Kisspeptin-10 peptide (TFA removed)

Kisspeptin-10 peptide (TFA removed)

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

Batch to batch variation of the purity

YNWNSFGLRY-NH2

Tyr-Asn-Trp-Asn-Ser-Phe-Gly-Leu-Arg-Tyr-NH2

10

98.8%

C₆₃H₈₃N₁₇O₁₅

1318.61

478507-53-8

Synthetic

Powder

The source of Kisspeptin-10 is Mus musculus. Kisspeptin-10 belongs to KISS1. Kisspeptin-10 is expressed in Weak in all tissue types with highest levels in lung and 15- 17-day embryos. Expressed in areas of the hypothalamus implicated in the neuroendocrine regulation of gonadotropin secretion, including the anteroventral periventricular nucleus, the periventricular nucleus, and the arcuate nucleus. The peptide has the modification: 1 Tyr Phosphotyrosine (By similarity); 10 Tyr amide (By similarity)

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

• Nielsen SB, Franzmann M, Basaiawmoit RV, Wimmer R, Mikkelsen JD, Otzen DE beta-Sheet aggregation of kisspeptin-10 is stimulated by heparin but inhibited by amphiphiles Biopolymers 2010 Aug;93(8):678-89

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.