gastric inhibitory polypeptide

Gastric Inhibitory Polypeptide (6-30) amide (human) is an incretin hormone used in diabetes research [1].

Gastric Inhibitory Polypeptide (1-30), porcine, deficient in the 12 C-terminal amino acids of the natural gastric inhibitory polypeptide (GIP), demonstrates biological activity by enhancing the release of insulin and somatostatin [1].

Acetyl Gastric Inhibitory Peptide (human) TFA, a fatty acid-derivatized analog of the glucose-dependent insulinotropic polypeptide, exhibits enhanced antihyperglycemic and insulinotropic properties. It is utilized in the research of diabetes, insulin resistance, and obesity [1] [2] [3].

Acetyl Gastric Inhibitory Peptide (human), a fatty acid-derivatized analog of glucose-dependent insulinotropic polypeptide, exhibits enhanced antihyperglycemic and insulinotropic characteristics. This compound is utilized in diabetes, insulin resistance, and obesity research [1] [2] [3].

GIP (3-42), human (Gastric Inhibitory Polypeptide (3-42) (human)) is a peptide that acts as a glucose-dependent proinsulinotropic polypeptide (GIP) receptor antagonist and regulates insulin secretion and the metabolic effects of GIP in vivo, which can be used to study type 2 diabetes.

[Tyr0] Gastric Inhibitory Peptide (23-42), human, is a glucose-dependent insulinotropic polypeptide (GIP) that modestly inhibits gastric acid secretion while enhancing insulin secretion, making it relevant for research on diabetes and obesity [1] [2].

Gastric Inhibitory Peptide (porcine), also known as a glucose-dependent insulinotropic polypeptide, is a 42-amino acid intestinal hormone that influences fat and glucose metabolism [1].

Gastric inhibitory peptide 1 (GIP-1) (3-42), a fragment of the incretin hormone GIP and antagonist to the GIP receptor, is generated through the action of serum dipeptidyl peptidase 4 (DDP-4). When administered at 25 nmol/kg to an ob/ob mouse diabetes model, GIP-1 (3-42) elevates plasma glucose levels and lowers plasma insulin levels, demonstrating its effect on reducing insulin secretion from BRIN-BD11 pancreatic cells at a concentration of 100 nM.

This GIP fragment has potent insulinotropic activity in the isolated, perfused rat pancreas but greatly reduced somatostatinotropic activity in the isolated perfused rat stomach. The site responsible for insulinotropic activity apparently lies between residues 19 and 30 of GIP.

Gastric inhibitory peptide (GIP) (1-42), an endogenous incretin hormone comprising 42 amino acids, promotes insulin secretion. Expressed in the intestinal neuroendocrine K cells and submandibular gland, it enters circulation after meals. GIP (1-42) blocks histamine, pentagastrin, and insulin-induced gastric acid and pepsin secretion, enhances glucose-stimulated insulin release, and accelerates gastric emptying in rats.

Gastric inhibitory peptide (GIP) (22-51), a pro-atherogenic peptide comprised of 30 amino acids from the residues 22-51 of its precursor protein proGIP, is present in human plasma. It activates the degradation of IκB-α and the nuclear translocation of NF-κB in both macrophage-differentiated THP-1 cells and human aortic endothelial cells at a concentration of 1 µM. Additionally, in ApoE-/- mice, GIP (22-51) escalates the area of atherosclerotic lesions and plaque development in vivo.

GIP (rat) (Glucose-dependent Insulinotropic Polypeptide), also known as Gastric Inhibitory Polypeptide, is a biologically active 42-amino acid peptide secreted by the K cells of the duodenum and jejunum following food consumption. It belongs to the incretin hormone peptide family, which includes GLP (Gastric-like Peptide), and it not only stimulates insulin release from pancreatic islet β-cells but also may encourage β-cell proliferation and survival. Additionally, recent research indicates GIP may have a role in lipid regulation and could contribute to the development of obesity.

GIP (1-30) amide, porcine TFA is a high-affinity full agonist of the glucose-dependent insulinotropic polypeptide (GIP) receptor, with potency comparable to native GIP(1-42) [1]. It also exhibits potent insulin-stimulating properties and weakly inhibits gastric acid secretion.

GIP, rat TFA (glucose-dependent insulinotropic polypeptide), a 42-amino acid peptide secreted by K cells in the duodenum and jejunum, promotes insulin release from pancreatic beta cells, supports beta cell proliferation, and enhances their survival. This rat-origin bioactive peptide, along with GLP (gastric-like peptide), belongs to the intestinal insulinotropic hormone family and is implicated in lipid homeostasis and potentially in the pathogenesis of obesity. Recent research suggests GIP's multifaceted role in these metabolic processes.