Murine Survivin (20-28)

Murine Survivin; Baculoviral IAP repeat-containing protein 5

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

CAT No: ta-578

Synonyms/Alias:Murine Survivin (20-28); Baculoviral IAP repeat-containing protein 5 (20-28)

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

Murine Survivin (20-28) is a synthetic peptide fragment derived from the mouse survivin protein, encompassing amino acid residues 20 through 28 of the full-length sequence. As a member of the inhibitor of apoptosis (IAP) family, survivin plays a pivotal role in the regulation of cell division and inhibition of programmed cell death, making it a significant target in cancer biology and immunological research. The 20-28 region of murine survivin has been identified as an immunodominant epitope, frequently studied for its capacity to stimulate antigen-specific T cell responses. Its defined sequence and immunological relevance have positioned this peptide as a valuable tool in molecular immunology, tumor immunogenicity investigations, and the development of peptide-based research reagents.

Immunological Assays: The peptide corresponding to murine survivin residues 20-28 is extensively utilized in immunological assays aimed at characterizing T cell responses. In particular, it serves as a model antigen for studying CD8+ cytotoxic T lymphocyte (CTL) activation in murine systems. By incorporating this sequence into in vitro assays such as ELISPOT, intracellular cytokine staining, or tetramer staining, researchers can quantitatively assess antigen-specific T cell populations, facilitating the evaluation of immune recognition mechanisms and the identification of immunodominant epitopes in preclinical models.

Tumor Immunogenicity Studies: The defined epitope represented by the 20-28 fragment is frequently employed in research focusing on tumor immunogenicity and immune surveillance. Its sequence is often used to pulse antigen-presenting cells or to generate peptide-loaded dendritic cells, enabling the investigation of tumor-associated antigen processing and presentation. This approach supports the elucidation of the molecular interactions between tumor cells and the immune system, providing insight into the mechanisms underlying tumor immune escape and the potential for immunotherapeutic targeting.

Vaccine Development Research: The immunogenic properties of the survivin 20-28 region have made it an important candidate for experimental peptide vaccine studies in murine models. When used as an immunogen, the peptide can help evaluate the efficacy of adjuvants, delivery systems, and immunization protocols in eliciting robust, antigen-specific cellular immune responses. Such studies are instrumental in advancing the design and optimization of peptide-based vaccine strategies targeting intracellular tumor antigens.

Epitope Mapping and Validation: The precise sequence of murine survivin (20-28) enables its use in epitope mapping experiments, where it serves as a reference standard for identifying and validating T cell epitopes within the survivin protein. By comparing immune responses to overlapping peptide libraries, researchers can delineate the minimal epitope necessary for T cell recognition, supporting the rational design of immunological assays and the development of targeted research reagents.

Peptide-MHC Binding Studies: The 20-28 peptide is also valuable in studies investigating peptide-MHC class I interactions. Its well-characterized binding properties allow researchers to analyze the affinity and stability of peptide-MHC complexes, which are critical for effective antigen presentation and T cell activation. These investigations contribute to a deeper understanding of antigen processing pathways and inform the selection of optimal peptides for immunological research and experimental model development.

Source#
Mus musculus (Mouse)
Epitope
20-28
Restricting HLA
H-2Db
References
A Lladser; Cancer immunology 2010

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