Other Proteins

Recombinant Human Amphiregulin (Legacy Tebubio ref. 167100-55B). Amphiregulin is an EGF related growth factor that signals through the EGF/TGF-alpha receptor, and stimulates growth of keratinocytes, epithelial cells and some fibroblasts. Amphiregulin also inhibits the growth of certain carcinoma cell lines. Synthesized as a transmembrane protein, Amphiregulin's extracellular domain is proteolytically processed to release the mature protein. There are 6 conserved cysteine residues, which form 3 intramolecular disulfide bonds essential for biological activity. Recombinant Human Amphiregulin is an 11.3 kDa glycoprotein consisting of 98 amino acid residues.

Recombinant Human Amphiregulin (Legacy Tebubio ref. 167100-55B). Amphiregulin is an EGF related growth factor that signals through the EGF/TGF-alpha receptor, and stimulates growth of keratinocytes, epithelial cells and some fibroblasts. Amphiregulin also inhibits the growth of certain carcinoma cell lines. Synthesized as a transmembrane protein, Amphiregulin's extracellular domain is proteolytically processed to release the mature protein. There are 6 conserved cysteine residues, which form 3 intramolecular disulfide bonds essential for biological activity. Recombinant Human Amphiregulin is an 11.3 kDa glycoprotein consisting of 98 amino acid residues.

Recombinant Human PlGF-2 (Legacy Tebubio ref. 167100-56A). PlGF-2 is an angiogenic factor that belongs to the cysteine-knot superfamily of growth factors. PlGF-2 is expressed in umbilical vein endothelial cells and placenta. It signals through the VEGFR-1/FLT1 receptor, and stimulates endothelial cell proliferation and migration. PlGF-2 also signals through Neuropilin (NP-1), and can bind with high affinity to heparin. Recombinant Human PlGF-2 is a 34.6 kDa disulfide-linked homodimeric protein of two 152 amino acid polypeptide chains.

Recombinant Human PlGF-2 (Legacy Tebubio ref. 167100-56A). PlGF-2 is an angiogenic factor that belongs to the cysteine-knot superfamily of growth factors. PlGF-2 is expressed in umbilical vein endothelial cells and placenta. It signals through the VEGFR-1/FLT1 receptor, and stimulates endothelial cell proliferation and migration. PlGF-2 also signals through Neuropilin (NP-1), and can bind with high affinity to heparin. Recombinant Human PlGF-2 is a 34.6 kDa disulfide-linked homodimeric protein of two 152 amino acid polypeptide chains.

Recombinant Human PlGF-3 (Legacy Tebubio ref. 167100-57). PlGF-3 is an angiogenic factor that belongs to the cysteine-knot superfamily of growth factors. PlGF-3 is expressed exclusively in the placenta. It signals through the VEGFR-1/FLT1 receptor, and stimulates endothelial cell proliferation and migration. PlGF-3 lacks heparin binding affinity. Recombinant Human PlGF-3 is a 45.7 kDa disulfide-linked homodimeric protein of two 203 amino acid polypeptide chains.

Recombinant Human PlGF-3 (Legacy Tebubio ref. 167100-57). PlGF-3 is an angiogenic factor that belongs to the cysteine-knot superfamily of growth factors. PlGF-3 is expressed exclusively in the placenta. It signals through the VEGFR-1/FLT1 receptor, and stimulates endothelial cell proliferation and migration. PlGF-3 lacks heparin binding affinity. Recombinant Human PlGF-3 is a 45.7 kDa disulfide-linked homodimeric protein of two 203 amino acid polypeptide chains.

Recombinant Human Thrombomodulin (Legacy Tebubio ref. 167100-58). Thrombomodulin (TM, CD141, THBD) is an endothelial cell-expressed, transmembrane glycoprotein that can form a complex with the coagulation factor, thrombin. The thrombomodulin/thrombin complex converts protein C to its activated form, protein Ca, which in turn proteolytically cleaves and deactivates factor Va and factor VIIIa, two essential components of the coagulation mechanism. This inactivation reduces the generation of additional thrombin, and thereby effectively prevents continued coagulation. Reduced levels of thrombomodulin can correlate with the pathogenesis of certain cardiovascular diseases, such as atherosclerosis and thrombosis. However, the serum levels of the truncated circulating form of thrombomodulin are typically elevated during inflammation and in the presence of various inflammatory-related diseases. The thrombomodulin protein contains 575 amino acids, including an 18 a.a. signal sequence, a 497 a.a.

Recombinant Human Thrombomodulin (Legacy Tebubio ref. 167100-58). Thrombomodulin (TM, CD141, THBD) is an endothelial cell-expressed, transmembrane glycoprotein that can form a complex with the coagulation factor, thrombin. The thrombomodulin/thrombin complex converts protein C to its activated form, protein Ca, which in turn proteolytically cleaves and deactivates factor Va and factor VIIIa, two essential components of the coagulation mechanism. This inactivation reduces the generation of additional thrombin, and thereby effectively prevents continued coagulation. Reduced levels of thrombomodulin can correlate with the pathogenesis of certain cardiovascular diseases, such as atherosclerosis and thrombosis. However, the serum levels of the truncated circulating form of thrombomodulin are typically elevated during inflammation and in the presence of various inflammatory-related diseases. The thrombomodulin protein contains 575 amino acids, including an 18 a.a. signal sequence, a 497 a.a.

Recombinant Human HPRG (Legacy Tebubio ref. 167100-60). Histidine-proline-rich glycoprotein (HPRG), a member of the Cystatin structural superfamily, is an abundantly secreted multi-domain glycoprotein. Although the physiological function is largely unknown, HPRG potentially regulates physiological processes such as cell adhesion and migration, fibrinolysis, coagulation, complement activation, immune complex clearance and phagocytosis of apoptotic cells. HPRG can exert anti-angiogneic activity by stimulating apoptosis of endothelial cells. Recombinant Human HPRG is a 57.7 kDa glycoprotein containing 507 amino acid residues.