Other Proteins

Recombinant Human ANG-2 (Legacy Tebubio ref. 167130-07). ANG-2 binds to the endothelial cell specific receptor Tie-2, but, in contrast to ANG-1, does not induce tyrosine phosphorylation. Consequently, ANG-2 modulates ANG-1 activation of Tie-2 and, depending on the physiological and biochemical environment, can act either as an agonist or antagonist of Tie-2 induced angiogenesis. The signaling interactions of ANG-1, ANG-2 and Tie-2, along with less characterized ANG-3 and ANG-4, are required for embryonic and adult angiogenesis. Physiologically, ANG-1 and ANG-2 are associated with sprouting, tube formation, and structural integrity of newly formed blood vessels. Mature human ANG-2 is a secreted protein containing 480 amino acid residues. ANG-2 is composed of an alpha-helix-rich "coiled coil" N-terminal domain and fibrinogen-like C-terminal domain. ANG-2 exists predominantly in the form of a disulfide-linked dimer. Recombinant Human ANG-2 is a C-terminal histidine-tagged glycoprot

Recombinant Human ANG-2 (Legacy Tebubio ref. 167130-07). ANG-2 binds to the endothelial cell specific receptor Tie-2, but, in contrast to ANG-1, does not induce tyrosine phosphorylation. Consequently, ANG-2 modulates ANG-1 activation of Tie-2 and, depending on the physiological and biochemical environment, can act either as an agonist or antagonist of Tie-2 induced angiogenesis. The signaling interactions of ANG-1, ANG-2 and Tie-2, along with less characterized ANG-3 and ANG-4, are required for embryonic and adult angiogenesis. Physiologically, ANG-1 and ANG-2 are associated with sprouting, tube formation, and structural integrity of newly formed blood vessels. Mature human ANG-2 is a secreted protein containing 480 amino acid residues. ANG-2 is composed of an alpha-helix-rich "coiled coil" N-terminal domain and fibrinogen-like C-terminal domain. ANG-2 exists predominantly in the form of a disulfide-linked dimer. Recombinant Human ANG-2 is a C-terminal histidine-tagged glycoprot

Recombinant Human GLP-1 (Legacy Tebubio ref. 167130-08). GLP-1 is a proglucagon-derived peptide hormone secreted primarily by intestinal L cells during feeding. Its major physiological function is the stimulation of pancreatic beta cells to release appropriate amounts of insulin after glucose absorption. Other biological actions exhibited by GLP-1 include the suppression of plasma glucagon levels, inhibition of gastric motility, and promotion of satiety. The secretion of GLP-1 from intestinal L cells is stimulated by nutrients, hormones, and neural inputs. On the other hand, insulin has been reported to inhibit GLP-1 release, indicating that a feedback loop mechanism regulates GLP-1 secretion. In addition to being the precursor of GLP-1, proglucagon, whose primary structure is highly conserved in mammalian species, is also the precursor for other members of the glucagon family of peptide hormones, including glicentin-related pancreatic peptide (GRPP), glucagons, and GLP-2. Recombinant

Recombinant Human GLP-1 (Legacy Tebubio ref. 167130-08). GLP-1 is a proglucagon-derived peptide hormone secreted primarily by intestinal L cells during feeding. Its major physiological function is the stimulation of pancreatic beta cells to release appropriate amounts of insulin after glucose absorption. Other biological actions exhibited by GLP-1 include the suppression of plasma glucagon levels, inhibition of gastric motility, and promotion of satiety. The secretion of GLP-1 from intestinal L cells is stimulated by nutrients, hormones, and neural inputs. On the other hand, insulin has been reported to inhibit GLP-1 release, indicating that a feedback loop mechanism regulates GLP-1 secretion. In addition to being the precursor of GLP-1, proglucagon, whose primary structure is highly conserved in mammalian species, is also the precursor for other members of the glucagon family of peptide hormones, including glicentin-related pancreatic peptide (GRPP), glucagons, and GLP-2. Recombinant

