Other Proteins

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.

Recombinant Human EGF-L7 (Legacy Tebubio ref. 167100-61). EGF-L7 (Epidermal growth factor-like protein 7, Multiple EGF-like domains protein 7, VE-statin) is a multi-domain protein containing two EGF-like domains and one EMI domain. It is expressed almost exclusively in endothelial cells and functions to promote normal development of the vascular system, particularly tubulogenesis. EGF-L7 is capable of antagonistic binding to Notch receptors, resulting in the inhibition of Notch signaling in HUVEC and neural stem cells. In research models inducing hypoxia and subsequent reoxygenation (H/R), EGF-L7 can inhibit ICAM-1 expression and enhance the inhibition of NF-kappaB activation. Additionally, EGF-L7 can chemoattract endothelial cells and bind to the extracellular matrix. The overexpression of EGF-L7 is observed in various cancers, and is generally correlated with increased metastasis and a poor prognosis. Recombinant Human EGF-L7 is a 27.4 kDa protein containing 251 amino acid residues.

Recombinant Human EGF-L7 (Legacy Tebubio ref. 167100-61). EGF-L7 (Epidermal growth factor-like protein 7, Multiple EGF-like domains protein 7, VE-statin) is a multi-domain protein containing two EGF-like domains and one EMI domain. It is expressed almost exclusively in endothelial cells and functions to promote normal development of the vascular system, particularly tubulogenesis. EGF-L7 is capable of antagonistic binding to Notch receptors, resulting in the inhibition of Notch signaling in HUVEC and neural stem cells. In research models inducing hypoxia and subsequent reoxygenation (H/R), EGF-L7 can inhibit ICAM-1 expression and enhance the inhibition of NF-kappaB activation. Additionally, EGF-L7 can chemoattract endothelial cells and bind to the extracellular matrix. The overexpression of EGF-L7 is observed in various cancers, and is generally correlated with increased metastasis and a poor prognosis. Recombinant Human EGF-L7 is a 27.4 kDa protein containing 251 amino acid residues.

Recombinant Human MPF (Legacy Tebubio ref. 167100-62). Originally identified as a differentiation antigen of mesotheliomas, ovarian cystadenocarcinomas, and pancreatic adenocarcinomas, Mesothelin is a glycosylphosphatidylinositol (GPI)-anchored, cell-surface glycoprotein predominantly secreted by cells of the mesothelium. Although Mesothelin is expressed at restricted levels by normal mesothelial cells of the pleural,pericardial, and peritoneal membranes, aberrant expression has been documented in the aforementioned cancers, as well as in endometriod uterine adenocarcinomas and squamous cell carcinomas of the esophagus, stomach, lung, and cervix. Proteolytic cleavage of Mesothelin yields a soluble, polypeptide fragment designated megakaryocyte potentiating factor (MPF) based on its ability to stimulate megakaryocyte colony-forming activity of murine interleukin-3 in murine bone marrow cell cultures. Originally isolated from the HPC-Y5 pancreatic cell line, MPF has been suggested to pla

Recombinant Human MPF (Legacy Tebubio ref. 167100-62). Originally identified as a differentiation antigen of mesotheliomas, ovarian cystadenocarcinomas, and pancreatic adenocarcinomas, Mesothelin is a glycosylphosphatidylinositol (GPI)-anchored, cell-surface glycoprotein predominantly secreted by cells of the mesothelium. Although Mesothelin is expressed at restricted levels by normal mesothelial cells of the pleural,pericardial, and peritoneal membranes, aberrant expression has been documented in the aforementioned cancers, as well as in endometriod uterine adenocarcinomas and squamous cell carcinomas of the esophagus, stomach, lung, and cervix. Proteolytic cleavage of Mesothelin yields a soluble, polypeptide fragment designated megakaryocyte potentiating factor (MPF) based on its ability to stimulate megakaryocyte colony-forming activity of murine interleukin-3 in murine bone marrow cell cultures. Originally isolated from the HPC-Y5 pancreatic cell line, MPF has been suggested to pla

