Other Proteins

Recombinant Human ICAM-2 Fc (Legacy Tebubio ref. 167150-22). Intracellular adhesion molecule‐2 (ICAM‐2), also known as CD102, is a member of the Ig superfamily of calcium‐independent transmembrane glycoproteins. ICAM‐2 is a ligand for the β2‐integrins, lymphocyte function‐associated antigen‐1 (LFA‐1) and Mac‐1. Constitutively expressed on all vascular endothelial cells and at endothelial cell junctions, it is also expressed at low levels on most leukocytes. As a cell surface adhesion molecule, it is involved in leukocyte recruitment and mediates leukocyte binding. Through interaction with LFA‐1, ICAM‐2 activates the PI3K/AKT pathway which leads to inhibition of TNF‐α and Fas‐mediated apoptosis. ICAM‐2 is highly expressed in lymphomas and it is postulated to be involved in lymphocyte recirculation and trafficking. T cell crawling and diapedesis across the blood‐brain barrier has been shown to be regulated by ICAM‐2 via ligation of LFA‐1 as well as neutrophil crawling and IL‐1ß‐stimulate

Recombinant Human ICAM-2 Fc (Legacy Tebubio ref. 167150-22). Intracellular adhesion molecule‐2 (ICAM‐2), also known as CD102, is a member of the Ig superfamily of calcium‐independent transmembrane glycoproteins. ICAM‐2 is a ligand for the β2‐integrins, lymphocyte function‐associated antigen‐1 (LFA‐1) and Mac‐1. Constitutively expressed on all vascular endothelial cells and at endothelial cell junctions, it is also expressed at low levels on most leukocytes. As a cell surface adhesion molecule, it is involved in leukocyte recruitment and mediates leukocyte binding. Through interaction with LFA‐1, ICAM‐2 activates the PI3K/AKT pathway which leads to inhibition of TNF‐α and Fas‐mediated apoptosis. ICAM‐2 is highly expressed in lymphomas and it is postulated to be involved in lymphocyte recirculation and trafficking. T cell crawling and diapedesis across the blood‐brain barrier has been shown to be regulated by ICAM‐2 via ligation of LFA‐1 as well as neutrophil crawling and IL‐1ß‐stimulate

Recombinant Human ICAM‐3 Fc (Legacy Tebubio ref. 167150-23). Intracellular adhesion molecule‐3 (ICAM‐3), also known as CD50, is a member of the Ig superfamily of calcium-independent transmembrane glycoproteins. ICAM‐3 is a ligand for the beta2‐integrins, lymphocyte function associated antigen‐1 (LFA‐1/alphaLbeta2) and alphaDbeta2, as well as DC‐specific ICAM‐3 grabbing nonintegrin (DC‐SIGN), a c-type lectin receptor. ICAM‐3 is a cell surface adhesion molecule expressed by resting T cells and antigen presenting cells (APCs). ICAM‐3/LFA‐1 binding mediates adhesion between APCs and T cells and induces co-stimulatory signals important for immune response (e.g., Ca2+mobilization and tyrosine phosphorylation). Binding with DC‐SIGN, expressed by dendritic cells (DC), facilitates DC‐T cell binding, which leads to T cell activation and proliferation. ICAM‐3 plays a dual role in apoptotic cell clearance of leukocytes by promoting chemoattraction of macrophages to sites of cell death and by media

Recombinant Human ICAM‐3 Fc (Legacy Tebubio ref. 167150-23). Intracellular adhesion molecule‐3 (ICAM‐3), also known as CD50, is a member of the Ig superfamily of calcium-independent transmembrane glycoproteins. ICAM‐3 is a ligand for the beta2‐integrins, lymphocyte function associated antigen‐1 (LFA‐1/alphaLbeta2) and alphaDbeta2, as well as DC‐specific ICAM‐3 grabbing nonintegrin (DC‐SIGN), a c-type lectin receptor. ICAM‐3 is a cell surface adhesion molecule expressed by resting T cells and antigen presenting cells (APCs). ICAM‐3/LFA‐1 binding mediates adhesion between APCs and T cells and induces co-stimulatory signals important for immune response (e.g., Ca2+mobilization and tyrosine phosphorylation). Binding with DC‐SIGN, expressed by dendritic cells (DC), facilitates DC‐T cell binding, which leads to T cell activation and proliferation. ICAM‐3 plays a dual role in apoptotic cell clearance of leukocytes by promoting chemoattraction of macrophages to sites of cell death and by media

