| Description | Syntide 2 (TFA), a Ca2+- and calmodulin (CaM)-dependent protein kinase II (CaMKII) substrate peptide, selectively inhibits the gibberellin (GA) response, leaving constitutive and abscisic acid-regulated events unaffected[1] | Angiotensin I/II 1-5 TFA is a peptide that contains the amino acids 1-5, which is converted from Angiotensin I/II. Angiotensin I is formed by the action of renin on angiotensinogen. Angiotensin II is produced from angiotensin I. Angiotensin II has been investigated for the treatment, basic science, Angiotensin I/II 1-5 TFA is a peptide that contains the amino acids 1-5, which is converted from Angiotensin I/II. Angiotensin I is formed by the action of renin on angiotensinogen. Angiotensin II is produced from angiotensin I. Angiotensin II has been investigated for the treatment, basic science, and diagnostic of Hypertension, Renin Angiotensin System, and Idiopathic Membranous Nephropathy[1][2][3]... Read More | Bradykinin is an effective endothelium-dependent vasodilator that can lower blood pressure. Bradykinin can induce contraction of bronchial and intestinal non-vascular smooth muscle, increase vascular permeability, and participate in the mechanism of pain[1][2][3][4][5] | GIP (Gastric inhibitory polypeptide) (mouse) is a gastrointestinal hormone that is secreted by the intestinal K cells, and also expressed in and secreted from pancreatic islets. GIP (mouse) promotes insulin secretion from pancreatic β cells via the G-protein-coupled GIP receptor (GIPR). GIP (GIP (Gastric inhibitory polypeptide) (mouse) is a gastrointestinal hormone that is secreted by the intestinal K cells, and also expressed in and secreted from pancreatic islets. GIP (mouse) promotes insulin secretion from pancreatic β cells via the G-protein-coupled GIP receptor (GIPR). GIP (mouse) promotes pancreatic β cell proliferation and inhibits apoptosis. GIP (mouse) also exerts direct lipogenic effects on adipose tissue[1][2][3]... Read More | L-Lactate dehydrogenase, Microorganism (LAD) is a redox enzyme. L-Lactate dehydrogenase catalyzes the reduction of pyruvate to L-lactate by NADH in vivo with absolute enantiospecificity[1] |