotein, recombinant protein.

Description: Ebola virus (subtype Sudan, strain Gulu) Glycoprotein, recombinant protein.

Description: Ebola virus (subtype Sudan, strain Gulu) Glycoprotein, recombinant protein.

Description: Ebola virus (subtype Zaire, strain H.sapiens-wt/GIN/2014/Kissidougou-C15) Glycoprotein, recombinant protein.

Description: Ebola virus (subtype Zaire, strain H.sapiens-wt/GIN/2014/Kissidougou-C15) Glycoprotein, recombinant protein.

Description: EBOV GPDTM, recombinant protein from Sf9 cells.

Description: FasL is a cytokine that binds to TNFRSF6/Fas, a receptor that transduces the apoptotic signal into cells. Is involved in cytotoxic T cell mediated apoptosis and in T cell development.

Description: BAFF is mainly produced by innate immune cells such as neutrophils, monocytes, macrophages, dendritic cells, follicular dendritic cells. T cells, activated B cells, some malignant B cells and also non-lymphoid cells like astrocytes, synoviocytes and epithelial cells can also produce BAFF. BAFF binds three distinct receptors (BAFF-R, TACI and BCMA) expressed predominantly on B cells, although activated T cells also express BAFF-R. BAFF is a master regulator of peripheral B cell survival, and together with IL-6, promotes Ig class-switching and plasma cell differentiation. Besides its major role in B cell biology, BAFF co-stimulates activated T cells. Deregulated expression of BAFF leads to autoimmune disorders in mice. In humans, elevated levels of soluble BAFF have been detected in the serum of patients with various autoimmune diseases such as Sjoegren syndrome, Rheumatoid arthritis (RA), Multiple sclerosis (MS) and Systemic Lupus Erythematosus (SLE). BAFF has also increased levels in some lymphoid cancers.

Description: Fc (human):FasL, Soluble (human) is a high activity construct in which two trimeric FasL are artificially linked via the Fc binding domain of human IgG1. This construct very effectively simulates the natural membrane-assisted aggregation of FasL in vivo. FasL is a cytokine that binds to TNFRSF6/Fas, a receptor that transduces the apoptotic signal into cells. It is involved in cytotoxic T cell mediated apoptosis and in T cell development.

Description: CD14 is a cell surface anchored glycoprotein that is expressed predominantly by monocytes and tissue macrophages. CD14 associates with MD-2 (LY-96) and TLR4 to form a receptor complex, which signals specifically in response to bacterial lipopolysaccharide (LPS) binding. The CD14/MD-2/TLR4 receptor complex signals via MyD88, TIRAP, and TRAF6, and ultimately activates NF-kappa-β. CD14 also exists in a soluble form, designated as sCD14, which is capable of specifically binding LPS in the extracellular space. Recombinant sCD14 is a 331 amino acid glycoprotein comprising the extracellular portion of the CD14 receptor.

Description: CD14 is a cell surface anchored glycoprotein that is expressed predominantly by monocytes and tissue macrophages. CD14 associates with MD-2 (LY-96) and TLR4 to form a receptor complex, which signals specifically in response to bacterial lipopolysaccharide (LPS) binding. The CD14/MD-2/TLR4 receptor complex signals via MyD88, TIRAP, and TRAF6, and ultimately activates NF-kappa-β. CD14 also exists in a soluble form, designated as sCD14, which is capable of specifically binding LPS in the extracellular space. Recombinant sCD14 is a 331 amino acid glycoprotein comprising the extracellular portion of the CD14 receptor.

Description: CD23, the low affinity receptor for IgE, belongs to the C-type lectin structural family and plays a role in the regulation of IgE synthesis and IgE mediated activities. It is found both as a transmembrane receptor protein and in a soluble form, which is generated by proteolytic cleavage of membrane bound CD23. The predominant soluble form of CD23 (sCD23) consists of 172 amino acids corresponding to the extracellular domain of the full length precursor. sCD23, in addition to binding IgE, also exerts a number of IgE independent activities, such as promoting the activation and differentiation of B-cells and stimulating the release of pro-inflammatory cytokines from monocytes. Recombinant human sCD23 is a 19.2 kDa non-glycosylated protein containing 172 amino-acid residues.

Description: CD23, the low affinity receptor for IgE, belongs to the C-type lectin structural family and plays a role in the regulation of IgE synthesis and IgE mediated activities. It is found both as a transmembrane receptor protein and in a soluble form, which is generated by proteolytic cleavage of membrane bound CD23. The predominant soluble form of CD23 (sCD23) consists of 172 amino acids corresponding to the extracellular domain of the full length precursor. sCD23, in addition to binding IgE, also exerts a number of IgE independent activities, such as promoting the activation and differentiation of B-cells and stimulating the release of pro-inflammatory cytokines from monocytes. Recombinant human sCD23 is a 19.2 kDa non-glycosylated protein containing 172 amino-acid residues.

Description: GITRL (Glucocorticoid-induced TNF receptor ligand) is expressed on dendritic cells (DC), monocytes, macrophages, B cells, activated T cells, endothelial cells, osteoclasts and various healthy non-lymphoid tissues (e. g. testis). GITRL is constitutively expressed and released as soluble form by solid tumors and various hematopoietic malignancies. GITRL causes differentiation of osteoclasts, activation of macrophages, but also alteration of carcinoma and leukemia cells and influences apoptosis. Binding to GITR is important in regulating T cell proliferation and TCR-mediated apoptosis. GITRL is implicated in development of autoimmune diseases and in the immune response against infectious pathogens and tumors.

Description: TNF-related apoptosis-inducing ligand (TRAIL; Apo2L;CD253; TNFSF10) is a type II transmembrane protein of about 34kDa. Like most members of the tumor necrosis factor (TNF) superfamily of cytokines TRAIL can be cleaved at the cell surface by metalloproteases to form a soluble molecule. Active TRAIL forms trimers and specifically binds to fi ve distinct receptors: TRAIL-R1 (DR4; Apo2;CD261; TNFRSF10A), TRAIL-R2 (DR5; KILLER; TRICK2A;TRICK2B; CD262; TNFRSF10B), TRAIL-R3 (DcR1;LIT; TRID; CD263; TNFRSF10C), TRAIL-R4 (DcR2;TRUNDD; CD264; TNFRSF10D), and osteoprotegerin (OPG; OCIF; TNFRSF11B). Trimerized TRAIL triggers apoptosis upon ligation of cell surface TRAIL-R1 and/or TRAIL-R2 by inducingthe formation of the so-called multiprotein death-inducing signaling complex (DISC).

Description: RANKL is an osteoclast differentiation and activation factor. Augments the ability of dendritic cells to stimulate naive T cell proliferation. Important regulator of interactions between T cells and dendritic cells and may play a role in the regulation of the T cell-dependent immune response. RANKL plays an important role in the progression of breast cancer.

