Pancreatic Polypeptide (human) acetate is a C-terminally amidated 36 amino acid peptide, which acts as a neuropeptide Y (NPY) Y4/Y5 receptor agonist.

Pancreatic Polypeptide, rat acetate is an agonist of NPY receptor, with high affinity at NPYR4.

Antifreeze Polypeptide 6 (winter flounder) is one of the winter flounder's antifreeze polypeptides, responsible for depressing the freezing point of plasma by inhibiting the expansion of ice nuclei [1].

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

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.

Pancreatic polypeptide, a peptide produced by the pancreas's endocrine PP cells, modulates pancreatic secretory functions and influences hepatic glycogen levels and gastrointestinal secretion [1].

[cPP1-7,NPY19-23,Ala31,Aib32,Gln34]-hPancreatic Polypeptide is a potent, selective neuropeptide Y Y5 receptor agonist, demonstrating binding affinity with an IC50 of 0.24 nM for the hY5 receptor. This compound significantly stimulates food intake [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 through the enhancement of insulin and somatostatin release [1].

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.

Tri-valine (NSC 35938) is a polypeptide isolated from creatine kinase, β-enolase, triosephosphate isomerase, and glyceraldehyde 3-phosphate dehydrogenase [1].

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.

Melittin free acid, a basic 26-amino-acid polypeptide, constitutes the primary active component of honeybee venom and serves as a phospholipase A2 (PLA2) activator. Exhibiting a broad-spectrum antifungal effect, it presents MIC values ranging from 0.4-60 μM. Its mechanism includes inducing cell apoptosis, inhibiting (1,3)-β-D-glucan synthase, and engaging in multiple pathways [1] [2].

Insulin bovine (Insulin from bovine pancreas) is a biologically derived two-chain polypeptide hormone, synthesized in vivo by pancreatic β cells. It is frequently utilized as a growth supplement in cell culture applications.

The amyloid β-protein is a 39- to 43-amino acid polypeptide that is the primary constituent of senile plaques and cerebrovascular deposits in Alzheimer's disease and Down's syndrome. Additionally it acts as an inhibitor of the ubiquitin-dependent protein degradation in vitro.

Amylin (IAPP), feline TFA, a 37-amino acid polypeptide derived from felines, stands as a principal secretion product of the pancreatic islets' β-cells. This regulatory peptide notably inhibits the secretion of insulin and glucagon [1].

Amyloid β-Protein (36-42), the 36-42 fragment of β-Amyloid, consists of a polypeptide chain of 36-43 amino acids and is a primary constituent of amyloid plaques in Alzheimer's disease (AD) patients' brains. β-Amyloid oligomers (Aβos) critically contribute to AD progression by causing neuronal harm and cognitive decline [1].