Holokinin-2 peptide

Holokinin-2 peptide

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

Batch to batch variation of the purity

PLGYM(O)FR

H-Pro-Leu-Gly-Tyr-Met(O)-Phe-Arg-OH

7

97.7%

C₄₂H₆₂N₁₀O₁₀S

899.1

Synthetic

Powder

The amino acid sequences of holokinins are homologous with those of bradykinins in vertebrates and wasps. Vertebrate bradykinins have a wide range of effects, mainly on the central nervous system and on smooth muscles. Holokinins had the most prominent effect among the peptides tested here and are the first fully characterized softening agent for sea cucumber dermis. As the only identified softening agents, the holokinins are unique. Their effect was easily suppressed by menthol, indicating that they can be classified as neuropeptides. Sequcen of Holokinin 1 is PLGYMFR(MW=883.06 g/mol)

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

• Birenheide R, Tamori M, Motokawa T, Ohtani M, Iwakoshi E, Muneoka Y, Fujita T, Minakata H, Nomoto K. Peptides controlling stifness of connective tissue in sea cucumbers. Biol Bull. 1998 Jun;194(3):253-9. doi: 10.2307/1543095. PMID: 9664654.

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.