Other Proteins

Recombinant Human sCD28 Fc (Legacy Tebubio ref. 167310-34). CTLA-4 and CD28 are receptors of the immunoglobulin superfamily that are expressed, along with the transmembrane glycoproteins B7-1 and B7-2, by antigen-presenting cells, and with these ligands constitute crucial co-stimulatory pathways for T and B cell regulatory responses. It is through engagement with CD28 and CTLA-4 that the B7 family ligands B7-1 and B7-2 play principal roles in immunity by activating immune response and maintaining immune tolerance. Co-stimulatory signals generated by B7-1 and B7-2 interactions with CD28 serve to stimulate T cell activation and prevent anergy through the amplification of T cell receptor (TCR) signaling. In contrast, interactions of the ligands with CTLA-4 serves to maintain T cell homeostasis and self-tolerance through the disruption of stimulatory signaling from B7 isoform-bound CD28 complexes, and by inducing powerful inhibitory signals in T cells. CTLA-4, like B7-1, is only poorly exp

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.