cAMP-dependent protein kinase target site peptide

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

Batch to batch variation of the purity

• RRASV polypeptide acts as a specific target site for cAMP-dependent protein kinase. This polypeptide can be strategically fused with other proteins, such as the major tail protein of bacteriophage lambda, through advanced molecular biology techniques. The fusion not only allows for efficient phosphorylation by the corresponding kinase but also holds great potential for various applications.
• In the realm of biotechnology, the RRASV polypeptide has diverse applications. It can be utilized in the development of protein display systems, where it can be attached to the surface of certain structures, such as bacteriophage particles. This enables the screening and selection of proteins with specific characteristics. For instance, in phage display libraries, the RRASV polypeptide - fused proteins can be presented to identify molecules with desired binding or catalytic properties. Moreover, its ability to be phosphorylated provides a means of controlling and studying protein - protein interactions. This can have implications in understanding signal transduction pathways and developing novel therapeutic strategies. Overall, the RRASV polypeptide holds great promise for advancing research and innovation in multiple scientific disciplines.

• Dunn IS. Assembly of functional bacteriophage lambda virions incorporating C-terminal peptide or protein fusions with the major tail protein. J Mol Biol. 1995 May 5;248(3):497-506. doi: 10.1006/jmbi.1995.0237. PMID: 7752219.

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.