Description: LIGHT (HVEML; CD258) is a cytokine that binds to TNFRSF3/LTBR. It activates NF-kappaB, stimulates the proliferation of T cells, and inhibits growth of the adenocarcinoma HT-29. Acts as a receptor for Herpes simplex virus.

Description: izTRAIL is a newly available, highly active recombinant form of soluble human TRAIL. Due to a trimerizing N-terminal isoleucine zipper (iz) motif the intrinsic trimerization of TRAIL, required for apoptosis-inducing activity of TRAIL, is enhanced when compared to non-tagged soluble human TRAIL (shTRAIL). Therefore, izTRAIL is a potent inducer of apoptosis in many human cancer cells, but not normal human hepatocytes. In addition, the half-life of izTRAIL is about eight-fold higher than the half-life of shTRAIL. These properties render izTRAIL highly suitable for both, in vitro and in vivo use, particularly for studies in which investigators plan to transfer their in vitro results into an in vivo system with human cancer cells in xenotransplant settings examining susceptibility to TRAIL-induced apoptosis.

Description: Ebola virus (subtype Zaire, strain H.sapiens-wt/GIN/2014/Kissidougou-C15) Glycoprotein (Virion spike glycoprotein), recombinant protein.

Description: Ebola virus (subtype Zaire, strain H.sapiens-wt/GIN/2014/Kissidougou-C15) Glycoprotein (Virion spike glycoprotein), recombinant protein.

Description: TNF-related apoptosis-inducing ligand (TRAIL; Apo2L;CD253; TNFSF10) is a type II transmembrane protein of about 34kDa. Like most members of the tumor necrosis factor (TNF) superfamily of cytokines TRAIL can be cleaved at the cell surface by metalloproteases to form a soluble molecule. Active TRAIL forms trimers and specifically binds to five distinct receptors: TRAIL-R1 (DR4; Apo2;CD261; TNFRSF10A), TRAIL-R2 (DR5; KILLER; TRICK2A;TRICK2B; CD262; TNFRSF10B), TRAIL-R3 (DcR1;LIT; TRID; CD263; TNFRSF10C), TRAIL-R4 (DcR2;TRUNDD; CD264; TNFRSF10D), and osteoprotegerin (OPG; OCIF; TNFRSF11B). Trimerized TRAIL triggers apoptosis upon ligation of cell surface TRAIL-R1 and/or TRAIL-R2 by inducing the formation of the so-called multiprotein death-inducing signaling complex (DISC).

Description: The TNF family ligand ectodysplasin A (EDA) and its receptor EDAR are required for proper development of skin appendages such as hair, teeth, and eccrine sweat glands. Loss of function mutations in the Eda gene cause X-linked hypohidrotic ectodermal dysplasia (XLHED), a condition that can be ameliorated in mice and dogs by timely administration of recombinant EDA. The Eda gene on the X chromosome is transcribed as multiple splice variants, only two of which code for the receptor-binding C-terminal TNF homology domain. These two variants code for 391- and 389-amino acid-long proteins called EDA1 and EDA2. EDA1 binds EDAR, whereas EDA2 binds to another receptor, XEDAR. The biology of EDA2 and XEDAR is distinct from that of EDA1. Indeed, XEDAR-deficient mice have no obvious ectodermal dysplasia phenotype, whereas mice deficient in EDA, EDAR, or the signaling adaptor protein EDARADD all display virtually indistinguishable ectodermal dysplasia phenotypes, indicating the predominance of the EDA1-EDAR axis in the development of skin-derived appendages.

Description: Cluster determinant 4 (CD4), a type I transmembrane glycoprotein of the immunoglobulin family of receptors, playsan integral role in signal transduction and T-cell differentiation, development and activation. CD4 is constitutively expressed on thesurface of various immune cells, including monocytes, macrophages, eosinophils, dendritic cells, and most prominently Tlymphocytes,where it functions as an essential co-receptor and co-ligand for T-cell receptor (TCR) and major histocompatibilitycomplex class II (MHC-II) molecules. Ligation by MHC-II molecules on the surface of antigen-presenting cells can serve toinfluence adaptive immunity by facilitating helper T-cell activation and macrophage differentiation, while ligation by proinflammatorycytokine IL-16 can contribute to innate immunity by chemoattracting CD4-expressing peripheral immune cells alongan IL-16 gradient for their recruitment and activation at sites of inflammation. The protean functionality of CD4 extends pastimmunity as CD4 also notably serves as the major receptor for HIV-1 and human herpes virus 7 (HHV-7) infections. During HIVpathogenesis, CD4 acts instrumentally as a high-affinity entry receptor for the internalization of HIV-1 following binding of the viralenvelope glycoprotein gp120 to CD4’s extracellular domain. Recombinant Human sCD4 is amonomeric glycoprotein of 371 amino acid residues, which correspond to the extracellular CD4 domain, and a calculated molecularweight of 41.3 kDa. As a result of glycosylation, Recombinant Human sCD4 migrates with an apparent molecular mass of approximately 45-55 kDa by SDS-Page Gel analysis, under reducing conditions.

Description: Cluster determinant 4 (CD4), a type I transmembrane glycoprotein of the immunoglobulin family of receptors, playsan integral role in signal transduction and T-cell differentiation, development and activation. CD4 is constitutively expressed on thesurface of various immune cells, including monocytes, macrophages, eosinophils, dendritic cells, and most prominently Tlymphocytes,where it functions as an essential co-receptor and co-ligand for T-cell receptor (TCR) and major histocompatibilitycomplex class II (MHC-II) molecules. Ligation by MHC-II molecules on the surface of antigen-presenting cells can serve toinfluence adaptive immunity by facilitating helper T-cell activation and macrophage differentiation, while ligation by proinflammatorycytokine IL-16 can contribute to innate immunity by chemoattracting CD4-expressing peripheral immune cells alongan IL-16 gradient for their recruitment and activation at sites of inflammation. The protean functionality of CD4 extends pastimmunity as CD4 also notably serves as the major receptor for HIV-1 and human herpes virus 7 (HHV-7) infections. During HIVpathogenesis, CD4 acts instrumentally as a high-affinity entry receptor for the internalization of HIV-1 following binding of the viralenvelope glycoprotein gp120 to CD4’s extracellular domain. Recombinant Human sCD4 is amonomeric glycoprotein of 371 amino acid residues, which correspond to the extracellular CD4 domain, and a calculated molecularweight of 41.3 kDa. As a result of glycosylation, Recombinant Human sCD4 migrates with an apparent molecular mass of approximately 45-55 kDa by SDS-Page Gel analysis, under reducing conditions.

