NAD-dependent protein deacetylase sirtuin-2 (192-200)

NAD-dependent protein deacetylase sirtuin-2 (192-200) is a synthetic peptide fragment derived from the human SIRT2 sequence, encompassing amino acids 192 to 200. As part of the sirtuin family, SIRT2 is a NAD+-dependent deacetylase that plays a critical role in regulating cellular processes such as gene expression, metabolism, cell cycle progression, and stress response through the removal of acetyl groups from lysine residues on target proteins. The 192-200 peptide region is of particular interest for biochemical research due to its involvement in substrate recognition, post-translational modification mapping, and potential regulatory interactions. Researchers utilize this peptide as a biochemical tool to dissect the molecular mechanisms underlying sirtuin-mediated deacetylation and to explore the functional domains of SIRT2 in various cellular contexts.

Peptide substrate studies: As a defined fragment of SIRT2, the 192-200 peptide serves as an important model substrate for in vitro deacetylation assays. By incorporating this peptide into enzymatic reactions, researchers can evaluate the catalytic activity of SIRT2 or related deacetylases, assess substrate specificity, and screen for modulators or inhibitors that affect deacetylation efficiency. The use of this synthetic sequence enables precise kinetic measurements and mechanistic studies, facilitating the development of novel biochemical assays for sirtuin enzymology.

Epitope mapping and antibody validation: The SIRT2 (192-200) peptide functions as a valuable antigenic determinant for generating and validating antibodies specific to this region of the protein. Employing this fragment in immunoassays such as ELISA, western blotting, or immunoprecipitation allows researchers to confirm antibody specificity, map epitopes, and optimize detection protocols. This application is fundamental for producing reliable immunological reagents for SIRT2 research and for distinguishing between closely related sirtuin isoforms.

Protein-protein interaction studies: The defined sequence of the 192-200 region is instrumental in probing the molecular interactions between SIRT2 and its binding partners. By using the peptide in pulldown assays, surface plasmon resonance, or other biophysical methods, scientists can identify and characterize proteins or small molecules that interact with this domain. Such studies contribute to elucidating the regulatory networks governing sirtuin function and provide insight into the structural determinants of protein-protein recognition.

Peptide modification and post-translational analysis: Synthetic access to the SIRT2 (192-200) peptide allows for the incorporation of site-specific modifications, such as acetylation, phosphorylation, or methylation, to mimic physiological post-translational states. These modified peptides are employed in mass spectrometry-based assays and structural studies to investigate how chemical modifications influence SIRT2 activity, substrate recognition, or interaction with regulatory factors. This approach supports detailed mapping of modification-dependent signaling pathways and the functional consequences of dynamic protein regulation.

Structural and conformational research: The 192-200 peptide is utilized in structural biology and conformational analysis to study the folding, secondary structure, and dynamic properties of SIRT2 domains. Techniques such as circular dichroism spectroscopy, NMR, or X-ray crystallography can be applied to this fragment to gain insights into the structural motifs that contribute to the protein's functional properties. These investigations advance the understanding of sirtuin architecture and inform structure-based drug design or inhibitor development efforts targeting the SIRT2 enzyme family.

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