Protein SSX4 (31-50)

Protein SSX4 (31-50) is a synthetic peptide fragment corresponding to amino acids 31 through 50 of the human Synovial Sarcoma, X Breakpoint 4 (SSX4) protein. As a member of the SSX gene family, SSX4 is implicated in transcriptional regulation and chromatin remodeling, with particular interest in its roles in cell differentiation and gene expression modulation. The 31-50 region encompasses a segment that may participate in protein-protein interactions or serve as an antigenic determinant, making it a valuable tool for dissecting molecular mechanisms associated with SSX4 biology. Researchers utilize such well-defined peptide fragments to probe structure-function relationships, develop analytical assays, and investigate post-translational modifications within the context of cancer biology and epigenetic regulation.

Epitope mapping: Synthetic peptides derived from defined regions of proteins, such as the 31-50 sequence of SSX4, are widely employed in epitope mapping studies. By providing a discrete segment of the parent protein, this peptide enables researchers to identify linear antibody-binding sites, facilitating the characterization of immune responses or the development of highly specific monoclonal antibodies. Its utility extends to the validation of antibody specificity and the fine mapping of B-cell or T-cell epitopes, which are essential steps in immunological research and assay development.

Protein-protein interaction analysis: The SSX4 (31-50) peptide can serve as a molecular probe in studies aimed at elucidating interaction interfaces within multiprotein complexes. By incorporating this fragment into binding assays, pull-down experiments, or surface plasmon resonance analyses, scientists can investigate how this region contributes to the recruitment of cofactors, chromatin modifiers, or other regulatory proteins. Such studies are instrumental in clarifying the functional domains of SSX4 and their roles in transcriptional repression or activation.

Post-translational modification research: Defined peptide fragments are often used as substrates for in vitro modification assays, enabling the investigation of site-specific phosphorylation, acetylation, or methylation events. The SSX4 (31-50) sequence may harbor potential modification sites, allowing researchers to examine the enzymatic activity of kinases, acetyltransferases, or methyltransferases that target this region. These experiments contribute to a deeper understanding of how post-translational modifications influence SSX4 function and its regulatory capacity in chromatin dynamics.

Assay development and standardization: The availability of a synthetic SSX4 (31-50) peptide facilitates the creation of quantitative and qualitative analytical assays. It can be used as a reference standard or positive control in enzyme-linked immunosorbent assays (ELISA), Western blotting, or mass spectrometry-based workflows. Such applications are crucial for assay calibration, validation, and reproducibility, particularly when studying SSX4 expression patterns or screening for interacting partners in complex biological samples.

Peptide-based functional studies: Researchers employ peptide fragments like SSX4 (31-50) to explore the minimal functional domains required for biological activity. By introducing this sequence into cell-based assays or in vitro systems, it is possible to assess its capacity to modulate gene expression, interfere with endogenous protein interactions, or act as a competitive inhibitor. These studies provide valuable insights into the mechanistic roles of discrete SSX4 regions and support the rational design of further functional analyses or molecular tools.

1. Constitutive and inflammation-dependent antimicrobial peptides produced by epithelium are differentially processed and inactivated by the commensal Finegoldia magna and the pathogen Streptococcus pyogenes

2. Store-operated Ca2+ entry sustains the fertilization Ca2+ signal in pig eggs

3. Odorant binding protein based biomimetic sensors for detection of alcohols associated with Salmonella contamination in packaged beef

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

5. cRGD-functionalized, DOX-conjugated, and 64Cu-labeled superparamagnetic iron oxide nanoparticles for targeted anticancer drug delivery and PET/MR imaging