Description: RANKL and RANK are members of the TNF superfamily of ligands and receptors that play an important role in the regulation of specific immunity and bone turnover. RANK (receptor) was originally identified as a dendritic-cell-membrane protein, which by interacting with RANKL augments the ability of dendritic cells to stimulate naïve T-cell proliferation in a mixed lymphocyte reaction, to promote the survival of RANK + T cells, and to regulate T-cell-dependent immune response. RANKL, which is expressed in a variety of cells including osteoblasts, fibroblasts, activated T-cells and bone marrow stromal cells, is also capable of interacting with a decoy receptor called OPG. Binding of soluble OPG to sRANKL inhibits osteoclastogenesis by interrupting the signaling between stromal cells and osteoclastic progenitor cells, thereby leading to excess accumulation of bone and cartilage. Recombinant rat sRANKL is a 19.4 kDa polypeptide comprising the TNF homologous region of RANKL (174 amino acid residues).

Description: RANKL and RANK are members of the TNF superfamily of ligands and receptors that play an important role in the regulation of specific immunity and bone turnover. RANK (receptor) was originally identified as a dendritic-cell-membrane protein, which by interacting with RANKL augments the ability of dendritic cells to stimulate naïve T-cell proliferation in a mixed lymphocyte reaction, to promote the survival of RANK + T cells, and to regulate T-cell-dependent immune response. RANKL, which is expressed in a variety of cells including osteoblasts, fibroblasts, activated T-cells and bone marrow stromal cells, is also capable of interacting with a decoy receptor called OPG. Binding of soluble OPG to sRANKL inhibits osteoclastogenesis by interrupting the signaling between stromal cells and osteoclastic progenitor cells, thereby leading to excess accumulation of bone and cartilage. Recombinant rat sRANKL is a 19.4 kDa polypeptide comprising the TNF homologous region of RANKL (174 amino acid residues).

Description: CD14 is a cell surface anchored glycoprotein that is expressed predominantly by monocytes and tissue macrophages. CD14 associates with MD-2 (LY-96) and TLR4 to form a receptor complex, which signals specifically in response to bacterial lipopolysaccharide (LPS) binding. The CD14/MD-2/TLR4 receptor complex signals via MyD88, TIRAP, and TRAF6, and ultimately activates NF-kappaB. CD14 also exists in a soluble form, designated as sCD14, which is capable of specifically binding LPS in the extracellular space. Recombinant sCD14 is a 331 amino acid glycoprotein comprising the extracellular portion of the CD14 receptor.

Description: CD14 is a cell surface anchored glycoprotein that is expressed predominantly by monocytes and tissue macrophages. CD14 associates with MD-2 (LY-96) and TLR4 to form a receptor complex, which signals specifically in response to bacterial lipopolysaccharide (LPS) binding. The CD14/MD-2/TLR4 receptor complex signals via MyD88, TIRAP, and TRAF6, and ultimately activates NF-kappaB. CD14 also exists in a soluble form, designated as sCD14, which is capable of specifically binding LPS in the extracellular space. Recombinant sCD14 is a 331 amino acid glycoprotein comprising the extracellular portion of the CD14 receptor.

Description: CD22 is a 135 kDa B-cell restricted sialoglycoprotein that binds to oligosaccharides containing 2-6-linked sialic acid residues. It is present in the cytoplasm of nearly all B-lineage cells and is also expressed on the surface of B-cells during advance stages of differentiation. Although the exact physiological function of CD22 is unclear, it appears to play a role in B-cell activation and to act as an adhesion molecule. The potential therapeutic use of CD22 and anti-CD22 may be useful in diagnostic and/or treatment of leukemia, lymphoma, non-Hodgkin's lymphoma and certain autoimmune conditions. (Cesano A. and Gayko U. Semin. Oncol. Apr. 2003 (2): 253-257). Recombinant human CD22 is a soluble 75.0 kDa (666 amino acid residues) protein which corresponds to the extracellular domain of CD22.

Description: CD22 is a 135 kDa B-cell restricted sialoglycoprotein that binds to oligosaccharides containing 2-6-linked sialic acid residues. It is present in the cytoplasm of nearly all B-lineage cells and is also expressed on the surface of B-cells during advance stages of differentiation. Although the exact physiological function of CD22 is unclear, it appears to play a role in B-cell activation and to act as an adhesion molecule. The potential therapeutic use of CD22 and anti-CD22 may be useful in diagnostic and/or treatment of leukemia, lymphoma, non-Hodgkin's lymphoma and certain autoimmune conditions. (Cesano A. and Gayko U. Semin. Oncol. Apr. 2003 (2): 253-257). Recombinant human CD22 is a soluble 75.0 kDa (666 amino acid residues) protein which corresponds to the extracellular domain of CD22.

Description: Recombinant human soluble EGFR is produced as a glycosylated monomeric protein with a mass of approximately 70 kDa in insect cells. The epidermal growth factor receptor (EGFR) subfamily of receptor tyrosine kinases comprises four members: EGFR (also known as HER1, ErbB1 or ErbB), ErbB2 (Neu, HER-2), ErbB3 (HER-3), and ErbB4 (HER-4). All family members are type I transmembrane glycoprotein that has an extracellular domain which contains two cysteine-rich domains separated by a spacer region that is involved in ligand-binding, and a cytoplasmic domain which has a membrane-proximal tyrosine kinase domain and a C-terminal tail with multiple tyrosine autophosphorylation sites. The human EGFR gene encodes a 1210 amino acid (aa) residue precursor with a 24aa putative signal peptide, a 621aa extracellular domain, a 23aa transmembrane domain, and a 542aa cytoplasmic domain. EGFR has been shown to bind a subset of the EGF family ligands, including EGF, amphiregulin, TGF-alpha, betacellulin, epiregulin, heparin-binding EGF and neuregulin-2 in the absence of a co-receptor. Ligand binding induces EGFR homodimerization as well as heterodimerization with ErbB2, resulting in kinase activation, tyrosine phosphorylation and cell signaling. EGFR can also be recruited to form heterodimers with the ligand-activated ErbB3 or ErbB4. EGFR signaling has been shown to regulate multiple biological functions including cell proliferation, differentiation, motility and apoptosis. In addition, EGFR signaling has also been shown to play a role in carcinogenesis.

Description: Recombinant human soluble EGFR is produced as a glycosylated monomeric protein with a mass of approximately 70 kDa in insect cells. The epidermal growth factor receptor (EGFR) subfamily of receptor tyrosine kinases comprises four members: EGFR (also known as HER1, ErbB1 or ErbB), ErbB2 (Neu, HER-2), ErbB3 (HER-3), and ErbB4 (HER-4). All family members are type I transmembrane glycoprotein that has an extracellular domain which contains two cysteine-rich domains separated by a spacer region that is involved in ligand-binding, and a cytoplasmic domain which has a membrane-proximal tyrosine kinase domain and a C-terminal tail with multiple tyrosine autophosphorylation sites. The human EGFR gene encodes a 1210 amino acid (aa) residue precursor with a 24aa putative signal peptide, a 621aa extracellular domain, a 23aa transmembrane domain, and a 542aa cytoplasmic domain. EGFR has been shown to bind a subset of the EGF family ligands, including EGF, amphiregulin, TGF-alpha, betacellulin, epiregulin, heparin-binding EGF and neuregulin-2 in the absence of a co-receptor. Ligand binding induces EGFR homodimerization as well as heterodimerization with ErbB2, resulting in kinase activation, tyrosine phosphorylation and cell signaling. EGFR can also be recruited to form heterodimers with the ligand-activated ErbB3 or ErbB4. EGFR signaling has been shown to regulate multiple biological functions including cell proliferation, differentiation, motility and apoptosis. In addition, EGFR signaling has also been shown to play a role in carcinogenesis.

