Alarin (human) peptide

Alarin (human) peptide

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

Batch to batch variation of the purity

APAHRSSTFPKWVTKTERGRQPLRS

H-Ala-Pro-Ala-His-Arg-Ser-Ser-Thr-Phe-Pro-Lys-Trp-Val-Thr-Lys-Thr-Glu-Arg-Gly-Arg-Gln-Pro-Leu-Arg-Ser-OH

25

97.5%

C₁₂₇H₂₀₅N₄₃O₃₅

2894.29

909409-86-5

Synthetic

Powder

Alarin is derived from a splice variant of galanin-like peptide (GALP) RNA. It shows potent and dose-dependent vasoconstrictor and anti-edema activity in the cutaneous microvasculature, as was also observed with other members of the galanin peptide family. Since alarin only shares five amino acids with GALP it is unlikely that the peptide can activate GALP-specific receptors. Originally discovered as neuropeptide in 2006 (Santic R et al 2006). It was termed alarin because of the N-terminal alanine and the C-terminal serine. In 2013, this peptide was demonstrated to have antimicrobial activity as well. Active against Gram-negative E. coli ML-35. Deletion of the conserved N-terminal sequence (APAHR) reduced its antimicrobial activity, suggesting that APAHR is essential for its antimicrobial activity. Electron microscopy showed that alarin caused bacterial membrane blebbing. Updated 11/26/2013. Alarin has Antibacterial activity. Alarin was found in brain, Homo sapiens.

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

• R.Santic et al., J. Mol. Neurosci., 29, 145 (2006)
• R.Santic et al., Proc. Natl. Acad. Sci. USA, 104, 10217 (2007)

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.