Gastrin-34 peptide

Gastrin-34 peptide

• COA/MS/HPLC Report
• Handling and Storage of Synthetic Peptides
• Material Safety Data Sheets (MSDS)

Batch to batch variation of the purity

Glp-LGPQGPPHLVADPSKKQGPWLEEEEEAYGWMDF-NH2, Glp=Pyroglutamic acid

pGlu-Leu-Gly-Pro-Gln-Gly-Pro-Pro-His-Leu-Val-Ala-Asp-Pro-Ser-Lys-Lys-Gln-Gly-Pro-Trp-Leu-Glu-Glu-Glu-Glu-Glu-Ala-Tyr-Gly-Trp-Met-Asp-Phe-NH2

34

97.6%

C₁₇₆H₂₅₁N₄₃O₅₃S

3849.18

Synthetic

Powder

Gastrin-34 is also referred to as Big Gastrin. Secretion of gastrin is induced by food intake and causes the release of gastric acid in the stomach. Secreted by the G cells in the gastric mucosa, it is one of the major bioactive forms of gastrin found in tissue and plasma (the other bioactive form is gastrin-17 or little gastrin). Both gastrin-17 and gastrin-34 are carboxy-amidated and partially tyrosine sulfated. Binding of gastrin to the CCK2/gastrin receptor requires carboxy-amidation, however sulfation is not necessary for binding to the receptor. Binding of Gastrin to the CCK2/gastrin receptors on parietal cells of the stomach causes them to secrete hydrochloric acid (HCl) and stimulates lectin-like protein Reg expression via activation of PKC and RhoA. Gastrin also plays a role in release of Histamine and Pepsinogen.

Normally, this peptide will be delivered in lyophilized form and should be stored in a freezer at or below -20 °C. For more details, please refer to the manual:Handling and Storage of Synthetic Peptides

• Boel E, Vuust J, Norris F, et al. Molecular cloning of human gastrin cDNA: evidence for evolution of gastrin by gene duplication. Proc Natl Acad Sci USA. 1983;80(10):2866-9.

Trifluoroacetic acid (TFA) has a significant impact on peptides due to its role in the peptide synthesis process.

TFA is essential for the protonation of peptides that lack basic amino acids such as Arginine (Arg), Histidine (His), and Lysine (Lys), or ones that have blocked N-termini. As a result, peptides often contain TFA salts in the final product.

TFA residues, when present in custom peptides, can cause unpredictable fluctuations in experimental data. At a nanomolar (nM) level, TFA can influence cell experiments, hindering cell growth at low concentrations (as low as 10 nM) and promoting it at higher doses (0.5–7.0 mM). It can also serve as an allosteric regulator on the GlyR of glycine receptors, thereby increasing receptor activity at lower glycine concentrations.

In an in vivo setting, TFA can trifluoroacetylate amino groups in proteins and phospholipids, inducing potentially unwanted antibody responses. Moreover, TFA can impact structure studies as it affects spectrum absorption.