Description: Receptor-tyrosine-kinase-like orphan receptor 1 (ROR1) is a tumor-associated, surface protein predominantly expressed during embryogenesis, where it is involved in organ morphogenesis, nervous system development, and neural progenitor cell maintenance and survival. Virtual absent from normal pediatric and adult tissues, with the exception of low-level expression in a subset of immature B-cell precursors known as hematogones and adipocytes, ROR1 is notably overexpressed, and considered a survival factor, in a number of B lymphoid and epithelial malignancies: most notably, but not exclusively, including chronic lymphocytic leukemia (CLL), mantle cell lymphoma (MCL), acute lymphoblastic leukemia (ALL), marginal zone lymphoma, lung adenocarcinoma. First identified during PCR-based cloning of a human neuroblastoma cell line in search of tyrosine kinases similar to tropomyosin-receptor-kinase (Trk) neurotropic receptors, ROR1, along with the related receptor tyrosine kinase (RTK) ROR2, was catalogued as an “orphan” receptor due to the fact its related ligand remained elusive. Wnt-5a has since been suggested as a candidate ligand for ROR1, and ROR1 has been implicated to function as a pseudokinase, promoting proliferation and resistance to apoptosis in cancer cells through interaction with Wnt-5a, and TCL1-co-activation of AKT. ROR1 is expressed as a glycoprotein containing extracellular immunoglobulin (Ig)-like, Frizzled, and Kringle domains, as well as an intracellular region containing a tyrosine kinase domain. Recombinant Human ROR1 is a glycoprotein containing 377 amino acid residues, and has a calculated molecular weight of approximately 42.4 kDa. As a result of glycosylation, Recombinant Human ROR1 migrates with an apparent molecular mass of approximately 55-65 kDa by SDS-PAGE gel, under reducing and non-reducing conditions.

Description: Receptor-tyrosine-kinase-like orphan receptor 1 (ROR1) is a tumor-associated, surface protein predominantly expressed during embryogenesis, where it is involved in organ morphogenesis, nervous system development, and neural progenitor cell maintenance and survival. Virtual absent from normal pediatric and adult tissues, with the exception of low-level expression in a subset of immature B-cell precursors known as hematogones and adipocytes, ROR1 is notably overexpressed, and considered a survival factor, in a number of B lymphoid and epithelial malignancies: most notably, but not exclusively, including chronic lymphocytic leukemia (CLL), mantle cell lymphoma (MCL), acute lymphoblastic leukemia (ALL), marginal zone lymphoma, lung adenocarcinoma. First identified during PCR-based cloning of a human neuroblastoma cell line in search of tyrosine kinases similar to tropomyosin-receptor-kinase (Trk) neurotropic receptors, ROR1, along with the related receptor tyrosine kinase (RTK) ROR2, was catalogued as an “orphan” receptor due to the fact its related ligand remained elusive. Wnt-5a has since been suggested as a candidate ligand for ROR1, and ROR1 has been implicated to function as a pseudokinase, promoting proliferation and resistance to apoptosis in cancer cells through interaction with Wnt-5a, and TCL1-co-activation of AKT. ROR1 is expressed as a glycoprotein containing extracellular immunoglobulin (Ig)-like, Frizzled, and Kringle domains, as well as an intracellular region containing a tyrosine kinase domain. Recombinant Human ROR1 is a glycoprotein containing 377 amino acid residues, and has a calculated molecular weight of approximately 42.4 kDa. As a result of glycosylation, Recombinant Human ROR1 migrates with an apparent molecular mass of approximately 55-65 kDa by SDS-PAGE gel, under reducing and non-reducing conditions.

Description: CD23, the low affinity receptor for IgE, belongs to the C-type lectin structural family and plays a role in the regulation of IgE synthesis and IgE mediated activities. It is found both as a transmembrane receptor protein and in a soluble form, which is generated by proteolytic cleavage of membrane bound CD23. The predominant soluble form of CD23 (sCD23) consists of 172 amino acids corresponding to the extracellular domain of the full length precursor. sCD23, in addition to binding IgE, also exerts a number of IgE independent activities, such as promoting the activation and differentiation of B-cells and stimulating the release of pro-inflammatory cytokines from monocytes. Recombinant human sCD23 is a 19.2 kDa non-glycosylated protein containing 172 amino-acid residues.

Description: CD23, the low affinity receptor for IgE, belongs to the C-type lectin structural family and plays a role in the regulation of IgE synthesis and IgE mediated activities. It is found both as a transmembrane receptor protein and in a soluble form, which is generated by proteolytic cleavage of membrane bound CD23. The predominant soluble form of CD23 (sCD23) consists of 172 amino acids corresponding to the extracellular domain of the full length precursor. sCD23, in addition to binding IgE, also exerts a number of IgE independent activities, such as promoting the activation and differentiation of B-cells and stimulating the release of pro-inflammatory cytokines from monocytes. Recombinant human sCD23 is a 19.2 kDa non-glycosylated protein containing 172 amino-acid residues.

Description: CD34 is a highly glycosylated type I membrane protein that is selectively expressed on hematopoietic stem cells and vascular endothelium. It has been widely used as a molecular marker for the identification, isolation, and manipulation of hemopoietic stem cells and progenitors. CD34 can function as a regulator of hemopoietic cell adhesion by mediating the attachment of stem cells to bone marrow stromal cells or other bone marrow components. The full length human CD34 is a 385 amino acid protein, consisting of a 31 amino acid signal sequence, a 74 amino acid cytoplasmic domain, a 21 amino acid transmembrane domain and a 259 amino acid extracellular domain. Recombinant human sCD34 is a 258 amino acid polypeptide containing only the extracellular domain of the full length CD34 protein.

Description: CD34 is a highly glycosylated type I membrane protein that is selectively expressed on hematopoietic stem cells and vascular endothelium. It has been widely used as a molecular marker for the identification, isolation, and manipulation of hemopoietic stem cells and progenitors. CD34 can function as a regulator of hemopoietic cell adhesion by mediating the attachment of stem cells to bone marrow stromal cells or other bone marrow components. The full length human CD34 is a 385 amino acid protein, consisting of a 31 amino acid signal sequence, a 74 amino acid cytoplasmic domain, a 21 amino acid transmembrane domain and a 259 amino acid extracellular domain. Recombinant human sCD34 is a 258 amino acid polypeptide containing only the extracellular domain of the full length CD34 protein.

