Amyloid β//A4 Protein Precursor770 (740-770) peptide

Amyloid β//A4 Protein Precursor770 (740-770) peptide

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

AAVTPEERHLSKMQQNGYENPTYKFFEQMQN

Ala-Ala-Val-Thr-Pro-Glu-Glu-Arg-His-Leu-Ser-Lys-Met-Gln-Gln-Asn-Gly-Tyr-Glu-Asn-Pro-Thr-Tyr-Lys-Phe-Phe-Glu-Gln-Met-Gln-Asn

31

96.2%

C₁₆₂H₂₄₃N₄₅O₅₂S₂

3717.14

Synthetic

Powder

Amyloid β/A4 Protein Precursor₇₇₀ (740-770) corresponds to a C-terminal amyloid precursor protein (APP) fragment known as C31. This fragment is intracellularly generated by proteolytic cleavage of APP by caspases-8 and -9. C31 had a proapoptotic and a cytotoxic effect on neuronal cells and was shown to be present in brains of Alzheimer's disease (AD) patients. In cultured cells caspase cleavage of APP was induced by amyloid β-protein and the subsequent generation of C31 contributed to the apoptotic cell death associated with amyloid β-protein. Amyloid precursor binding protein BP1 (APP-BP1) a cell cycle protein which is increased in AD brain was demonstrated to bind to the C31 region of APP and to mediate APP-induced apoptosis.

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

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.