CD20 (188-196)

CD20 (188-196) is a synthetic peptide fragment corresponding to amino acid residues 188 through 196 of the human CD20 protein, an integral membrane phosphoprotein predominantly expressed on the surface of B lymphocytes. As a highly specific epitope, this peptide serves as a valuable molecular tool in immunological and biochemical studies focused on B-cell biology and CD20-related signaling pathways. Its sequence specificity allows researchers to investigate the structural and functional aspects of CD20, which is fundamental to understanding B-cell maturation, activation, and immune response regulation. The availability of this defined peptide fragment enables precise experimental design in both basic and translational research settings.

Epitope mapping: The CD20 (188-196) peptide is widely employed in epitope mapping studies to identify antibody recognition sites within the CD20 protein. By using this peptide in immunoassays or peptide array platforms, researchers can assess the binding specificity of monoclonal or polyclonal antibodies directed against CD20. This approach is instrumental in characterizing immune responses, validating antibody reagents, and supporting the development of novel B-cell targeting strategies in laboratory settings.

Antibody production and validation: As an immunogenic peptide sequence, CD20 (188-196) can be conjugated to carrier proteins and used as an antigen for generating sequence-specific antibodies in animal models. The resulting antibodies are subsequently validated using the same peptide in ELISA, Western blot, or immunoprecipitation assays, ensuring their specificity for the targeted CD20 region. Such reagents are essential for dissecting CD20 expression patterns and for use in downstream immunological assays.

Functional studies of B-cell signaling: The defined sequence of this peptide allows for the dissection of CD20-mediated signaling mechanisms in B lymphocytes. By introducing the peptide into cell-based assays or biochemical systems, researchers can investigate its role in modulating protein-protein interactions, receptor clustering, or downstream phosphorylation events. These studies advance the understanding of CD20's contribution to B-cell physiology and its potential as a molecular switch in immune signaling cascades.

Competitive binding assays: CD20 (188-196) serves as a useful competitor in binding assays designed to evaluate the affinity and specificity of anti-CD20 antibodies or ligands. By competing with the native CD20 protein for antibody binding, the peptide helps determine binding kinetics and epitope accessibility. Such assays are critical for optimizing antibody-based detection systems and for screening candidate molecules that interact with the CD20 extracellular domain.

Peptide-based assay development: The availability of a well-characterized CD20 peptide fragment supports the development of robust immunoassays, such as peptide ELISAs, for the quantification and monitoring of antibody responses or for screening hybridoma supernatants. Incorporating this peptide into assay platforms enhances analytical precision and reproducibility, facilitating high-throughput screening and quality control in research and antibody production workflows.

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

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

3. Immune responses to peptides containing homocitrulline or citrulline in the DR4-transgenic mouse model of rheumatoid arthritis

4. Proinsulin C-peptide and insulin: Limited pattern similarities of interest in inter-peptide interactions but no C-peptide effect on insulin and IGF-1 receptor signaling

5. Tachykinin-related peptides modulate immune-gene expression in the mealworm beetle Tenebrio molitor L