Fructose-bisphosphate aldolase A isoform 2 (207-222)

Fructose-bisphosphate aldolase A isoform 2 (207-222) is a synthetic peptide fragment derived from the human aldolase A enzyme, specifically corresponding to amino acid residues 207 to 222 of isoform 2. As a peptide compound, it represents a defined segment of a key glycolytic enzyme, making it a valuable tool for research into enzyme structure-function relationships, protein-protein interactions, and post-translational modifications. Its sequence specificity and biochemical relevance position it as a versatile reagent for studies focused on metabolic regulation, signal transduction, and immunological recognition involving aldolase A and related pathways.

Enzyme structure-function analysis: Researchers utilize this peptide to dissect the functional domains of aldolase A, particularly to investigate how the 207-222 region contributes to the enzyme's catalytic activity and substrate binding. By employing the peptide in binding assays or as a competitive inhibitor, scientists can map critical residues involved in the enzyme's active site or allosteric regulation. Such studies provide mechanistic insights into glycolytic control and the modulation of energy metabolism at the molecular level.

Protein interaction mapping: The defined sequence of this peptide enables targeted exploration of protein-protein interactions involving aldolase A. It can serve as a probe in pull-down assays, surface plasmon resonance, or co-immunoprecipitation experiments to identify cellular partners that interact with the 207-222 region. This application is particularly relevant for elucidating non-glycolytic roles of aldolase A, such as its participation in cytoskeletal dynamics or signal transduction complexes, thereby expanding understanding of its multifunctional nature in the cell.

Epitope mapping and antibody production: The peptide's precise sequence makes it an excellent antigen for generating site-specific antibodies or for mapping immunogenic epitopes within the aldolase A protein. Researchers can use it to immunize animals or to screen for antibody specificity in immunoassays, facilitating the development of tools for detecting or quantifying aldolase A isoform 2 in biological samples. This approach supports studies in proteomics, biomarker discovery, and the validation of antibody-based detection methods.

Post-translational modification studies: The 207-222 segment of aldolase A may encompass residues susceptible to phosphorylation, acetylation, or other modifications. By using this synthetic peptide in in vitro modification assays, investigators can assess the enzymatic activity of modifying enzymes, map modification sites, and evaluate their impact on protein function. Such experiments are critical for unraveling regulatory mechanisms that control aldolase A activity and its integration into cellular signaling networks.

Mass spectrometry and analytical method development: As a chemically defined standard, the peptide is highly useful in mass spectrometry-based proteomics workflows. It can be spiked into complex samples to optimize peptide identification, validate quantification protocols, or calibrate instrument response. Its use enhances the accuracy and reproducibility of analytical methods aimed at characterizing the aldolase A protein or monitoring its abundance in various experimental contexts. Through these diverse applications, the peptide supports a broad range of biochemical, analytical, and molecular biology research initiatives.

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