GLP-1 (1-37), Glucagon-like peptide 1

GLP-1 (1-37), Glucagon-like peptide 1

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

Batch to batch variation of the purity

HDEFERHAEGTFTSDVSSYLEGQAAKEFIAWLVKGRG

H-His-Asp-Glu-Phe-Glu-Arg-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

37

97.4%

C₁₈₆H₂₇₅N₅₁O₅₉

4169.54

Synthetic

Powder

Glucagon-Like Peptide 1 (GLP-1) is synthesized by posttranslational processing of proglucagon in the intestine and pancreas and plays an important role in metabolic homeostasis. Among the different molecular forms, such as GLP-1 (7-36) amide and GLP-1 (7-37), the function of GLP-1 (1-37) has been unclear. GLP-1 (1-37) was shown to convert intestinal epithelial cells into insulin-producing cells. These observations turned GLP-1 (1-37) into a new promising therapeutic compound for the treatment of

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

• A.Suzuki et al., Proc. Natl. Acad. Sci. USA, 100, 5034 (2003)
• M.A.Nauck et al., Diabetes, 53 (Suppl. 3), S190 (2004)
• A.K.Bose et al., Cardiovasc. Drugs Ther., 19, 9 (2005)
• D.J.Grieve et al., Br. J. Pharmacol., 157, 1340 (2009)

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.