Description: CD34 is a highly glycosylated type I membrane protein that is selectively expressed on hematopoietic stem cells and vascular endothelium. It has been widely used as a molecular marker for the identification, isolation, and manipulation of hemopoietic stem cells and progenitors. CD34 can function as a regulator of hemopoietic cell adhesion by mediating the attachment of stem cells to bone marrow stromal cells or other bone marrow components. The full length human CD34 is a 385 amino acid protein, consisting of a 31 amino acid signal sequence, a 74 amino acid cytoplasmic domain, a 21 amino acid transmembrane domain and a 259 amino acid extracellular domain. Recombinant human sCD34 is a 258 amino acid polypeptide containing only the extracellular domain of the full length CD34 protein.

Description: CD34 is a highly glycosylated type I membrane protein that is selectively expressed on hematopoietic stem cells and vascular endothelium. It has been widely used as a molecular marker for the identification, isolation, and manipulation of hemopoietic stem cells and progenitors. CD34 can function as a regulator of hemopoietic cell adhesion by mediating the attachment of stem cells to bone marrow stromal cells or other bone marrow components. The full length human CD34 is a 385 amino acid protein, consisting of a 31 amino acid signal sequence, a 74 amino acid cytoplasmic domain, a 21 amino acid transmembrane domain and a 259 amino acid extracellular domain. Recombinant human sCD34 is a 258 amino acid polypeptide containing only the extracellular domain of the full length CD34 protein.

Description: ROR2 is a signaling receptor for Wnt ligands that is known to play important roles in limb development, but having no essential roles known in adult tissues. Recent evidence has implicated ROR2 in mediating both canonical and non-canonical signaling pathways. ROR2 was initially found to be highly expressed in osteosarcoma and renal cell carcinomas, and has recently been found in an increasingly long list of cancers currently including melanoma, colon cancer, melanoma, squamous cell carcinoma of the head and neck, and breast cancer. In the majority of these cancer types, ROR2 expression is associated with more aggressive disease states, consistent with a role mediating Wnt signaling regardless of the canonical or non-canonical signal. Because of the pattern of tissue distribution, the association with high-risk diseases, and the cell surface localization of this receptor, ROR2 has been identified as a potential high value target for therapeutic development. However, the recent discovery that ROR2 may function through non-kinase activities challenges this strategy and opens up opportunities to target this important molecule through alternative means.

Description: ROR2 is a signaling receptor for Wnt ligands that is known to play important roles in limb development, but having no essential roles known in adult tissues. Recent evidence has implicated ROR2 in mediating both canonical and non-canonical signaling pathways. ROR2 was initially found to be highly expressed in osteosarcoma and renal cell carcinomas, and has recently been found in an increasingly long list of cancers currently including melanoma, colon cancer, melanoma, squamous cell carcinoma of the head and neck, and breast cancer. In the majority of these cancer types, ROR2 expression is associated with more aggressive disease states, consistent with a role mediating Wnt signaling regardless of the canonical or non-canonical signal. Because of the pattern of tissue distribution, the association with high-risk diseases, and the cell surface localization of this receptor, ROR2 has been identified as a potential high value target for therapeutic development. However, the recent discovery that ROR2 may function through non-kinase activities challenges this strategy and opens up opportunities to target this important molecule through alternative means.

Description: Tumor necrosis factor (TNF, cachexin or cachectin and formerly known as tumor necrosis factor-alpha) is a cytokine involved in systemic inflammation and is a member of a group of cytokines that stimulate the acute phase reaction. The receptor TNF-R1 is activated by both the membrane-bound and soluble trimeric forms of TNF-alpha, whereas the receptor TNF-R2 only responds to the membrane-bound form of TNF-alpha (MultimericTNF-alpha (Prod. No. AG-40B-0019). Since the MultimericTNF-alpha mimics the membrane-bound form (forms oligomers higher than trimer), it is the only TNF-alpha protein that can activate the TNF-R2. For TNF-R1 activation, either "normal" TNF-alpha or MultimericTNF-alpha can be used.

Description: Tumor necrosis factor (TNF, cachexin or cachectin and formerly known as tumor necrosis factor-alpha) is a cytokine involved in systemic inflammation and is a member of a group of cytokines that stimulate the acute phase reaction. The receptor TNF-R1 is activated by both the membrane-bound and soluble trimeric forms of TNF-alpha, whereas the receptor TNF-R2 only responds to the membrane-bound form of TNF-alpha (MultimericTNF-alpha (Prod. No. AG-40B-0019). Since the MultimericTNF-alpha mimics the membrane-bound form (forms oligomers higher than trimer), it is the only TNF-alpha protein that can activate the TNF-R2. For TNF-R1 activation, either "normal" TNF-alpha or MultimericTNF-alpha can be used.

Description: RANKL and RANK are members of the TNF superfamily of ligands and receptors that play an important role in the regulation of specific immunity and bone turnover. RANK (receptor) was originally identified as a dendritic cell-membrane protein, which, by interacting with RANKL, augments the ability of dendritic cells. These dendritic cells then stimulate naïve T-cell proliferation in a mixed lymphocyte reaction,promote the survival of RANK + T-cells, and regulate T-cell-dependent immune response. RANKL, which is expressed in a variety of cells,including osteoblasts, fibroblasts, activated T-cells and bone marrow stromal cells, is also capable of interacting with a decoy receptor called OPG. Binding of soluble OPG to sRANKL inhibits osteoclastogenesis by interrupting the signaling between stromal cells and osteoclastic progenitor cells, thereby leading to excess accumulation of bone and cartilage. Human RANKL is reactive on murine cells. Recombinant Human sRANK Ligand is a 22.1 kDa polypeptide comprised of the TNF-homologous region of RANKL and a N-terminal His-tag.

Description: RANKL and RANK are members of the TNF superfamily of ligands and receptors that play an important role in the regulation of specific immunity and bone turnover. RANK (receptor) was originally identified as a dendritic cell-membrane protein, which, by interacting with RANKL, augments the ability of dendritic cells. These dendritic cells then stimulate naïve T-cell proliferation in a mixed lymphocyte reaction,promote the survival of RANK + T-cells, and regulate T-cell-dependent immune response. RANKL, which is expressed in a variety of cells,including osteoblasts, fibroblasts, activated T-cells and bone marrow stromal cells, is also capable of interacting with a decoy receptor called OPG. Binding of soluble OPG to sRANKL inhibits osteoclastogenesis by interrupting the signaling between stromal cells and osteoclastic progenitor cells, thereby leading to excess accumulation of bone and cartilage. Human RANKL is reactive on murine cells. Recombinant Human sRANK Ligand is a 22.1 kDa polypeptide comprised of the TNF-homologous region of RANKL and a N-terminal His-tag.

