Other Proteins

Recombinant Human sDLL-1 (Legacy Tebubio ref. 167140-08). Human soluble DLL-1 comprises the extracellular signaling domain of DLL-1, a member of the Delta/Serrate/Lag-2 (DSL) family of single-pass type I trans-membrane proteins that serve as ligands for Notch receptors. It is expressed primarily in the heart, pancreas and epidermis. DLL-1 functions to specifically activate the Notch-1 and Notch-2 receptors. Proteolytic cleavage of DLL-1 produces a secreted extracellular domain, sDLL-1, that interacts with Notch receptors expressed on adjacent cells. Notch signaling plays an essential role in controlling cell fate decisions during prenatal development and postnatal stem cell renewal, and differentiation in many tissues. Human sDLL-1 blocks monocyte differentiation into macrophages, but permits differentiation into dendritic cells. In hematopoietic progenitor cells, hsDLL-1 suppresses differentiation into B-cells, while promoting differentiation into T-cells and NK cell precursors. In ce

Recombinant Human sDLL-1 (Legacy Tebubio ref. 167140-08). Human soluble DLL-1 comprises the extracellular signaling domain of DLL-1, a member of the Delta/Serrate/Lag-2 (DSL) family of single-pass type I trans-membrane proteins that serve as ligands for Notch receptors. It is expressed primarily in the heart, pancreas and epidermis. DLL-1 functions to specifically activate the Notch-1 and Notch-2 receptors. Proteolytic cleavage of DLL-1 produces a secreted extracellular domain, sDLL-1, that interacts with Notch receptors expressed on adjacent cells. Notch signaling plays an essential role in controlling cell fate decisions during prenatal development and postnatal stem cell renewal, and differentiation in many tissues. Human sDLL-1 blocks monocyte differentiation into macrophages, but permits differentiation into dendritic cells. In hematopoietic progenitor cells, hsDLL-1 suppresses differentiation into B-cells, while promoting differentiation into T-cells and NK cell precursors. In ce

Recombinant Human PAF-AH (Legacy Tebubio ref. 167140-10). Platelet Activating Factor (PAF) is a biologically active phospholipid, which exerts primarily proinflammatory activities by specifically signaling through G-protein-coupled receptors on platelets, neutrophils, and monocytes. Platelet Activating Factor Acetylhydrolase (PAF-AH) is a secreted protein that mediates PAF activity by specifically catalyzing hydrolysis of the "sn2" ester bond, resulting in the conversion of PAF to the biologically inactive lyso-PAF. PAF-AH can also interact with LDL particles to induce the hydrolysis of LDL-associated, oxidized phospholipids, generating lysophosphatidylcholine (lyso-PC) and other lysophospholipids. Recombinant Human PAF-AH is a 420 amino acid glycoprotein which migrates with an apparent molecular mass of 47-55 kDa by SDS-PAGE analysis. Recombinan Human PAF-AH has a calculated, theoretical molecular weight of 47.8 kDa.

Recombinant Human PAF-AH (Legacy Tebubio ref. 167140-10). Platelet Activating Factor (PAF) is a biologically active phospholipid, which exerts primarily proinflammatory activities by specifically signaling through G-protein-coupled receptors on platelets, neutrophils, and monocytes. Platelet Activating Factor Acetylhydrolase (PAF-AH) is a secreted protein that mediates PAF activity by specifically catalyzing hydrolysis of the "sn2" ester bond, resulting in the conversion of PAF to the biologically inactive lyso-PAF. PAF-AH can also interact with LDL particles to induce the hydrolysis of LDL-associated, oxidized phospholipids, generating lysophosphatidylcholine (lyso-PC) and other lysophospholipids. Recombinant Human PAF-AH is a 420 amino acid glycoprotein which migrates with an apparent molecular mass of 47-55 kDa by SDS-PAGE analysis. Recombinan Human PAF-AH has a calculated, theoretical molecular weight of 47.8 kDa.

