Wilms tumor protein (332-347)

Wilms tumor protein (332-347) is a synthetic peptide fragment derived from the Wilms tumor protein, a transcription factor critically involved in kidney development and oncogenesis. This specific peptide segment corresponds to amino acid residues 332 to 347 within the WT1 protein, a region implicated in DNA-binding and regulatory functions. Its sequence is frequently studied in the context of tumor biology, immunology, and molecular recognition due to its relevance in both normal developmental processes and tumor-associated pathways. As a research reagent, this peptide offers a defined tool for dissecting protein-protein and protein-DNA interactions, as well as for investigating antigenic epitopes relevant to immune recognition.

Epitope mapping: The 332-347 fragment of the Wilms tumor protein is widely employed in epitope mapping studies to delineate antigenic determinants recognized by antibodies or T cell receptors. Researchers utilize this peptide to identify and characterize immunodominant regions within the WT1 protein, enhancing the understanding of immune surveillance mechanisms in the context of tumorigenesis. Such studies inform the development of immunological assays and contribute to the rational design of peptide-based probes for WT1 detection.

Immunogenicity assessment: In immunological research, this peptide serves as a defined antigen for evaluating T cell responses and antibody generation in vitro. By incorporating the 332-347 sequence into assays such as ELISPOT or intracellular cytokine staining, scientists can quantify and analyze cellular immune responses specific to WT1-derived epitopes. These applications are fundamental in elucidating the immunological relevance of WT1 in various biological and pathological contexts, including tumor immunology and autoimmunity.

Protein interaction studies: The peptide is also utilized as a molecular probe to investigate the binding preferences and specificity of WT1-interacting partners. By providing a discrete segment of the protein, researchers can examine how this region contributes to the formation of complexes with nucleic acids or regulatory proteins. Such studies are essential for mapping functional domains within WT1 and for understanding the molecular mechanisms underlying its activity as a transcription factor.

Assay development: The defined sequence and high specificity of the 332-347 peptide make it an ideal standard or control in the development and validation of biochemical assays targeting WT1. Its use facilitates the optimization of assay conditions, calibration of detection systems, and benchmarking of antibody reagents. This contributes to the reproducibility and reliability of experimental data in both basic and applied research settings.

Peptide modification research: The Wilms tumor protein (332-347) fragment provides a tractable template for exploring the effects of amino acid substitutions, post-translational modifications, or conjugation strategies. Researchers employ this peptide to systematically investigate how specific changes impact structure, stability, or recognition by biological targets. Insights gained from such studies advance the design of modified peptides with tailored properties for research and diagnostic applications.

1. Low bone turnover and low BMD in Down syndrome: effect of intermittent PTH treatment

2. C-peptide and its C-terminal fragments improve erythrocyte deformability in type 1 diabetes patients

3. Investigating Potential Interactions Between Neurohypophyseal Peptides, their Drug Analogs, and Coagulation Factor VIII

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

5. An Isolated TCR αβ Restricted by HLA-A* 02: 01/CT37 Peptide Redirecting CD8+ T Cells to Kill and Secrete IFN-γ in Response to Lung Adenocarcinoma Cell Lines