Pancreatic Polypeptide, bovine

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Pancreatic Polypeptide, bovine
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Pancreatic Polypeptide, bovine, a straight chain polypeptide containing 36 amino acids, derived primarily from the pancreas, and stimulates pancreatic secretion by inhibiting secretin and cholecystokinin. As the NPY receptor agonist, it has a high affinity at NPYR4.

Category
Peptide Inhibitors
Catalog number
BAT-010582
CAS number
179986-89-1
Molecular Formula
C186H287N53O56S2
Molecular Weight
4225.78
Pancreatic Polypeptide, bovine
Synonyms
Ala-Pro-Leu-Glu-Pro-Glu-Tyr-Pro-Gly-Asp-Asn-Ala-Thr-Pro-Glu-Gln-Met-Ala-Gln-Tyr-Ala-Ala-Glu-Leu-Arg-Arg-Tyr-Ile-Asn-Met-Leu-Thr-Arg-Pro-Arg-Tyr-NH2; Pancreatic polypeptide (pig), 6-L-glutamic acid-; Bovine pancreatic polypeptide
Appearance
White or Off-white Lyophilized Powder
Purity
≥95%
Sequence
APLEPEYPGDNATPEQMAQYAAELRRYINMLTRPRY-NH2
Storage
Store at -20°C
Solubility
Soluble in DMSO
1.The ductal origin of structural and functional heterogeneity between pancreatic islets.
Merkwitz C1, Blaschuk OW, Schulz A, Lochhead P, Meister J, Ehrlich A, Ricken AM. Prog Histochem Cytochem. 2013 Oct;48(3):103-40. doi: 10.1016/j.proghi.2013.09.001. Epub 2013 Oct 4.
Islets form in the pancreas after the first endocrine cells have arisen as either single cells or small cell clusters in the epithelial cords. These cords constitute the developing pancreas in one of its earliest recognizable stages. Islet formation begins at the time the cords transform into a branching ductal system, continues while the ductal system expands, and finally stops before the exocrine tissue of ducts and acini reaches its final expansion. Thus, islets continuously arise from founder cells located in the branching and ramifying ducts. Islets arising from proximal duct cells locate between the exocrine lobules, develop strong autonomic and sensory innervations, and pass their blood to efferent veins (insulo-venous efferent system). Islets arising from cells of more distal ducts locate within the exocrine lobules, respond to nerve impulses ending at neighbouring blood vessels, and pass their blood to the surrounding acini (insulo-acinar portal system).
2.Structural and functional relationships of natural and artificial dimeric bovine ribonucleases: new scaffolds for potential antitumor drugs.
Gotte G1, Laurents DV, Merlino A, Picone D, Spadaccini R. FEBS Lett. 2013 Nov 15;587(22):3601-8. doi: 10.1016/j.febslet.2013.09.038. Epub 2013 Oct 7.
Protein aggregation via 3D domain swapping is a complex mechanism which can lead to the acquisition of new biological, benign or also malignant functions, such as amyloid deposits. In this context, RNase A represents a fascinating model system, since by dislocating different polypeptide chain regions, it forms many diverse oligomers. No other protein displays such a large number of different quaternary structures. Here we report a comparative structural analysis between natural and artificial RNase A dimers and bovine seminal ribonuclease, a natively dimeric RNase with antitumor activity, with the aim to design RNase A derivatives with improved pharmacological potential.
3.Immunohistochemical study on the ontogenetic development of the regional distribution of peptide YY, pancreatic polypeptide, and glucagon-like peptide 1 endocrine cells in bovine gastrointestinal tract.
Pyarokhil AH1, Ishihara M, Sasaki M, Kitamura N. Regul Pept. 2012 Apr 10;175(1-3):15-20. doi: 10.1016/j.regpep.2011.12.004. Epub 2012 Jan 9.
The regional distribution and relative frequency of peptide YY (PYY)-, pancreatic polypeptide (PP)-, and glucagon-like peptide 1 (GLP-1)-immunoreactive (IR) cells were determined immunohistochemically in the gastrointestinal tract at seven ontogenetic stages in pre- and postnatal cattle. Different frequencies of PYY-, PP-, and GLP-1-IR cells were found in the intestines at all stages; they were not found in the esophagus and stomach. The frequencies varied depending on the intestinal segment and the developmental stage. The frequencies of PYY- and PP-IR cells were lower in the small intestine and increased from ileum to rectum, whereas GLP-1-IR cells were more numerous in duodenum and jejunum, decreased in ileum and cecum, and increased again in colon and rectum. The frequencies also varied according to pre- and postnatal stages. All three cell types were most numerous in fetus, and decreased in calf and adult groups, indicating that the frequencies of these three types of endocrine cells decrease with postnatal development.
4.Pancreatic polypeptide administration enhances insulin sensitivity and reduces the insulin requirement of patients on insulin pump therapy.
Rabiee A1, Galiatsatos P, Salas-Carrillo R, Thompson MJ, Andersen DK, Elahi D. J Diabetes Sci Technol. 2011 Nov 1;5(6):1521-8.
INTRODUCTION: The effects of pancreatic polypeptide (PP) infusion were examined in patients on insulin pump therapy to determine whether PP administration can reduce insulin requirements in patients with type 1 diabetes mellitus (T1DM) or type 3c diabetes mellitus (T3cDM; pancreatogenic).

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