H10, Biotinylated carries a functional peptide motif covalently linked to biotin, enabling high-affinity capture on streptavidin matrices. The construct permits controlled orientation in pull-down, ELISA, or imaging assays. Researchers exploit the tag to study protein-peptide interactions and complex formation. Applications include affinity purification, interaction screening, and biosensor development.
CAT No: R2744
H10, biotinylated, is a synthetic peptide conjugated with biotin at a specific site, designed to facilitate high-affinity binding interactions with avidin or streptavidin-based reagents. As a biotinylated peptide, it combines the functional specificity of its amino acid sequence with the versatile affinity tag properties of biotin, enabling robust and selective capture, detection, or immobilization in a variety of biochemical and molecular biology workflows. The unique structure of H10 allows researchers to exploit both its peptide-driven biological activity and the strong biotin-streptavidin interaction, making it a valuable tool for diverse experimental applications in protein interaction studies, assay development, and advanced analytical techniques.
Affinity purification: In biochemical research, biotinylated H10 is widely employed for affinity purification protocols. The biotin tag enables the peptide to be efficiently captured by streptavidin- or avidin-coated matrices, allowing for the targeted isolation of interacting proteins, peptides, or other biomolecules from complex mixtures. This approach is particularly advantageous for pull-down assays, where the immobilized peptide serves as bait to selectively enrich binding partners, facilitating downstream identification and characterization by mass spectrometry or immunodetection.
Protein-protein interaction studies: The conjugation of biotin to H10 enhances its utility in mapping protein-protein interactions. By immobilizing the peptide on streptavidin-coated surfaces, researchers can create a controlled environment to probe specific binding events with candidate proteins, antibodies, or cellular extracts. This strategy is instrumental in elucidating signaling pathways, mapping binding domains, and validating molecular interactions under physiologically relevant conditions, contributing to a deeper understanding of cellular mechanisms.
Immunoassay development: Biotinylated peptides such as H10 are integral components in the design of sensitive and specific immunoassays, including ELISA and multiplex bead-based platforms. The strong affinity between biotin and streptavidin ensures stable and reproducible attachment of the peptide to assay surfaces, improving signal consistency and reducing background noise. This property supports the reliable detection of peptide-specific antibodies, enabling quantitative and qualitative analysis of immune responses, epitope mapping, and biomarker validation in research settings.
Surface plasmon resonance (SPR) and biosensor applications: The biotin modification on H10 allows for its precise and oriented immobilization on streptavidin-functionalized sensor chips, which is essential for SPR and other label-free biosensing technologies. Such immobilization optimizes the accessibility of the peptide's active site, enabling real-time kinetic analysis of binding interactions with analytes of interest. The resulting data provide valuable insights into affinity constants, binding kinetics, and specificity, supporting the rational design of inhibitors, ligands, or therapeutic candidates in early-stage research.
Cellular uptake and localization studies: Researchers utilize biotinylated H10 to investigate peptide internalization pathways and subcellular localization in cultured cells. By exploiting the biotin-streptavidin system in conjunction with fluorescently labeled streptavidin probes, it becomes possible to visualize and track the distribution of the peptide within cellular compartments using advanced imaging techniques. These studies contribute to the understanding of peptide-mediated delivery mechanisms, cellular trafficking, and the intracellular fate of bioactive sequences, informing the development of targeted delivery strategies and functional peptide design.
3. SERS spectrum of the peptide thymosin‐β4 obtained with Ag nanorod substrate
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