SHBG141–161 peptide

SHBG141–161 peptide

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

H-IALGGLLFPASNLRLPLVPAL-OH

H-Ile-Ala-Leu-Gly-Gly-Leu-Leu-Phe-Pro-Ala-Ser-Asn-Leu-Arg-Leu-Pro-Leu-Val-Pro-Ala-Leu-OH

21

95.72%

C₁₀₃H₁₇₃N₂₅O₂₄

2145.62

Synthetic

Powder

SHBG141–161 is a peptide corresponding to amino acids 141–161 of sex hormone binding globulin (SHBG), the loop region of SHBG connecting β-strands 11 and 12. SHBG141–161 is an agonist of the class C orphan G protein coupled receptor GPRC6A, a major regulator of energy metabolism and male fertility, and SHBG141-161 competes for binding to it with its endogenous ligand undercarboxylated osteocalcin (ucOCN). In vitro, SHBG141-161 stimulates insulin secretion from β-cells and also the production and release of testosterone from Leydig and Langerhans β-cells cell lines.

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

• De Toni et al (2019) SHBG141-161 Domain-Peptide Stimulates GPRC6A-Mediated Response in Leydig and β-Langerhans cell lines. Sci Rep. 9(1) 19432 PMID: 31857654

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.