Ankyrin repeat domain-containing protein 11 (421-433)

Ankyrin repeat domain-containing protein 11

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.

CAT No: ta-132

Synonyms/Alias:Ankyrin repeat domain-containing protein 11 (421-433)

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Sequence
GTGEKLRLSAHTI
Areas of Interest
Antigen-presenting Cells; Cancer Research

Ankyrin repeat domain-containing protein 11 (421-433) is a synthetic peptide fragment corresponding to residues 421 through 433 of the human ANKRD11 protein. As a segment derived from a protein characterized by multiple ankyrin repeat motifs, this peptide is of significant interest in the study of protein-protein interactions, transcriptional regulation, and chromatin remodeling processes. The ANKRD11 protein itself is implicated in diverse cellular pathways, particularly those governing gene expression and epigenetic modification, making its peptide derivatives valuable molecular tools for dissecting functional domains and interaction sites. Researchers utilize this peptide as a precise probe to map the biological roles of ankyrin repeat-containing regions and to elucidate mechanisms underlying protein complex assembly and signaling networks.

Protein interaction mapping: The 421-433 peptide segment serves as a specialized reagent for investigating the binding partners of ANKRD11 and related ankyrin repeat proteins. By acting as a competitive inhibitor or affinity probe in pull-down assays and immunoprecipitation experiments, the peptide facilitates identification of specific protein interaction motifs. This approach enables researchers to characterize the molecular determinants of complex formation and to delineate the structural basis for selective recognition within the ankyrin repeat domain, advancing understanding of how these motifs mediate cellular signaling and scaffold assembly.

Epigenetic regulation studies: ANKRD11 is known for its involvement in chromatin remodeling and transcriptional repression. The 421-433 peptide fragment can be employed in mechanistic studies to interrogate the contribution of discrete ankyrin repeat sequences to epigenetic regulatory functions. Incorporating this peptide into in vitro assays allows researchers to assess its impact on chromatin-binding proteins, histone modifiers, or transcriptional co-regulators, shedding light on the modular architecture of transcriptional control and the role of ankyrin repeats in gene silencing or activation.

Antibody development and validation: Synthetic peptides derived from defined regions of proteins, such as the 421-433 sequence of ANKRD11, are frequently used as immunogens for generating sequence-specific antibodies. These antibodies are essential for the selective detection of endogenous ANKRD11 or its post-translationally modified forms in cellular and tissue samples. The peptide also serves as a reliable standard for evaluating antibody specificity and affinity in immunoassays, thereby supporting the development of robust reagents for molecular and cell biology research.

Peptide-based functional assays: The defined sequence of the 421-433 peptide enables its use in functional assays aimed at dissecting the biological activity of ankyrin repeat motifs. Researchers may use this peptide to screen for small molecules or proteins that interact with the ankyrin repeat domain, facilitating the discovery of modulators or inhibitors of ANKRD11 function. Such assays are instrumental in unraveling the contribution of specific sequence elements to protein stability, localization, and regulatory capacity within the cell.

Structural and biophysical analysis: The 421-433 peptide provides a tractable model for structural studies of ankyrin repeat domains. Its defined length and sequence make it suitable for high-resolution techniques such as nuclear magnetic resonance (NMR) spectroscopy, circular dichroism (CD), or molecular dynamics simulations. These studies yield insights into the secondary structure, conformational dynamics, and interaction surfaces of ankyrin repeat regions, informing broader efforts to model protein folding, domain organization, and the structural determinants of protein-protein recognition in cellular signaling pathways.

Source#
Homo sapiens (human)
Epitope
421-433
Restricting HLA
HLA-A2
References
Kwasi Antwi; Mol Immunol 2009

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