Description: RANKL and RANK are members of the TNF superfamily of ligands and receptors that play an important role in the regulation of specific immunity and bone turnover. RANK (receptor) was originally identified as a dendritic-cell-membrane protein, which by interacting with RANKL augments the ability of dendritic cells to stimulate naïve T-cell proliferation in a mixed lymphocyte reaction, to promote the survival of RANK + T cells, and to regulate T-cell-dependent immune response. RANKL, which is expressed in a variety of cells including osteoblasts, fibroblasts, activated T-cells and bone marrow stromal cells, is also capable of interacting with a decoy receptor called OPG. Binding of soluble OPG to sRANKL inhibits osteoclastogenesis by interrupting the signaling between stromal cells and osteoclastic progenitor cells, thereby leading to excess accumulation of bone and cartilage. Recombinant human sRANKL is a 20.0 kDa polypeptide comprising the TNF homologous region of RANKL (176 amino acid residues).

Description: RANKL and RANK are members of the TNF superfamily of ligands and receptors that play an important role in the regulation of specific immunity and bone turnover. RANK (receptor) was originally identified as a dendritic-cell-membrane protein, which by interacting with RANKL augments the ability of dendritic cells to stimulate naïve T-cell proliferation in a mixed lymphocyte reaction, to promote the survival of RANK + T cells, and to regulate T-cell-dependent immune response. RANKL, which is expressed in a variety of cells including osteoblasts, fibroblasts, activated T-cells and bone marrow stromal cells, is also capable of interacting with a decoy receptor called OPG. Binding of soluble OPG to sRANKL inhibits osteoclastogenesis by interrupting the signaling between stromal cells and osteoclastic progenitor cells, thereby leading to excess accumulation of bone and cartilage. Recombinant human sRANKL is a 20.0 kDa polypeptide comprising the TNF homologous region of RANKL (176 amino acid residues).

Description: RANKL and RANK are members of the TNF superfamily of ligands and receptors that play an important role in the regulation of specific immunity and bone turnover. RANK (receptor) was originally identified as a dendritic-cell-membrane protein, which by interacting with RANKL augments the ability of dendritic cells to stimulate naïve T-cell proliferation in a mixed lymphocyte reaction, to promote the survival of RANK + T cells, and to regulate T-cell-dependent immune response. RANKL, which is expressed in a variety of cells including osteoblasts, fibroblasts, activated T-cells and bone marrow stromal cells, is also capable of interacting with a decoy receptor called OPG. Binding of soluble OPG to sRANKL inhibits osteoclastogenesis by interrupting the signaling between stromal cells and osteoclastic progenitor cells, thereby leading to excess accumulation of bone and cartilage. Recombinant human sRANKL is a 20.0 kDa polypeptide comprising the TNF homologous region of RANKL (176 amino acid residues).

Description: RANKL and RANK are members of the TNF superfamily of ligands and receptors that play an important role in the regulation of specific immunity and bone turnover. RANK (receptor) was originally identified as a dendritic-cell-membrane protein, which by interacting with RANKL augments the ability of dendritic cells to stimulate naïve T-cell proliferation in a mixed lymphocyte reaction, to promote the survival of RANK + T cells, and to regulate T-cell-dependent immune response. RANKL, which is expressed in a variety of cells including osteoblasts, fibroblasts, activated T-cells and bone marrow stromal cells, is also capable of interacting with a decoy receptor called OPG. Binding of soluble OPG to sRANKL inhibits osteoclastogenesis by interrupting the signaling between stromal cells and osteoclastic progenitor cells, thereby leading to excess accumulation of bone and cartilage. Recombinant human sRANKL is a 20.0 kDa polypeptide comprising the TNF homologous region of RANKL (176 amino acid residues).

Description: RANKL and RANK are members of the TNF superfamily of ligands and receptors that play an important role in the regulation of specific immunity and bone turnover. RANK (receptor) was originally identified as a dendritic-cell-membrane protein, which by interacting with RANKL augments the ability of dendritic cells to stimulate naïve T-cell proliferation in a mixed lymphocyte reaction, to promote the survival of RANK + T cells, and to regulate T-cell-dependent immune response. RANKL, which is expressed in a variety of cells including osteoblasts, fibroblasts, activated T-cells and bone marrow stromal cells, is also capable of interacting with a decoy receptor called OPG. Binding of soluble OPG to sRANKL inhibits osteoclastogenesis by interrupting the signaling between stromal cells and osteoclastic progenitor cells, thereby leading to excess accumulation of bone and cartilage. Recombinant murine sRANKL is a 19.4 kDa polypeptide comprising the TNF homologous region of RANKL (174 amino acid residues).

Description: RANKL and RANK are members of the TNF superfamily of ligands and receptors that play an important role in the regulation of specific immunity and bone turnover. RANK (receptor) was originally identified as a dendritic-cell-membrane protein, which by interacting with RANKL augments the ability of dendritic cells to stimulate naïve T-cell proliferation in a mixed lymphocyte reaction, to promote the survival of RANK + T cells, and to regulate T-cell-dependent immune response. RANKL, which is expressed in a variety of cells including osteoblasts, fibroblasts, activated T-cells and bone marrow stromal cells, is also capable of interacting with a decoy receptor called OPG. Binding of soluble OPG to sRANKL inhibits osteoclastogenesis by interrupting the signaling between stromal cells and osteoclastic progenitor cells, thereby leading to excess accumulation of bone and cartilage. Recombinant murine sRANKL is a 19.4 kDa polypeptide comprising the TNF homologous region of RANKL (174 amino acid residues).

Description: CD40, a member of the TNF receptor family, is a cell surface protein expressed on B cells, dendritic cells, monocytes, thymic epithelial cells and, at low levels, on T cells. Signaling though CD40 plays an important role in the proliferation and differentiation of B cells, and is critical for immunoglobulin (Ig) class switching. The membrane-anchored CD40-Ligand is expressed almost exclusively on activated CD4+ T lymphocytes. Failure to express CD40L leads to "immunodeficiency with hyper-IgM", a disease characterized by failure to produce IgG, IgA and IgE. The soluble form of CD40L is an 18kDa protein comprising the entire TNF homologous region of CD40L and is generated in vivo by an intracellular proteolytic processing of the full length CD40L. Recombinant murine CD40L is a soluble 16.4 kDa protein containing 149 amino acid residues comprising the receptor binding TNF-like domain of CD40L.

Description: CD40, a member of the TNF receptor family, is a cell surface protein expressed on B cells, dendritic cells, monocytes, thymic epithelial cells and, at low levels, on T cells. Signaling though CD40 plays an important role in the proliferation and differentiation of B cells, and is critical for immunoglobulin (Ig) class switching. The membrane-anchored CD40-Ligand is expressed almost exclusively on activated CD4+ T lymphocytes. Failure to express CD40L leads to "immunodeficiency with hyper-IgM", a disease characterized by failure to produce IgG, IgA and IgE. The soluble form of CD40L is an 18kDa protein comprising the entire TNF homologous region of CD40L and is generated in vivo by an intracellular proteolytic processing of the full length CD40L. Recombinant murine CD40L is a soluble 16.4 kDa protein containing 149 amino acid residues comprising the receptor binding TNF-like domain of CD40L.

