CQAASIKVAV peptide

CQAASIKVAV peptide

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

Batch to batch variation of the purity

H-CQAASIKVAV-OH

H-Cys-Gln-Ala-Ala-Ser-Ile-Lys-Val-Ala-Val-OH

10

95.66%

C₄₂H₇₆N₁₂O₁₃S

989.19

Synthetic

Powder

The CQAASIKVAV peptide was originated from the effective fragments of laminin, which is validated to enhance the adhesion of SCs and neurite differentiation of PC 12 and DRG cells. CQAASIKVAV peptides derived from the effective linking fragment of laminin can promote the adhesion of various types of cells, in particular those cells of nervous system. It can induce the neurite differentiation of DRG and PC 12 cells, and is thus beneficial for PNS regeneration in vivo

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

• Zhang D, Li Z, Shi H, Yao Y, Du W, Lu P, Liang K, Hong L, Gao C. Micropatterns and peptide gradient on the inner surface of a guidance conduit synergistically promotes nerve regeneration in vivo. Bioact Mater. 2021 Jul 15;9:134-146. doi: 10.1016/j.bioactmat.2021.07.010. PMID: 34820561; PMCID: PMC8586031.

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.