Glyceraldehyde-3-phosphate dehydrogenase (219-230)

Glyceraldehyde-3-phosphate dehydrogenase (219-230) is a synthetic peptide fragment corresponding to amino acid residues 219 through 230 of the enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH). As a highly conserved region of a central glycolytic enzyme, this peptide serves as a valuable molecular tool for probing protein structure, function, and interaction dynamics. Researchers utilize such defined peptide sequences to investigate site-specific biochemical properties and to advance understanding of post-translational modifications, protein-protein interactions, and immune recognition. Its defined sequence and origin from a functionally critical region of GAPDH make it particularly relevant in studies of metabolism, cellular signaling, and molecular recognition.

Epitope mapping: The 219-230 peptide fragment of GAPDH is widely employed in epitope mapping experiments to identify antibody binding sites within the parent protein. By providing a discrete linear sequence, the peptide enables researchers to localize immunogenic epitopes and assess the specificity of antibodies raised against GAPDH. Such studies are essential for developing precise immunodetection reagents and for characterizing immune responses in basic and applied research contexts.

Protein-protein interaction studies: Researchers use this peptide to elucidate interaction interfaces between GAPDH and its binding partners. The 219-230 region may participate in or influence the formation of protein complexes involved in metabolic regulation or cellular signaling. By incorporating the peptide in in vitro binding assays or pull-down experiments, scientists can dissect the molecular determinants of these interactions and gain mechanistic insights into GAPDH's non-glycolytic functions.

Post-translational modification analysis: The defined sequence of the 219-230 peptide allows for targeted investigation of post-translational modifications, such as phosphorylation or acetylation, that may occur within this region of GAPDH. Incorporating the peptide into mass spectrometry workflows or modification-specific assays enables precise characterization of modification sites, their functional consequences, and their regulatory significance in cellular metabolism and stress response pathways.

Peptide-based assay development: The synthetic peptide is a useful standard or substrate in the development and optimization of peptide-based analytical assays, including enzyme-linked immunosorbent assays (ELISAs) and competitive binding assays. Its defined sequence and high solubility facilitate assay calibration, sensitivity testing, and the validation of detection reagents for GAPDH-derived peptides in complex biological samples.

Structural and conformational studies: The 219-230 peptide fragment serves as a model for investigating secondary structure propensity and conformational dynamics within the larger GAPDH protein. By employing spectroscopic techniques such as circular dichroism or nuclear magnetic resonance, researchers can analyze the isolated peptide to infer structural features relevant to protein folding, stability, or interaction motifs. These studies contribute to a deeper understanding of the structural biology of GAPDH and its functional domains.

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