Description: RANKL and RANK are members of the TNF superfamily of ligands and receptors that play an important role in the regulation of specific immunity and bone turnover. RANK (receptor) was originally identified as a dendritic-cell-membrane protein, which by interacting with RANKL augments the ability of dendritic cells to stimulate naïve T-cell proliferation in a mixed lymphocyte reaction, to promote the survival of RANK + T cells, and to regulate T-cell-dependent immune response. RANKL, which is expressed in a variety of cells including osteoblasts, fibroblasts, activated T-cells and bone marrow stromal cells, is also capable of interacting with a decoy receptor called OPG. Binding of soluble OPG to sRANKL inhibits osteoclastogenesis by interrupting the signaling between stromal cells and osteoclastic progenitor cells, thereby leading to excess accumulation of bone and cartilage. Recombinant rat sRANKL is a 19.4 kDa polypeptide comprising the TNF homologous region of RANKL (174 amino acid residues).

Description: RANKL and RANK are members of the TNF superfamily of ligands and receptors that play an important role in the regulation of specific immunity and bone turnover. RANK (receptor) was originally identified as a dendritic-cell-membrane protein, which by interacting with RANKL augments the ability of dendritic cells to stimulate naïve T-cell proliferation in a mixed lymphocyte reaction, to promote the survival of RANK + T cells, and to regulate T-cell-dependent immune response. RANKL, which is expressed in a variety of cells including osteoblasts, fibroblasts, activated T-cells and bone marrow stromal cells, is also capable of interacting with a decoy receptor called OPG. Binding of soluble OPG to sRANKL inhibits osteoclastogenesis by interrupting the signaling between stromal cells and osteoclastic progenitor cells, thereby leading to excess accumulation of bone and cartilage. Recombinant rat sRANKL is a 19.4 kDa polypeptide comprising the TNF homologous region of RANKL (174 amino acid residues).

Description: RANKL and RANK are members of the TNF superfamily of ligands and receptors that play an important role in the regulation of specific immunity and bone turnover. RANK (receptor) was originally identified as a dendritic-cell-membrane protein, which by interacting with RANKL augments the ability of dendritic cells to stimulate naïve T-cell proliferation in a mixed lymphocyte reaction, to promote the survival of RANK + T cells, and to regulate T-cell-dependent immune response. RANKL, which is expressed in a variety of cells including osteoblasts, fibroblasts, activated T-cells and bone marrow stromal cells, is also capable of interacting with a decoy receptor called OPG. Binding of soluble OPG to sRANKL inhibits osteoclastogenesis by interrupting the signaling between stromal cells and osteoclastic progenitor cells, thereby leading to excess accumulation of bone and cartilage. Recombinant murine sRANKL is a 19.4 kDa polypeptide comprising the TNF homologous region of RANKL (174 amino acid residues).

Description: RANKL and RANK are members of the TNF superfamily of ligands and receptors that play an important role in the regulation of specific immunity and bone turnover. RANK (receptor) was originally identified as a dendritic-cell-membrane protein, which by interacting with RANKL augments the ability of dendritic cells to stimulate naïve T-cell proliferation in a mixed lymphocyte reaction, to promote the survival of RANK + T cells, and to regulate T-cell-dependent immune response. RANKL, which is expressed in a variety of cells including osteoblasts, fibroblasts, activated T-cells and bone marrow stromal cells, is also capable of interacting with a decoy receptor called OPG. Binding of soluble OPG to sRANKL inhibits osteoclastogenesis by interrupting the signaling between stromal cells and osteoclastic progenitor cells, thereby leading to excess accumulation of bone and cartilage. Recombinant murine sRANKL is a 19.4 kDa polypeptide comprising the TNF homologous region of RANKL (174 amino acid residues).

Description: RANKL and RANK are members of the TNF superfamily of ligands and receptors that play an important role in the regulation of specific immunity and bone turnover. RANK (receptor) was originally identified as a dendritic cell-membrane protein, which, by interacting with RANKL, augments the ability of dendritic cells. These dendritic cells then stimulate naïve T-cell proliferation in a mixed lymphocyte reaction, promote the survival of RANK + T-cells, and regulate T-cell-dependent immune response. RANKL, which is expressed in a variety of cells, including osteoblasts, fibroblasts, activated T-cells and bone marrow stromal cells, is also capable of interacting with a decoy receptor called OPG. Binding of soluble OPG to sRANKL inhibits osteoclastogenesis by interrupting the signaling between stromal cells and osteoclastic progenitor cells, thereby leading to excess accumulation of bone and cartilage. Recombinant mouse sRANK Ligand is a 19.8 kDa polypeptide comprising the TNF-homologous region of RANKL (178 amino acid residues).

Description: RANKL and RANK are members of the TNF superfamily of ligands and receptors that play an important role in the regulation of specific immunity and bone turnover. RANK (receptor) was originally identified as a dendritic cell-membrane protein, which, by interacting with RANKL, augments the ability of dendritic cells. These dendritic cells then stimulate naïve T-cell proliferation in a mixed lymphocyte reaction, promote the survival of RANK + T-cells, and regulate T-cell-dependent immune response. RANKL, which is expressed in a variety of cells, including osteoblasts, fibroblasts, activated T-cells and bone marrow stromal cells, is also capable of interacting with a decoy receptor called OPG. Binding of soluble OPG to sRANKL inhibits osteoclastogenesis by interrupting the signaling between stromal cells and osteoclastic progenitor cells, thereby leading to excess accumulation of bone and cartilage. Recombinant mouse sRANK Ligand is a 19.8 kDa polypeptide comprising the TNF-homologous region of RANKL (178 amino acid residues).

Description: The Semaphorins are a large family of phylogenetically conserved proteins that play a pivotal role in maintaining homeostasis in the immune system. Twenty members of this family have been identified and categorized into eight subclasses based on sequence similarity and distinctive structural features. CD100, also known as Sema4D, is a 150 kDa transmembrane class IV semaphorin. Studies have shown that CD100 can induce monocyte migration, T-cell activation, and B-cell survival, as well as T/B cell and T/DC “cooperation”. The CD100 precursor contains 862 amino acids, including a 21 a.a. signal sequence, a 713 a.a. extracellular domain, a 21 a.a. transmembrane sequence, and a 107 a.a cytoplasmic region. The extracellular sequence contains several structural features, including a 479 a.a “sema” domain, a 79 a.a. Ig-like sequence, and a 52 a.a “Plexin-type repeat”. Recombinant soluble CD100 (sCD100) is a 78.9 kDa protein comprising the extracellular domain of CD100 (711 amino acids). SDS-PAGE analysis run under non-reducing conditions shows a mixture of disulfide linked dimer and monomer.

