Alpha-MSH (oxidized) peptide

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

Batch to batch variation of the purity

Alpha-MSH (oxidized) is a post-translationally modified neuropeptide derived from the proopiomelanocortin (POMC) precursor protein. It is characterized by the acetylation of its N-terminal serine residue and the oxidation of a methionine residue within its sequence, resulting in the molecular form Ac-SYS-Mox-EHFRWGKPV-amide. This peptide is generated within neuroendocrine tissues through a series of enzymatic processing steps involving prohormone convertases, with PC2 playing a critical role in its biosynthesis. In studies using PC2 knockout mice, Alpha-MSH (oxidized) was undetectable in hypothalamic extracts, indicating its production is largely dependent on PC2-mediated endoproteolytic cleavage of the POMC precursor.

• Pan H, Che FY, Peng B, Steiner DF, Pintar JE, Fricker LD The role of prohormone convertase-2 in hypothalamic neuropeptide processing: a quantitative neuropeptidomic study J Neurochem 2006 Sep;98(6):1763-77

Trifluoroacetic acid (TFA) is a common counterion from the purification process using High-Performance Liquid Chromatography (HPLC). The presence of TFA can affect the peptide's net weight, appearance, and solubility.

Impact on Net Weight: The TFA salt contributes to the total mass of the product. In most cases, the peptide content constitutes >80% of the total weight, with TFA accounting for the remainder.

Solubility: TFA salts generally enhance the solubility of peptides in aqueous solutions.

In Biological Assays: For most standard in vitro assays, the residual TFA levels do not cause interference. However, for highly sensitive cellular or biochemical studies, please be aware of its presence.