Allatostatin B 12 peptide

Allatostatin B 12 peptide

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

H-VPNDWAHFRGSW-NH2

H-Val-Pro-Asn-Asp-Trp-Ala-His-Phe-Arg-Gly-Ser-Trp-NH2

12

95.88%

C₆₉H₉₁N₂₁O₁₆

1470.59

Synthetic

Powder

The source of Allatostatin B 12 is common shore crab / green crab (Carcinus maenas).
Allatostatin B 12, which is also called CbAST-B1, is a novel B type allatostatin identified and sequenced in the pericardial organs of the crabs, Cancer borealis and Cancer productus. It shares a conserved C-terminal motif of W(X)6W, which is characteristic of the B-type allatostatin peptide family.
Allatostatin B 12 has been found to modulate the pyloric rhythm of the crab's stomatogastric ganglion (STG) in a dose-dependent manner. It reduces the pyloric network frequency and its effects depend on the preceding physiological state of the preparation.
Despite its dissimilarity in amino acid sequence with the A-type allatostatin family, Allatostatin B 12 has similar physiological effects to AST-A. The frequency of the pyloric rhythm is dependent on neuromodulatory inputs from the anterior ganglia, and the effects of Allatostatin B 12 on the pyloric neurons are dependent on the starting frequency of the pyloric rhythm.

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

• Fu Q, Tang LS, Marder E, Li L. Mass spectrometric characterization and physiological actions of VPNDWAHFRGSWamide, a novel B type allatostatin in the crab, Cancer borealis. J Neurochem. 2007 May;101(4):1099-107.
• Ma M, Bors EK, Dickinson ES, et al. Characterization of the Carcinus maenas neuropeptidome by mass spectrometry and functional genomics. Gen Comp Endocrinol. 2009;161(3):320-34.
• Szabo TM, Chen R, Goeritz ML, Maloney RT, Tang LS, Li L, Marder E. Distribution and physiological effects of B-type allatostatins (myoinhibitory peptides, MIPs) in the stomatogastric nervous system of the crab Cancer borealis. J Comp Neurol. 2011 Sep 1;519(13):2658-76.

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.