Glucagon-Like Peptide 1, GLP-1 (9-36), amide, human, mouse, rat, bovine, guinea pig - 1 mg
- Cat.Number : AS-65070
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GLP-1 (9-36) is the result of the rapid degradation of GLP-1 (7-36) amide, by the enzyme dipeptidyl peptidase IV (DPP-4), which is widely expressed in a number of sites, including the endothelial cells of small gut arterioles. GLP-1 (9-36) accounts for the majority of GLP-1 that reaches the system circulation. Whereas GLP-1 (7-36) amide stimulates glucose-dependent insulin secretion and inhibits glucagon secretion, GLP-1(9-36) amide administration had no effect on glucose clearance or insulin secretion in humans. GLP-1(9-36) amide however was shown to exert cardioprotective actions in rodent hearts.
Pyroglutamyl (pGlu) peptides may spontaneously form when either Glutamine (Q) or Glutamic acid (E) is located at the sequence N-terminus. The conversion of Q or E to pGlu is a natural occurrence and in general it is believed that the hydrophobic γ-lactam ring of pGlu may play a role in peptide stability against gastrointestinal proteases. Pyroglutamyl peptides are therefore considered a normal subset of such peptides and are included as part of the peptide purity during HPLC analysis.
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References
GLP‐1 (9–36) Amide, Cleavage Product of GLP‐1 (7–36) Amide, Is a Glucoregulatory Peptide
Obesity . 2012 Sep 06 ; 16(7) 1501 | DOI : https://doi.org/10.1038/oby.2008.229
- D. Elahi
- et al
Glucagon-Like Peptide (GLP)-1(9-36)Amide-Mediated Cytoprotection Is Blocked by Exendin(9-39) Yet Does Not Require the Known GLP-1 Receptor
Endocrinol . 2012 Sep 06 ; 151(4) 1520 | DOI : https://doi.org/10.1210/en.2009-1197
- K. Ban
- et al
N-terminal acetylation protects glucagon-like peptide GLP-1-(7-34)-amide from DPP-IV-mediated degradation retaining cAMP- and insulin-releasing capacity
Eur J Med Res . 2008 Feb 25 ; 13(2) 73 | DOI : PMID: 18424366
- H. John