Catalog number: 223 - 91-457
Product Category: Business & Industrial > Science & Laboratory
Size: 0.05 mg
40-123-02mg
GLP-1 is a proglucagon-derived peptide hormone secreted primarily by intestinal L cells during feeding. Its major physiological function is stimulation of pancreatic β-cells to release appropriate amounts of insulin after glucose absorption. Other biological actions exhibited by GLP-1 include suppression of plasma glucagons 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 human GLP-1 is a 3.3 kDa consisting of 31 amino acid residues.
40-123-10mg
GLP-1 is a proglucagon-derived peptide hormone secreted primarily by intestinal L cells during feeding. Its major physiological function is stimulation of pancreatic β-cells to release appropriate amounts of insulin after glucose absorption. Other biological actions exhibited by GLP-1 include suppression of plasma glucagons 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 human GLP-1 is a 3.3 kDa consisting of 31 amino acid residues.
40-126-0002mg
Plasminogen Activator Inhibitor-1 (PAI-1, Serpin E1) is a member of the serpin family of serine protease inhibitors, and is the primary inhibitor of urokinase and tissue plasminogen activator (tPA). PAI-1 is expressed predominantly in adipose, liver and vascular tissues, and is also produced by certain tumor cells. Elevated levels of PAI-1 are associated with obesity, diabetes and cardiovascular disease, and increased production of PAI-1 is induced by various obesity related factors such as TNFα, glucose, insulin, and very-low-density lipoprotein. The obesity related elevation of PAI-1 levels along with the consequential deficiency in plasminogen activators can lead directly to increased risk of thrombosis and other coronary diseases. Accordingly, PAI-1 has been implicated as an important molecular link between obesity and coronary disease. PAI-1 can also specifically bind vitronectin (VTN) to form a stable active complex with an increased circulatory half life relative to free PAI-1. Recombinant human PAI-1 is a 42.7 kDa protein containing 379 amino acid residues.
91-447
Neurexophilin-1 (NXPH1) is a member of Neurexophilin family. NXPH1 consist of 271 amino acis. It contains a 21 amino acid signal peptide, 86 amino acid propeptide, and 164 amino acid mature protein. NXPH1 is expressed in subpopulations of neurons within the cerebral cortex, cerebellum and olfactory bulb that are thought to be inhibitory interneurons. In humans, NXPH2 and NXPH3 are most similar to NXPH1, sharing 84% and 64% aa identity within the mature region, respectively. By contrast, NXPH4 dost not bind a-neurexins. Genetic deletion of NXPH1 or NXPH3 produces no anatomical effect.
91-454
TIE-1 (Tyrosine Kinase with Ig and EGF Homology domains 1) and TIE-2/Tek comprise a receptor tyrosine kinase (RTK) subfamily. These receptors are expressed on endothelial and hematopoietic progenitor cells and play critical roles in angiogenesis, vasculogenesis and hematopoiesis. Human TIE-1 cDNA encodes a 1124 amino acid (aa) residue precursor protein with an 18aa signal peptide, a 727 aa extracellular domain and a 354 aa cytoplasmic domain. so far, two ligands have been described for TIE-2 [angiopoietin-1 (Ang1) and angiopoietin-2 (Ang2)], but no ligand was found for TIE-1.
91-473
Kininogen-1 is a secreted protein which contains three cystatin domains. There are two alternatively spliced forms, designated as the high molecular weight (HMW) and low MW (LMW) forms. Kininogen-1 plays a critical role in blood coagulation and inflammatory response. Kininogens are inhibitors of thiol proteases. Kininogen-1 participates in blood coagulation by helping to position optimally prekallikrein and factor XI next to factor XII, also inhibits the thrombin- and plasmin-induced aggregation of thrombocytes. The active peptide bradykinin that is released from Kininogen-1 shows a variety of physiological effects: influence in smooth muscle contraction, induction of hypotension, natriuresis and diuresis, decrease in blood glucose level. It is a mediator of inflammation and causes increase in vascular permeability, stimulation of nociceptors release of other mediators of inflammation. It has a cardioprotective effect. LMW-kininogen inhibits the aggregation of thrombocytes and doesn’t involved in blood clotting.