Recombinant Human TLR-3 (Legacy Tebubio ref. 167160-01). TLR-3 is a single-pass type I receptor that binds to and signals the presence of microbial pathogens and double stranded RNA (dsRNA) viruses. Signaling through TLR-3 can promote the NF-kappaB pathway to initiate innate and adaptive immune responses to bacterial and viral infections, as well as the p53 pathway to trigger apoptosis in cells infected with dsRNA viruses. TLR-3 belongs to a family of structurally-related toll-like receptors (TLRs) containing an N-terminal domain rich in leucine repeats, and a C-terminal intracellular Toll/interleukin (IL)-1 (TIL) domain. TLR-3 is expressed primarily in dendritic cells of the placenta and pancreas where it can reside on both sides of the plasma membrane, and in the endosomal compartment of the cells. Recombinant Human TLR-3 is 77.4 kDa glycoprotein containing 681 residues which comprise the TLR-3 extracellular domain.

Recombinant Human TLR-3 (Legacy Tebubio ref. 167160-01). TLR-3 is a single-pass type I receptor that binds to and signals the presence of microbial pathogens and double stranded RNA (dsRNA) viruses. Signaling through TLR-3 can promote the NF-kappaB pathway to initiate innate and adaptive immune responses to bacterial and viral infections, as well as the p53 pathway to trigger apoptosis in cells infected with dsRNA viruses. TLR-3 belongs to a family of structurally-related toll-like receptors (TLRs) containing an N-terminal domain rich in leucine repeats, and a C-terminal intracellular Toll/interleukin (IL)-1 (TIL) domain. TLR-3 is expressed primarily in dendritic cells of the placenta and pancreas where it can reside on both sides of the plasma membrane, and in the endosomal compartment of the cells. Recombinant Human TLR-3 is 77.4 kDa glycoprotein containing 681 residues which comprise the TLR-3 extracellular domain.

Recombinant Human FGFR1a (IIIc) Fc (Legacy Tebubio ref. 167160-02). The FGF family plays a central role during prenatal development and postnatal growth, and the regeneration of a variety of tissues, by promoting cellular proliferation and differentiation. The FGF ligands bind to a family of type I transmembrane tyrosine kinase receptors, which leads to dimerization and activation by sequential autophosphorylation of specific tyrosine residues. Four genes encoding structurally related FGF receptors (FGFR-1 to -4) are known. Alternative splicing of the mRNAs generates numerous forms of FGFR-1 to -3. Alternate forms of FGF receptors can exhibit different specificities with respect to ligand binding. For example, the form designated as FGFR1a (IIc) interacts predominantly with FGF-acidic (FGF1) and FGF-basic (FGF2). A frequent splicing event involving FGFR-1 and -2 results in receptors containing all three Ig domains, referred to as the alpha isoform, or only IgII and IgIII, referred to a

Recombinant Human FGFR1a (IIIc) Fc (Legacy Tebubio ref. 167160-02). The FGF family plays a central role during prenatal development and postnatal growth, and the regeneration of a variety of tissues, by promoting cellular proliferation and differentiation. The FGF ligands bind to a family of type I transmembrane tyrosine kinase receptors, which leads to dimerization and activation by sequential autophosphorylation of specific tyrosine residues. Four genes encoding structurally related FGF receptors (FGFR-1 to -4) are known. Alternative splicing of the mRNAs generates numerous forms of FGFR-1 to -3. Alternate forms of FGF receptors can exhibit different specificities with respect to ligand binding. For example, the form designated as FGFR1a (IIc) interacts predominantly with FGF-acidic (FGF1) and FGF-basic (FGF2). A frequent splicing event involving FGFR-1 and -2 results in receptors containing all three Ig domains, referred to as the alpha isoform, or only IgII and IgIII, referred to a

Recombinant Human FGFR2a (IIIc) Fc (Legacy Tebubio ref. 167160-03). The FGF family plays a central role during prenatal development and postnatal growth, and the regeneration of a variety of tissues, by promoting cellular proliferation and differentiation. The FGF ligands bind to a family of type I transmembrane tyrosine kinase receptors, which leads to dimerization and activation by sequential autophosphorylation of specific tyrosine residues. Four genes encoding structurally related FGF receptors (FGFR-1 to -4) are known. Alternative splicing of the mRNAs generates numerous forms of FGFR-1 to -3. Alternate forms of FGF receptors can exhibit different specificities with respect to ligand binding. For example, the form designated as FGFR1a (IIc) interacts predominantly with FGF-acidic (FGF1) and FGF-basic (FGF2). A frequent splicing event involving FGFR-1 and -2 results in receptors containing all three Ig domains, referred to as the alpha isoform, or only IgII and IgIII, referred to a