Baculoviral IAP repeat-containing protein 5 (95-104)

Baculoviral IAP repeat-containing protein 5 (95-104) is a synthetic peptide fragment derived from the inhibitor of apoptosis protein (IAP) family, specifically from the sequence corresponding to amino acids 95 through 104 of BIRC5, also known as survivin. As a peptide compound, it represents a biologically relevant motif from a protein recognized for its roles in cell cycle regulation, apoptosis inhibition, and mitotic progression. The availability of this defined peptide segment enables researchers to dissect the structure-function relationships of survivin, investigate post-translational modifications, and explore protein-protein interactions critical to cellular survival pathways. Its defined sequence and origin make it a valuable tool for mechanistic studies in cell biology, molecular signaling, and peptide-based assay development.

Peptide mapping: The peptide corresponding to residues 95-104 of BIRC5 is frequently utilized in peptide mapping experiments to identify and characterize the functional domains of survivin. By isolating this specific region, researchers can map antibody epitopes, determine the accessibility of sequence motifs, and study the peptide's involvement in protein-protein interactions. This approach is particularly important for elucidating the role of the C-terminal region in survivin's anti-apoptotic activity and its interactions with cellular partners.

Antibody generation and validation: As a synthetic epitope, the 95-104 peptide fragment serves as an ideal antigen for the generation of sequence-specific antibodies against survivin. These antibodies are instrumental in immunoassays such as Western blotting, immunoprecipitation, and immunohistochemistry, enabling precise detection and quantification of the native protein in complex biological samples. The use of a defined peptide antigen ensures high specificity, reducing cross-reactivity with related IAP family members and facilitating studies of survivin expression dynamics.

Protein interaction studies: The defined sequence of the 95-104 peptide allows for detailed investigation of survivin's binding partners and interaction motifs. By employing peptide pull-down assays or surface plasmon resonance, researchers can assess the affinity and specificity of interactions between this region and regulatory proteins, small molecules, or post-translational modifiers. Such studies help clarify the molecular mechanisms underlying survivin's functional roles in cell survival and division, supporting the development of targeted modulators for research applications.

Phosphorylation analysis: The 95-104 region of survivin encompasses potential phosphorylation sites, making the synthetic peptide an effective substrate for in vitro kinase assays. Researchers can use the peptide to characterize kinase specificity, monitor phosphorylation kinetics, and assess the impact of post-translational modifications on survivin function. These studies provide insights into the regulation of survivin activity during the cell cycle and in response to cellular stress, contributing to a deeper understanding of cell fate decisions.

Peptide-based assay development: The defined sequence and biochemical relevance of the 95-104 peptide enable its use in the development and optimization of peptide-based assays. These assays, such as enzyme-linked immunosorbent assays (ELISA) or competitive binding formats, can be tailored for the detection of survivin, the quantification of antibody responses, or the screening of potential interaction inhibitors. Such applications support both basic research and high-throughput screening efforts, facilitating the discovery of novel modulators and advancing the study of apoptosis regulation at the molecular level.

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