Holokinin-1 peptide

Holokinin-1 peptide

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

Batch to batch variation of the purity

H-PLGYMFR-OH

H-Pro-Leu-Gly-Tyr-Met-Phe-Arg-OH

7

95.78%

C₄₂H₆₂N₁₀O₉S

883.06

Synthetic

Powder

Four holokinins have been isolated from A. japonicus: holokinin-1 (PLGYMFR) and derivatives of holokinin-1 with either an oxidised methionine residue (PLGYM(O)FR, holokinin-2) or with a brominated tyrosine residue (PLGY(Br)MFR, holokinin-3) or with N-terminal truncation (GYMFR, holokinin-1(3–7)). All four peptides cause inhibition of electrically induced contraction of radial longitudinal muscle (RLM) preparations and contraction of intestine preparations.

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

• Elphick MR. The protein precursors of peptides that affect the mechanics of connective tissue and/or muscle in the echinoderm Apostichopus japonicus. PLoS One. 2012;7(8):e44492. doi:10.1371/journal.pone.0044492

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.