Other Homo sapiens (human) protein
Cysteine-rich protein 2 isoform 2 (133-147) is a synthetic peptide fragment derived from the C-terminal region of the CRP2 protein, a member of the LIM domain protein family known for its involvement in cytoskeletal organization and cellular signaling pathways. This peptide encompasses a sequence rich in cysteine residues, which are critical for the formation of disulfide bonds and the stabilization of tertiary protein structures. Researchers utilize this fragment to investigate the structural and functional properties of CRP2, particularly in the context of protein-protein interactions, cellular architecture, and regulatory mechanisms within the cytoplasm. The defined sequence and biochemical features of this peptide make it a valuable tool for elucidating the molecular dynamics of LIM domain-containing proteins and their roles in cellular physiology.
Peptide structure-function analysis: The 133-147 segment of CRP2 serves as an essential model for studying the relationship between primary amino acid sequence and higher-order structural motifs. Its cysteine-rich composition allows researchers to probe the formation and stabilization of disulfide bridges, which are fundamental to the conformational integrity of LIM domain proteins. By incorporating this peptide into biophysical assays such as circular dichroism or NMR, scientists can assess how specific cysteine arrangements influence folding patterns and domain stability, thereby gaining insights into the structural determinants that underpin CRP2 function.
Protein-protein interaction studies: The peptide fragment is frequently employed in affinity-based assays and pull-down experiments to identify and characterize binding partners of CRP2. Its defined sequence enables selective interrogation of interaction interfaces, facilitating the mapping of contact sites between CRP2 and other cytoskeletal or signaling proteins. By immobilizing the peptide on solid supports or using it as a probe in surface plasmon resonance studies, researchers can quantitatively evaluate binding affinities and kinetics, advancing the understanding of CRP2-mediated regulatory complexes.
Antibody generation and epitope mapping: Due to its unique sequence and cysteine content, the 133-147 peptide is an effective immunogen for raising sequence-specific antibodies against CRP2 isoform 2. These antibodies are instrumental in detecting endogenous or recombinant CRP2 in various biochemical and cell biological assays, including western blotting, immunoprecipitation, and immunofluorescence. Additionally, the peptide can be used in epitope mapping studies to define antibody binding sites, thereby supporting the development of highly specific research reagents.
Cell signaling and cytoskeletal research: As a functional domain of CRP2, the 133-147 peptide is utilized to dissect the role of this protein in actin cytoskeleton dynamics and cellular signaling pathways. By introducing the peptide into cultured cells or in vitro reconstitution systems, researchers can investigate its impact on actin filament organization, LIM domain-mediated signaling cascades, and the modulation of cellular architecture. Such studies are vital for understanding how CRP2 contributes to cell shape regulation, migration, and signal transduction.
Peptide synthesis and analytical method development: The well-defined sequence of this cysteine-rich peptide makes it a valuable standard for optimizing solid-phase peptide synthesis protocols, particularly those involving multiple cysteine residues and disulfide bond formation. It is also used in the development and validation of analytical techniques such as HPLC, mass spectrometry, and peptide mapping assays. By serving as a model substrate, the peptide assists in troubleshooting synthetic challenges and refining analytical workflows for complex peptide products.
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