Retinal dehydrogenase 1
Retinal dehydrogenase 1 (88-96) is a synthetic peptide corresponding to amino acid residues 88 through 96 of the human retinal dehydrogenase 1 (ALDH1A1) enzyme. As a targeted peptide fragment, it serves as a valuable molecular tool for investigating the structure, function, and regulation of aldehyde dehydrogenases, particularly within the context of retinoid metabolism and cellular redox homeostasis. Its defined sequence enables precise interrogation of protein-protein interactions, epitope mapping, and post-translational modification studies, making it highly relevant to biochemical research focused on enzymology, signal transduction, and metabolic regulation.
Enzyme function analysis: Researchers utilize this peptide to study the structure-function relationships within the ALDH1A1 enzyme family. By examining the biochemical properties of the 88-96 region, investigators can identify critical residues involved in substrate recognition, catalysis, or cofactor binding. This targeted approach supports mechanistic studies that dissect the role of specific sequence motifs in aldehyde oxidation and retinoic acid biosynthesis, thereby advancing understanding of metabolic pathways regulated by retinal dehydrogenases.
Epitope mapping and antibody development: The defined sequence of this peptide is instrumental in generating and validating antibodies specific to ALDH1A1. It provides a reliable antigen for mapping linear epitopes, which facilitates the production of monoclonal or polyclonal antibodies with high specificity. These antibodies are essential tools for immunodetection techniques such as Western blotting, ELISA, and immunohistochemistry, enabling sensitive and selective quantification or localization of the native enzyme in complex biological samples.
Protein-protein interaction studies: The 88-96 peptide fragment can be employed as a probe to investigate molecular interactions involving ALDH1A1. By serving as a competitive inhibitor or binding substrate in affinity-based assays, it helps elucidate the binding partners and regulatory proteins that associate with the enzyme's functional domains. Such studies are crucial for mapping interaction networks, understanding regulatory mechanisms, and identifying modulators of enzymatic activity within cellular pathways.
Post-translational modification analysis: Synthetic peptides derived from defined regions of enzymes are frequently used to study post-translational modifications such as phosphorylation, acetylation, or oxidation. The 88-96 sequence can be incorporated into assays designed to detect or characterize modifications that regulate ALDH1A1 activity, stability, or localization. These investigations provide insight into the dynamic regulation of retinoid metabolism and the role of post-translational events in cellular signaling.
Peptide-based assay development: As a well-characterized peptide fragment, the 88-96 region of ALDH1A1 is suitable for use in developing quantitative or qualitative assays. It can serve as a standard or calibrator in mass spectrometry-based proteomic workflows, or as a substrate in enzyme activity assays. The high sequence specificity ensures reliable detection and measurement, supporting robust analytical methods for studying enzyme kinetics, inhibitor screening, or biomarker quantification in research and industrial applications.
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