Wilms tumor protein (337-347)

Wilms tumor protein (337-347) is a synthetic peptide fragment corresponding to amino acids 337 through 347 of the Wilms tumor protein, a transcription factor critically involved in cellular growth and differentiation. This peptide segment is derived from the WT1 protein, which plays a pivotal role in the regulation of gene expression during embryonic development and has garnered significant attention in cancer biology, particularly in the context of Wilms tumor and other malignancies. Its defined sequence and biochemical properties make it a valuable tool for probing the molecular functions of WT1, as well as for developing and validating experimental assays related to peptide-protein interactions, immunological recognition, and post-translational modification studies.

Epitope mapping: Researchers frequently utilize this peptide fragment to investigate the immunogenic epitopes of the WT1 protein. By employing it in binding assays or as an antigen in immunological studies, scientists can identify antibody recognition sites and characterize T-cell responses against WT1. Such applications are crucial in understanding immune surveillance mechanisms in oncogenesis and in the design of peptide-based immunoassays for basic and translational research.

Peptide-protein interaction studies: The 337-347 segment serves as a defined probe for dissecting protein-protein or peptide-protein interactions involving WT1. Its use in affinity binding assays, pull-down experiments, or surface plasmon resonance analyses aids in elucidating the molecular partners and interaction domains that regulate WT1's functional activity. These insights are essential for mapping signaling pathways and identifying potential modulators of WT1-associated cellular processes.

Phosphorylation and post-translational modification analysis: As a synthetic peptide corresponding to a specific region of WT1, this fragment is well-suited for in vitro studies of post-translational modifications, such as phosphorylation. Researchers can employ it as a substrate in kinase assays or mass spectrometry workflows to investigate modification patterns, enzyme specificity, and regulatory mechanisms affecting WT1 function. Such studies deepen the understanding of how post-translational events influence protein activity and stability.

Analytical assay development: The defined sequence and high specificity of the WT1 (337-347) peptide enable its use in the development and validation of analytical assays, including ELISA, western blot, and mass spectrometry-based detection methods. It can serve as a calibration standard or a positive control, supporting the quantification and identification of WT1 or related peptides in complex biological samples. This facilitates robust assay performance and reproducibility in research and quality control environments.

Peptide synthesis and method optimization: Laboratories engaged in peptide chemistry and analytical method development often employ this WT1 fragment as a model substrate. Its use assists in optimizing solid-phase peptide synthesis protocols, purification strategies, and analytical techniques such as HPLC or LC-MS. Working with a well-characterized peptide like WT1 (337-347) supports process validation and the establishment of reliable workflows for broader peptide research applications.

1. Extended exenatide administration enhances lipid metabolism and exacerbates pancreatic injury in mice on a high fat, high carbohydrate diet

2. Effect of Short-Term Desiccation, Recovery Time, and CAPA-PVK Neuropeptide on the Immune System of the Burying Beetle Nicrophorus vespilloides

3. Genetic, cellular, and structural characterization of the membrane potential-dependent cell-penetrating peptide translocation pore

4. The effect of sex on immune responses to a homocitrullinated peptide in the DR4-transgenic mouse model of Rheumatoid Arthritis

5. Myotropic activity and immunolocalization of selected neuropeptides of the burying beetle Nicrophorus vespilloides (Coleoptera: Silphidae)