Recombinant Human Mesothelin (Legacy Tebubio ref. 167100-63). Originally identified as a differentiation antigen of mesotheliomas, ovarian cystadenocarcinomas, and pancreatic adenocarcinomas, mesothelin is a glycosylphosphatidylinositol (GPI)-anchored, cell-surface glycoprotein predominantly secreted by cells of the mesothelium. Although mesothelin is expressed at restricted levels by normal mesothelial cells of the pleural, pericardial, and peritoneal membranes, aberrant expression has been documented in the aforementioned cancers, as well as in endometrioid uterine adenocarcinomas and squamous cell carcinomas of the esophagus, stomach, lung, and cervix. Proteolytic cleavage of mesothelin yields a soluble, polypeptide fragment-designated megakaryocyte-potentiating factor (MPF) based on its ability to stimulate megakaryocyte colony-forming activity of murine IL-3 in murine bone marrow cell cultures. Originally isolated from the HPC-Y5 pancreatic cell line, MPF has been suggested to pla

Recombinant Human Mesothelin (Legacy Tebubio ref. 167100-63). Originally identified as a differentiation antigen of mesotheliomas, ovarian cystadenocarcinomas, and pancreatic adenocarcinomas, mesothelin is a glycosylphosphatidylinositol (GPI)-anchored, cell-surface glycoprotein predominantly secreted by cells of the mesothelium. Although mesothelin is expressed at restricted levels by normal mesothelial cells of the pleural, pericardial, and peritoneal membranes, aberrant expression has been documented in the aforementioned cancers, as well as in endometrioid uterine adenocarcinomas and squamous cell carcinomas of the esophagus, stomach, lung, and cervix. Proteolytic cleavage of mesothelin yields a soluble, polypeptide fragment-designated megakaryocyte-potentiating factor (MPF) based on its ability to stimulate megakaryocyte colony-forming activity of murine IL-3 in murine bone marrow cell cultures. Originally isolated from the HPC-Y5 pancreatic cell line, MPF has been suggested to pla

Recombinant Human EPO (Legacy Tebubio ref. 167100-64). Erythropoietin (EPO) is a glycoprotein hormone that is principally known for its role in erythropoiesis, where it is responsible for stimulating proliferation and differentiation of erythroid progenitor cells. The differentiation of CFU-E (Colony Forming Unit-Erythroid) cells into erythrocytes can only be accomplished in the presence of EPO. Physiological levels of EPO in adult mammals are maintained primarily by the kidneys, whereas levels in fetal or neonatal mammals are maintained by the liver. EPO also can exert various non-hematopoietic activities, including vascularization and proliferation of smooth muscle, neural protection during hypoxia, and stimulation of certain B cells. PeproTech's Human EPO contains 166 amino acid residues and has a calculated molecular weight of approximately 18.4 kDa. As a result of glycosylation, Recombinant Human EPO migrates with an apparent molecular mass of 37.0 kDa by SDS-PAGE gel, under reduc

Recombinant Human EPO (Legacy Tebubio ref. 167100-64). Erythropoietin (EPO) is a glycoprotein hormone that is principally known for its role in erythropoiesis, where it is responsible for stimulating proliferation and differentiation of erythroid progenitor cells. The differentiation of CFU-E (Colony Forming Unit-Erythroid) cells into erythrocytes can only be accomplished in the presence of EPO. Physiological levels of EPO in adult mammals are maintained primarily by the kidneys, whereas levels in fetal or neonatal mammals are maintained by the liver. EPO also can exert various non-hematopoietic activities, including vascularization and proliferation of smooth muscle, neural protection during hypoxia, and stimulation of certain B cells. PeproTech's Human EPO contains 166 amino acid residues and has a calculated molecular weight of approximately 18.4 kDa. As a result of glycosylation, Recombinant Human EPO migrates with an apparent molecular mass of 37.0 kDa by SDS-PAGE gel, under reduc