Other Proteins

Recombinant Human B7-H2 Fc (Legacy Tebubio ref. 167310-37). B7-H2, or inducible costimulator-ligand (ICOSL), is a transmembrane, co-stimulatory ligand of the T cell-specific surface receptor Inducible T cell costimulator (ICOS) that belongs to the B7 family and immunoglobulin superfamily, along with B7-1, B7-2, PD-L1 (B7-H1) and PD-L2. Whereas expression of inducible B7-1 and B7-2 is largely confined to specialized antigen-presenting cells of lymphoid tissues, B7-H2 expression occurs constitutively in hematopoietic and non-hematopoietic cells of peripheral organs. This striking difference in expression indicates that these three B7 ligands may enable temporally and spatially specific regulation of T cell response through non-competitive CD28 interaction; marking a unique function of B7-H2 in immune reactions of nonlymphoid organs in which T cells have migrated to peripheral tissues having only limited expression of B7-1 and B7-2. Expression of B7-H2 has been shown to be differentially

Recombinant Human B7-H2 Fc (Legacy Tebubio ref. 167310-37). B7-H2, or inducible costimulator-ligand (ICOSL), is a transmembrane, co-stimulatory ligand of the T cell-specific surface receptor Inducible T cell costimulator (ICOS) that belongs to the B7 family and immunoglobulin superfamily, along with B7-1, B7-2, PD-L1 (B7-H1) and PD-L2. Whereas expression of inducible B7-1 and B7-2 is largely confined to specialized antigen-presenting cells of lymphoid tissues, B7-H2 expression occurs constitutively in hematopoietic and non-hematopoietic cells of peripheral organs. This striking difference in expression indicates that these three B7 ligands may enable temporally and spatially specific regulation of T cell response through non-competitive CD28 interaction; marking a unique function of B7-H2 in immune reactions of nonlymphoid organs in which T cells have migrated to peripheral tissues having only limited expression of B7-1 and B7-2. Expression of B7-H2 has been shown to be differentially

Recombinant Human sCD8alpha (Legacy Tebubio ref. 167310-41). Cluster of differentiation 8 (CD8), a type I transmembrane glycoprotein of the immunoglobulin family of receptors, plays an integral role in signal transduction, and T cell differentiation and activation. CD8 is predominantly expressed on T cells as a disulfide-linked heterodimer of CD8alpha and CD8beta, where it functions as a co-receptor, along with T cell receptor (TCR), for major histocompatibilty complex class I (MHC-I) molecules; whereas its counterpart, CD4, acts as a co-receptor for MHC-II molecules. CD8 exists on the cell surface, where the CD8alpha chain is essential for binding to MHC-I. CD8 is also expressed on a subset of T cells, NK cells, monocytes and dendritic cells as disulfide-linked homodimers of CD8alpha. Ligation of MHC-I/peptide complexes presented by antigen-presenting cells (APCs), triggers the recruitment of lymphocyte-specific protein tyrosine kinase (Lck), which leads to lymphokine production, moti

Recombinant Human sCD8alpha (Legacy Tebubio ref. 167310-41). Cluster of differentiation 8 (CD8), a type I transmembrane glycoprotein of the immunoglobulin family of receptors, plays an integral role in signal transduction, and T cell differentiation and activation. CD8 is predominantly expressed on T cells as a disulfide-linked heterodimer of CD8alpha and CD8beta, where it functions as a co-receptor, along with T cell receptor (TCR), for major histocompatibilty complex class I (MHC-I) molecules; whereas its counterpart, CD4, acts as a co-receptor for MHC-II molecules. CD8 exists on the cell surface, where the CD8alpha chain is essential for binding to MHC-I. CD8 is also expressed on a subset of T cells, NK cells, monocytes and dendritic cells as disulfide-linked homodimers of CD8alpha. Ligation of MHC-I/peptide complexes presented by antigen-presenting cells (APCs), triggers the recruitment of lymphocyte-specific protein tyrosine kinase (Lck), which leads to lymphokine production, moti

