Biotinyl-Prion Protein (106-126) (human) is a biotin-tagged prion protein peptide corresponding to residues 106-126 of the human sequence, placing it in the class of peptide fragments used for chemical biology and protein-interaction studies. The molecule contains the peptide backbone with side chains derived from the specified amino acid sequence, and the biotinyl modification provides a pendant affinity handle while the terminal amino and carboxyl groups remain those of the peptide fragment as supplied. In research workflows, this labeled peptide is employed as a defined substrate or probe for binding assays, pull-down experiments, and analytical detection methods where the biotin tag enables immobilization or enrichment of the peptide-target complexes.
CAT No: CP10905
Biotinyl-Prion Protein (106-126) (human) is a biotin-tagged prion protein fragment corresponding to residues 106-126 of the human sequence, designed for affinity-based capture and downstream detection in chemical biology workflows. This peptide format combines a defined linear epitope region with a biotin handle that supports streptavidin/avidin binding, enabling robust pull-down, immobilization, and assay readouts. Researchers typically use this construct as a sequence-specific reagent for studying prion-related protein interactions, peptide binding behavior, and assay development where controlled presentation of the biotinylated fragment is advantageous.
1. Streptavidin Pull-Down Assays
Biotinyl-Prion Protein (106-126) (human) is used to enable affinity capture of the peptide and associated binding partners via streptavidin or avidin systems in protein-peptide interaction studies. In practice, it supports pull-down experiments where the biotin tag provides strong, noncovalent attachment to beads or surfaces, allowing researchers to enrich for candidate interacting proteins from complex lysates or purified binding mixtures. This format is particularly useful when the experimental design benefits from a consistent immobilization geometry and a straightforward workflow for washing and enrichment prior to LC-MS/MS identification or immunoblot analysis.
2. Immobilized Binding and Screening
Biotinyl-Prion Protein (106-126) (human) is commonly applied in immobilized assay formats, including surface-based binding studies and peptide screening workflows where the peptide must be presented at a defined location on a streptavidin-coated platform. By using the biotin handle for surface attachment, teams can compare binding behavior across conditions such as buffer composition, ionic strength, or candidate ligands while keeping the peptide tethering strategy consistent. This approach is frequently adopted in chemical biology and protein interaction research to generate reproducible binding curves and to support iterative optimization of binding reagents.
3. Chemical Biology Interaction Probing
Biotinyl-Prion Protein (106-126) (human) serves as a sequence-specific probe for mapping interaction interfaces and validating binding specificity in prion protein-related research. The biotin tag enables convenient recovery of the peptide-partner complex for downstream characterization, including targeted analysis of co-enriched proteins or confirmation of interaction trends across experimental variants. Because the reagent is a defined fragment rather than a full-length protein, it is often selected to focus on the behavior of the 106-126 region while maintaining compatibility with peptide-centric assay designs.
4. Proteomics and Target Enrichment Reagents
Biotinyl-Prion Protein (106-126) (human) is used as an enrichment reagent in workflows that combine peptide capture with mass spectrometry or other analytical readouts. Researchers leverage the biotin-streptavidin interaction to isolate peptide-associated species from mixtures, improving the practicality of downstream detection and characterization. This application is especially relevant when the goal is to identify co-purifying components, assess relative enrichment across conditions, or support method development for sample preparation steps that rely on affinity capture.
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