Description: The Semaphorins are a large family of phylogenetically conserved proteins that play a pivotal role in maintaining homeostasis in the immune system. Twenty members of this family have been identified and categorized into eight subclasses based on sequence similarity and distinctive structural features. CD100, also known as Sema4D, is a 150 kDa transmembrane class IV semaphorin. Studies have shown that CD100 can induce monocyte migration, T-cell activation, and B-cell survival, as well as T/B cell and T/DC “cooperation”. The CD100 precursor contains 862 amino acids, including a 21 a.a. signal sequence, a 713 a.a. extracellular domain, a 21 a.a. transmembrane sequence, and a 107 a.a cytoplasmic region. The extracellular sequence contains several structural features, including a 479 a.a “sema” domain, a 79 a.a. Ig-like sequence, and a 52 a.a “Plexin-type repeat”. Recombinant soluble CD100 (sCD100) is a 78.9 kDa protein comprising the extracellular domain of CD100 (711 amino acids). SDS-PAGE analysis run under non-reducing conditions shows a mixture of disulfide linked dimer and monomer.

Description: Fas and Fas Ligand (FasL) belong to the TNF superfamily and are type I and type II transmembrane proteins, respectively. Binding of FasL to Fas triggers apoptosis in Fas-bearing cells. The mechanism of apoptosis involves recruitment of pro-caspase 8 through an adaptor molecule called FADD followed by processing of the pro-enzyme to active forms. These active caspases then cleave various cellular substrates leading to the eventual cell death. sFasR is capable of inhibiting FasL-induced apoptosis by acting as a decoy receptor that serves as a sink for FasL. The full length Fas (receptor) is a 319 amino acid type I transmembrane protein, which contains a 157 amino acid extracellular domain, a 17 amino acid transmembrane domain, and 145 amino acid cytoplasmic domain. Recombinant human soluble Fas (sFas Receptor) is a 157 amino acid polypeptide (17.6 kDa) corresponding to the TNFR homologous cysteine rich extracellular domain Fas.

Description: Fas and Fas Ligand (FasL) belong to the TNF superfamily and are type I and type II transmembrane proteins, respectively. Binding of FasL to Fas triggers apoptosis in Fas-bearing cells. The mechanism of apoptosis involves recruitment of pro-caspase 8 through an adaptor molecule called FADD followed by processing of the pro-enzyme to active forms. These active caspases then cleave various cellular substrates leading to the eventual cell death. sFasR is capable of inhibiting FasL-induced apoptosis by acting as a decoy receptor that serves as a sink for FasL. The full length Fas (receptor) is a 319 amino acid type I transmembrane protein, which contains a 157 amino acid extracellular domain, a 17 amino acid transmembrane domain, and 145 amino acid cytoplasmic domain. Recombinant human soluble Fas (sFas Receptor) is a 157 amino acid polypeptide (17.6 kDa) corresponding to the TNFR homologous cysteine rich extracellular domain Fas.

Description: EBOV Virus-Like Particles, recombinant protein from Sf9 cells.

Description: TNF-related apoptosis-inducing ligand (TRAIL; Apo2L;CD253; TNFSF10) is a type II transmembrane protein of about 34kDa. Like most members of the tumor necrosis factor (TNF) superfamily of cytokines TRAIL can be cleaved at the cell surface by metalloproteases to form a soluble molecule. Active TRAIL forms trimers and specifically binds to five distinct receptors: TRAIL-R1 (DR4; Apo2;CD261; TNFRSF10A), TRAIL-R2 (DR5; KILLER; TRICK2A;TRICK2B; CD262; TNFRSF10B), TRAIL-R3 (DcR1;LIT; TRID; CD263; TNFRSF10C), TRAIL-R4 (DcR2; TRUNDD; CD264; TNFRSF10D), and osteoprotegerin (OPG; OCIF; TNFRSF11B). Trimerized TRAIL triggers apoptosis upon ligation of cell surface TRAIL-R1 and/or TRAIL-R2 by inducing the formation of the so-called multiprotein death-inducing signaling complex (DISC).

Description: TNF-related apoptosis-inducing ligand (TRAIL; Apo2L;CD253; TNFSF10) is a type II transmembrane protein of about 34kDa. Like most members of the tumor necrosis factor (TNF) superfamily of cytokines TRAIL can be cleaved at the cell surface by metalloproteases to form a soluble molecule. Active TRAIL forms trimers and specifically binds to five distinct receptors: TRAIL-R1 (DR4; Apo2;CD261; TNFRSF10A), TRAIL-R2 (DR5; KILLER; TRICK2A;TRICK2B; CD262; TNFRSF10B), TRAIL-R3 (DcR1;LIT; TRID; CD263; TNFRSF10C), TRAIL-R4 (DcR2; TRUNDD; CD264; TNFRSF10D), and osteoprotegerin (OPG; OCIF; TNFRSF11B). Trimerized TRAIL triggers apoptosis upon ligation of cell surface TRAIL-R1 and/or TRAIL-R2 by inducing the formation of the so-called multiprotein death-inducing signaling complex (DISC).

Description: RANKL and RANK are members of the TNF superfamily of ligands and receptors that play an important role in the regulation of specific immunity and bone turnover. RANK (receptor) was originally identified as a dendritic-cell-membrane protein, which by interacting with RANKL augments the ability of dendritic cells to stimulate naïve T cell proliferation and to promote the survival of RANK + T cells. RANK is also expressed in a variety of tissues including skeletal muscle, thymus, liver, colon, small intestine and adrenal gland. The RANK/RANKL interaction is important in the regulation of osteoclastogenesis and in dendritic-cell-mediated T cell immune responses. Impairments in RANK signaling have been implicated in the induction of expansile osteolysis and Paget disease of bone (PDB2). Recombinant human sRANK receptor is a 19.3 kDa polypeptide containing the TNFR homologous cysteine rich portion of the extracellular domain of RANK receptor (175 amino acid residues).

Description: RANKL and RANK are members of the TNF superfamily of ligands and receptors that play an important role in the regulation of specific immunity and bone turnover. RANK (receptor) was originally identified as a dendritic-cell-membrane protein, which by interacting with RANKL augments the ability of dendritic cells to stimulate naïve T cell proliferation and to promote the survival of RANK + T cells. RANK is also expressed in a variety of tissues including skeletal muscle, thymus, liver, colon, small intestine and adrenal gland. The RANK/RANKL interaction is important in the regulation of osteoclastogenesis and in dendritic-cell-mediated T cell immune responses. Impairments in RANK signaling have been implicated in the induction of expansile osteolysis and Paget disease of bone (PDB2). Recombinant human sRANK receptor is a 19.3 kDa polypeptide containing the TNFR homologous cysteine rich portion of the extracellular domain of RANK receptor (175 amino acid residues).