alpha-Melanocyte-stimulating hormone peptide

alpha-Melanocyte-stimulating hormone peptide

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

Batch to batch variation of the purity

SYAMEHFRWGKPV

H-Ser-Tyr-Ala-Met-Glu-His-Phe-Arg-Trp-Gly-Lys-Pro-Val-NH2

13

97.3%

C₇₅H₁₀₇N₂₁O₁₇S

1606.8

Synthetic

Powder

alpha-Melanocyte-stimulating hormone was found in American chameleon / green anole (Anolis carolinensis), leopard gecko (Eublepharis macularius), brown tree snake (Boiga irregularis). α-Melanotropin (α-MSH) is a peptide hormone derived from the proopiomelanocortin (POMC) polyprotein. It is present in various vertebrates. The melanotropic core sequence, Met-Glu-His-Phe-Arg-Trp-Gly, is conserved in many species at multiple locations within the primary sequence of its precursor. In different species, there are variations in the N-terminal and C-terminal regions. In contrast, in mammals, it is typically NAc-Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly-Lys-Pro-Val-amide. In many species, the major forms of α-MSH are N-acetylated, and this posttranslational processing event appears to enhance its biological activity. However, in Anolis carolinensis, the major storage form of α-MSH in melanotropic cells is nonacetylated.

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

• Dores RM, Lancha A, Rand-weaver M, Jankelow L, Adamczyk DL. Detection of a novel sequence change in the major form of alpha-MSH isolated from the intermediate pituitary of the reptile, Anolis carolinensis. Peptides. 1991;12(6):1261-6.

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.