Recombinant Human Relaxin-3 (Legacy Tebubio ref. 167130-10). Relaxin-3 is a secreted protein structurally related to insulin that is expressed primarily in the brain and central nervous system. Relaxin-3 has been identified as the ligand for the GPCR135 receptor, previously known as "somatostatin-like" or "angiotensin-like" peptide receptor, and has also been identified for binding specifically to the LGR7 receptor, previously identified as an "orphan" G protein-coupled receptor. Signaling by relaxin-3 through its target receptors is, most likely, part of a CNS processing system, activated in response to signaling by neuropeptides and other factors. Intracerebroventricular injections of relaxin-3 have been shown to cause a significant increase of food intake and body weight in Wistar rats. Recombinant Human Relaxin-3 is a 5.5 kDa, disulfide-linked, heterodimeric protein consisting of a 24 amino acid A-chain and a 27 amino acid B-chain.

Recombinant Human Relaxin-3 (Legacy Tebubio ref. 167130-10). Relaxin-3 is a secreted protein structurally related to insulin that is expressed primarily in the brain and central nervous system. Relaxin-3 has been identified as the ligand for the GPCR135 receptor, previously known as "somatostatin-like" or "angiotensin-like" peptide receptor, and has also been identified for binding specifically to the LGR7 receptor, previously identified as an "orphan" G protein-coupled receptor. Signaling by relaxin-3 through its target receptors is, most likely, part of a CNS processing system, activated in response to signaling by neuropeptides and other factors. Intracerebroventricular injections of relaxin-3 have been shown to cause a significant increase of food intake and body weight in Wistar rats. Recombinant Human Relaxin-3 is a 5.5 kDa, disulfide-linked, heterodimeric protein consisting of a 24 amino acid A-chain and a 27 amino acid B-chain.

Recombinant Human Maspin (Legacy Tebubio ref. 167130-12). Maspin (mammary serine protease inhibitor) is a non-inhibitory serpin that is expressed predominantly in normal mammary epithelial cells, but at significantly reduced levels or absent in most breast carcinomas. It has the ability to block the growth, invasiveness, and metastatic potential of breast and lung tumors. This anti-tumor activity is achieved, in part, by the contribution of maspin to the inhibition of angiogenesis, and its ability to preferentially promote apoptosis of tumor cells. Recombinant Human Maspin is a 42.1 kDa non-glycosylated protein containing 375 amino acid residues.

Recombinant Human Maspin (Legacy Tebubio ref. 167130-12). Maspin (mammary serine protease inhibitor) is a non-inhibitory serpin that is expressed predominantly in normal mammary epithelial cells, but at significantly reduced levels or absent in most breast carcinomas. It has the ability to block the growth, invasiveness, and metastatic potential of breast and lung tumors. This anti-tumor activity is achieved, in part, by the contribution of maspin to the inhibition of angiogenesis, and its ability to preferentially promote apoptosis of tumor cells. Recombinant Human Maspin is a 42.1 kDa non-glycosylated protein containing 375 amino acid residues.

Recombinant Human PEDF (Legacy Tebubio ref. 167130-13). PEDF is a noninhibitory serpin with neurotrophic, anti-angiogenic, and anti-tumorigenic properties. It is a 50 kDa glycoprotein produced and secreted in many tissues throughout the body. A major component of the anti-angiogenic action of PEDF is the induction of apoptosis in proliferating endothelial cells. In addition, PEDF is able to inhibit the activity of angiogenic factors, such as VEGF and FGF-2. The neuroprotective effects of PEDF are achieved through suppression of neuronal apoptosis induced by peroxide, glutamate, or other neurotoxins. The recent identification of a lipase-linked cell membrane receptor for PEDF (PEDF-R) that binds to PEDF with high affinity (1) should facilitate further elucidation of the underlying mechanisms of this pluripotent serpin. To date, PEDF-R is the only signaling receptor known to be used by a serpin family member. The unique range of PEDF activities implicate it as a potential therapeutic age