GLP-1 (7-37) peptide

GLP-1 (7-37) peptide

• Handling and Storage of Synthetic Peptides
• Material Safety Data Sheets (MSDS)

Batch to batch variation of the purity

H-HAEGTFTSDVSSYLEGQAAKEFIAWLVKGRG-OH

H-His-Ala-Glu-Gly-Thr-Phe-Thr-Ser-Asp-Val-Ser-Ser-Tyr-Leu-Glu-Gly-Gln-Ala-Ala-Lys-Glu-Phe-Ile-Ala-Trp-Leu-Val-Lys-Gly-Arg-Gly-OH

31

95.73%

C₁₅₁H₂₂₈N₄₀O₄₇

3355.65

Synthetic

Powder

GLP-1 (7-37) is an endogenous truncated form of GLP-1 that arises from proglucagon processing in intestinal endocrine L cells, GLP-1 (7-37) acts as a GLP-1 receptor agonist and is an insulinotropic hormone that augments glucose induced insulin secretion. GLP-1 (7-37) and derivatives GLP-1 (9-37) and GLP-1 (28-37) can reduce plaque inflammation and increase phenotypic characteristics of plaque stability in a murine model of atherosclerosis.

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

• Hargrove et al (1995) Glucose-dependent action of glucagon-like peptide-1 (7-37) in vivo during short- or long-term administration. Metabolism 44(9) 1231 PMID: 7666800
• Vahl (2003) Effects of GLP-1-(7-36)NH2, GLP-1-(7-37), and GLP-1- (9-36)NH2 on intravenous glucose tolerance and glucose-induced insulin secretion in healthy humans. J Clin Endocrinol Metab. 88(4) 1772 PMID: 12679472
• Burgmaier et al (2013) Glucagon-like peptide-1 (GLP-1) and its split products GLP-1(9-37) and GLP-1(28-37) stabilize atherosclerotic lesions in apoe⁻/⁻ mice. Atherosclerosis 231(2) 427 PMID: 24267262

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.