Prostate Specific Antigen-1 (153-161)

Prostate Specific Antigen-1 (153-161) is a synthetic peptide corresponding to a defined amino acid sequence within the prostate-specific antigen (PSA) protein. As a segment of PSA, which is a well-characterized serine protease and biomarker in prostate biology, this peptide fragment provides a valuable tool for researchers investigating protein function, antigenicity, and molecular interactions. The precise sequence derived from the 153-161 region of PSA enables targeted studies into the structural and functional motifs of the parent protein, supporting a wide range of biochemical and biomedical research applications.

Epitope Mapping: The defined sequence of Prostate Specific Antigen-1 (153-161) allows it to serve as a reference epitope for mapping antibody recognition sites on PSA. Researchers utilize this peptide to identify and characterize monoclonal or polyclonal antibodies that specifically bind to the 153-161 region, facilitating the development of immunoassays and advancing understanding of immune recognition patterns. Such studies are crucial for improving the specificity and sensitivity of PSA detection techniques in laboratory settings.

Immunogenicity Studies: As a representative antigenic fragment, this peptide is frequently employed in studies assessing the immunogenic properties of PSA. By exposing cells or model systems to the 153-161 sequence, investigators can evaluate T-cell or B-cell responses, analyze peptide-MHC binding affinities, and explore the mechanisms underlying immune surveillance in prostate tissue. These experiments provide insights into antigen processing and presentation relevant to prostate biology.

Peptide-Protein Interaction Analysis: The synthetic peptide form of the 153-161 segment offers a controlled system for studying protein-protein or protein-peptide interactions involving PSA. Using techniques such as surface plasmon resonance, isothermal titration calorimetry, or pull-down assays, researchers can probe the binding characteristics of this region with potential regulatory partners, inhibitors, or substrates. Such analyses help elucidate the biochemical pathways in which PSA participates and inform the design of novel molecular probes.

Analytical Standards: In proteomics and mass spectrometry-based workflows, the 153-161 peptide fragment serves as a reliable analytical standard. Its defined sequence and physicochemical properties make it suitable for calibrating instrumentation, validating peptide identification algorithms, and quantifying PSA-derived peptides in complex biological samples. Employing this peptide as a standard enhances the accuracy and reproducibility of quantitative proteomic analyses.

Structure-Function Relationship Studies: The specific 153-161 sequence enables detailed investigations into the structure-function relationships within PSA. By examining the conformational properties, post-translational modification potential, or enzymatic activity related to this region, scientists can dissect the molecular determinants that govern PSA's biological roles. These studies contribute to a deeper understanding of how discrete peptide segments influence the overall function and regulation of serine proteases in the prostate.

1. Adipose tissue is a key organ for the beneficial effects of GLP-2 metabolic function

2. The spatiotemporal control of signalling and trafficking of the GLP-1R

3. Multifunctional peptide-oligonucleotide conjugate promoted sensitive electrochemical biosensing of cardiac troponin I

4. Autoinhibition and phosphorylation-induced activation of phospholipase C-γ isozymes

5. A possible role of tachykinin-related peptide on an immune system activity of mealworm beetle, Tenebrio molitor L