Recombinant Human sCD42b/GP1Ba (Legacy Tebubio ref. 167310-48). CD42b, also known as GP1Ba (GP1B alpha, Glycoprotein 1Ba) is a single pass transmembrane glycoprotein that functions as the key ligand binding subunit of the GP1B platelet surface receptor. The association of CD42b/GP1Ba with GP1Bb (covalently) and platelet glycoproteins IX and V (non‐covalently) forms the von Willebrand factor receptor. The binding of von Willebrand factor (VWF) to its platelet receptor initiates the primary mechanism for the adhesion of platelets to a site of vascular injury and subsequent platelet activation. Additionally, the cytoplasmic (C‐terminal) domain of CD42b/GP1Ba can bind and activate signal transduction molecules, including 14‐3‐3zeta and beta‐filamin. Mutations in von Willebrand factor and to a lesser extent, CD42b/GP1Ba, that affect the binding of VWF to the GP1B receptor are the primary cause of the hereditary bleeding disorder known as Type 2 von Willebrand disease (VWD). Mutations in the

Recombinant Human sCD42b/GP1Ba (Legacy Tebubio ref. 167310-48). CD42b, also known as GP1Ba (GP1B alpha, Glycoprotein 1Ba) is a single pass transmembrane glycoprotein that functions as the key ligand binding subunit of the GP1B platelet surface receptor. The association of CD42b/GP1Ba with GP1Bb (covalently) and platelet glycoproteins IX and V (non‐covalently) forms the von Willebrand factor receptor. The binding of von Willebrand factor (VWF) to its platelet receptor initiates the primary mechanism for the adhesion of platelets to a site of vascular injury and subsequent platelet activation. Additionally, the cytoplasmic (C‐terminal) domain of CD42b/GP1Ba can bind and activate signal transduction molecules, including 14‐3‐3zeta and beta‐filamin. Mutations in von Willebrand factor and to a lesser extent, CD42b/GP1Ba, that affect the binding of VWF to the GP1B receptor are the primary cause of the hereditary bleeding disorder known as Type 2 von Willebrand disease (VWD). Mutations in the

Recombinant Murine M-CSF (Legacy Tebubio ref. 167315-02). M-CSF is a potent hematopoietic factor produced by a variety of cells, including lymphocytes, monocytes, fibroblasts, endothelial cells, myoblasts and osteoblasts. It is a key regulator of cellular proliferation, differentiation, and survival for blood monocytes, tissue macrophages, and their respective progenitor cells. M-CSF has been shown to play important roles in modulating dermal thickness and fertility. M-CSF is clinically used in the treatment of infection, malignancies and atherosclerosis. It facilitates hematopoietic recovery after bone marrow transplantation. Human M-CSF is reactive in murine systems, but the murine molecule exhibits no activity on human cells. Recombinant Murine M-CSF is a 36.4 kDa homodimeric protein consisting of two 156 amino acid polypeptide subunits.

Recombinant Murine M-CSF (Legacy Tebubio ref. 167315-02). M-CSF is a potent hematopoietic factor produced by a variety of cells, including lymphocytes, monocytes, fibroblasts, endothelial cells, myoblasts and osteoblasts. It is a key regulator of cellular proliferation, differentiation, and survival for blood monocytes, tissue macrophages, and their respective progenitor cells. M-CSF has been shown to play important roles in modulating dermal thickness and fertility. M-CSF is clinically used in the treatment of infection, malignancies and atherosclerosis. It facilitates hematopoietic recovery after bone marrow transplantation. Human M-CSF is reactive in murine systems, but the murine molecule exhibits no activity on human cells. Recombinant Murine M-CSF is a 36.4 kDa homodimeric protein consisting of two 156 amino acid polypeptide subunits.

Recombinant Murine GM-CSF (Legacy Tebubio ref. 167315-03). GM-CSF is a hematopoietic growth factor that stimulates the development of neutrophils and macrophages, and promotes the proliferation and development of early erythroid megakaryocytic and eosinophilic progenitor cells. It is produced in endothelial cells, monocytes, fibroblasts and T-lymphocytes. GM-CSF inhibits neutrophil migration and enhances the functional activity of the mature end-cells. The human and murine molecules are species-specific and exhibit no cross-species reactivity. Recombinant Murine GM-CSF is a 14.2 kDa globular protein consisting of 125 amino acid residues.