Recombinant Human Fetuin A/AHSG (Legacy Tebubio ref. 167140-13). Fetuin A/AHSG is a human plasma glycoprotein belonging to the Cystatin family of protease inhibitors. It is highly expressed in embryonic cells and adult hepatocytes, and is expressed to a lesser extent in monocytes/macrophages. Fetuin A/AHSG is a major serum protein component that exerts various calcium-dependent physiological activities, and can mediate growth signaling in certain tumor cells. It also can act as a natural antagonist against specific TGF-beta and BMP signaling proteins, Recombinant Human Fetuin A is a heterodimeric protein containing a 282 amino acid A chain and a 27 amino acid B chain. The calculated molecular weight of Recombinant Human Fetuin A is 32.9 kDa. Due to glycosylation, recombinant Fetuin A migrates at an apparent molecular weight of 45-55 kDa by SDS-PAGE run under non-reducing conditions.

Recombinant Human Fetuin A/AHSG (Legacy Tebubio ref. 167140-13). Fetuin A/AHSG is a human plasma glycoprotein belonging to the Cystatin family of protease inhibitors. It is highly expressed in embryonic cells and adult hepatocytes, and is expressed to a lesser extent in monocytes/macrophages. Fetuin A/AHSG is a major serum protein component that exerts various calcium-dependent physiological activities, and can mediate growth signaling in certain tumor cells. It also can act as a natural antagonist against specific TGF-beta and BMP signaling proteins. Recombinant Human Fetuin A is a heterodimeric protein containing a 282 amino acid A chain and a 27 amino acid B chain. The calculated molecular weight of Recombinant Human Fetuin A is 32.9 kDa. Due to glycosylation, recombinant Fetuin A migrates at an apparent molecular weight of 45-55 kDa by SDS-PAGE run under non-reducing conditions.

Recombinant Human/Murine/Rat Thymosin-beta4 (Legacy Tebubio ref. 167140-14). Thymosin-beta4 is a small, actin-sequestering protein belonging to the thymosin-beta family that is found at high concentrations within the spleen, thymus, and peritoneal macrophages, where it is most notably responsible for the organization of cytoskeletal structure. In mammalian tissues, this protein acts as a modulator for the polymerization/depolymerization of actin through the formation of a 1:1 complex with the monomer G (globular)-actin, and inhibits actin's polymerization to form F (filamentous) actin, which together with other proteins binds microfilaments to construct the cytoskeleton. Commonly found at significant quantities within the brain, lungs, liver, kidneys, testes, and heart, thymosin-beta4 has also been shown to be synthesized by cells unrelated to the reticuloendothelial system, such as myoblasts and fibroblasts, and expressed at irregular levels by several hemopoietic cell lines, malignan

Recombinant Human/Murine/Rat Thymosin-beta4 (Legacy Tebubio ref. 167140-14). Thymosin-beta4 is a small, actin-sequestering protein belonging to the thymosin-beta family that is found at high concentrations within the spleen, thymus, and peritoneal macrophages, where it is most notably responsible for the organization of cytoskeletal structure. In mammalian tissues, this protein acts as a modulator for the polymerization/depolymerization of actin through the formation of a 1:1 complex with the monomer G (globular)-actin, and inhibits actin's polymerization to form F (filamentous) actin, which together with other proteins binds microfilaments to construct the cytoskeleton. Commonly found at significant quantities within the brain, lungs, liver, kidneys, testes, and heart, thymosin-beta4 has also been shown to be synthesized by cells unrelated to the reticuloendothelial system, such as myoblasts and fibroblasts, and expressed at irregular levels by several hemopoietic cell lines, malignan

Recombinant Human VCAM-1 (Legacy Tebubio ref. 167150-04). VCAM is a 110 kDa, cell surface integral membrane glycoprotein that belongs to the Ig-related superfamily of adhesion molecules. The primary function of VCAM-1 is the mediation of leukocyte-endothelial cell adhesion and signal transduction. VCAM-1 may play a vital role in the development of several diseases, including atherosclerosis and rheumatoid arthritis. The human VCAM-1 gene codes for a 715 amino acid transmembrane glycoprotein containing a 19 amino acid cytoplasmic domain, a 22 amino acid transmembrane domain, and a 674 amino acid extracellular domain. Recombinant Human VCAM-1 is a 74.1 kDa glycoprotein comprising the extracellular domain (674 amino acid residues) of VCAM-1. Monomeric glycosylated VCAM-1 migrates at an apparent molecular weight of approximately 90.0 kDa by SDS-PAGE analysis under reducing conditions.