Catalog number: 223 - 91-229
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.
91-454
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.
91-457
Triggering Receptor Expressed on Myeloid Cells 1 (TREM-1) is a transmembrane protein with a single Ig-like domain. TREM-1 associates with the adapter protein, DAP12, to deliver an activating signal. TREM-1 is expressed on blood neutrophils and monocytes, and the expression is up-regulated by bacterial LPS. TREM-1 is expressed at high levels on neutrophils of patients with microbial sepsis and in mice with a TREM-1/Fc fusion protein protected mice against LPS-induced shock. Human TREM-1 shares 42% sequence homology with mouse TREM-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.