Kisspeptin-54 (human) peptide (TFA removed)

Kisspeptin-54 (human) 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

GTSLSPPPESSGSRQQPGLSAPHSRQIPAPQGAVLVQREKDLPNYNWNSFGLRF-NH2

H-Gly-Thr-Ser-Leu-Ser-Pro-Pro-Pro-Glu-Ser-Ser-Gly-Ser-Arg-Gln-Gln-Pro-Gly-Leu-Ser-Ala-Pro-His-Ser-Arg-Gln-Ile-Pro-Ala-Pro-Gln-Gly-Ala-Val-Leu-Val-Gln-Arg-Glu-Lys-Asp-Leu-Pro-Asn-Tyr-Asn-Trp-Asn-Ser-Phe-Gly-Leu-Arg-Phe-NH2

54

95.02%

C₂₅₈H₄₀₁N₇₉O₇₈

5857.51

Synthetic

Powder

KISSPEPTIN IS A 54-amino-acid peptide encoded by the KiSS-1 gene which acts via the G protein-coupled receptor (GPR) GPR54. GPR54 was discovered to be necessary for normal pubertal development when it was demonstrated that mice lacking GPR54 and humans with GPR54-null mutations do not mature sexually and have low circulating gonadotropins and sex hormones (hypogonadotropic hypogonadism). It was also found that kisspeptin in human females potently stimulates LH release in the preovulatory phase and may manipulate the HPG axis in women.

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

• M.L.Gottsch et al., Endocrinology, 145, 4073 (2004)
• S.B.Seminara and U.B.Kaiser, Endocrinology, 146, 1686 (2005)
• W.S.Dhillo et al., J. Clin. Endocrinol. Metab., 90, 6609 (2005)
• W.S.Dhillo et al., J. Clin. Endocrinol. Metab., 92, 3958 (2007)

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.