Prostatic Acid Phosphatase-3 (PAP-3)
CAT No: ta-547
Synonyms/Alias:Prostatic Acid Phosphatase-3 (135-143); PAP-3 (135-143)
PAP-3 (135-143) is a synthetic peptide fragment corresponding to amino acid residues 135 through 143 of prostatic acid phosphatase (PAP), a phosphatase enzyme highly expressed in the prostate and implicated in various physiological and pathological processes. As a defined peptide sequence, PAP-3 (135-143) serves as a valuable molecular tool for probing the structure-function relationships of PAP and its interactions with other biomolecules. Its precise sequence and biochemical features make it particularly relevant for research focused on peptide-mediated signaling, immunological recognition, and enzymatic regulation in the context of prostate biology and related areas.
Peptide mapping: PAP-3 (135-143) is frequently utilized in peptide mapping studies to elucidate the structural domains and functional motifs of prostatic acid phosphatase. By employing this fragment in mass spectrometry or immunochemical assays, researchers can identify specific regions involved in substrate binding, catalytic activity, or protein-protein interactions. Such mapping is critical for understanding the molecular determinants of PAP function and for designing targeted experiments to dissect its biological roles.
Epitope characterization: The defined sequence of PAP-3 (135-143) enables its use in the identification and characterization of B-cell or T-cell epitopes within prostatic acid phosphatase. By serving as a model antigen in immunological assays, this peptide assists in mapping immune recognition sites, supporting the development of diagnostic reagents or immunological probes. Its application in epitope mapping contributes to the broader understanding of immune responses against PAP and related antigens.
Protein interaction studies: As a synthetic peptide corresponding to a specific region of PAP, PAP-3 (135-143) is applied in binding assays and protein interaction screens to investigate molecular partners that recognize or interact with this domain. Such studies are instrumental in revealing the mechanisms by which PAP interfaces with regulatory proteins, inhibitors, or cellular receptors, providing insights into its physiological and pathological functions.
Antibody production: The unique sequence of PAP-3 (135-143) makes it suitable as an immunogen for the generation of sequence-specific polyclonal or monoclonal antibodies. When conjugated to carrier proteins and administered in animal models, it can elicit an immune response, resulting in antibodies that selectively recognize the corresponding region of PAP. These antibodies are valuable tools for immunodetection, quantification, or localization studies in biochemical and cell biological research.
Enzyme substrate specificity: PAP-3 (135-143) may also be employed in studies designed to assess the substrate specificity of prostatic acid phosphatase or related phosphatases. By incorporating this peptide into enzymatic assays, investigators can evaluate its suitability as a substrate or inhibitor, thereby gaining insights into the catalytic preferences, regulatory mechanisms, or potential allosteric sites of the enzyme. Such applications are essential for advancing our understanding of PAP enzymology and for informing the design of selective modulators.
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3. Adipose tissue is a key organ for the beneficial effects of GLP-2 metabolic function
5. SERS spectrum of the peptide thymosin‐β4 obtained with Ag nanorod substrate
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