ZIP with a biotin moiety covalently attached that effectively binds to avidins (Kd = 4 x 10-14 M). It mediates detection of ZIP in biochemical assays.
CAT No: R0904
Synonyms/Alias:z-Pseudosubstrate inhibitory peptide, biotinylated
ZIP, Biotinylated, is a synthetic peptide derivative that incorporates a biotin moiety for enhanced detection and affinity applications in biochemical research. As a modified peptide, it is structurally designed to mimic the zeta inhibitory peptide (ZIP), which is widely recognized for its role in modulating protein kinase M zeta (PKMζ) activity. The addition of a biotin tag facilitates downstream processes such as affinity capture, visualization, and quantification, making it a versatile tool in both molecular and cellular studies. Its unique combination of sequence specificity and biotinylation expands its utility across a range of experimental platforms, supporting advanced investigations into protein-protein interactions, signal transduction mechanisms, and peptide-based assay development.
Affinity Purification: The biotinylated form of ZIP enables efficient affinity purification workflows, leveraging the strong interaction between biotin and streptavidin or avidin-conjugated supports. Researchers can use this peptide to selectively isolate binding partners or interacting proteins from complex biological mixtures. This approach is particularly valuable for mapping protein interaction networks or identifying novel regulatory factors involved in PKMζ-associated signaling pathways, as the biotin tag ensures high specificity and minimal non-specific binding during pull-down assays.
Protein-Protein Interaction Studies: In studies focused on elucidating the molecular mechanisms of signal transduction, the biotinylated peptide serves as a robust probe for detecting and characterizing protein-protein interactions. By immobilizing the tagged peptide on streptavidin-coated surfaces, investigators can assess the binding affinity and specificity of candidate proteins or protein complexes. This application is instrumental in dissecting the functional roles of PKMζ and related signaling molecules, providing insights into the dynamics of synaptic plasticity and memory-related processes at the molecular level.
Detection and Quantification: The biotin label on ZIP allows for sensitive detection and quantification in a variety of assay formats, including ELISA, Western blotting, and fluorescence-based systems. Utilizing streptavidin-conjugated reporters, researchers can visualize the presence and distribution of the peptide or its interacting partners with high precision. This capability supports rigorous validation of experimental results, enabling reproducible quantification of peptide binding events and facilitating the development of high-throughput screening assays for modulators of PKMζ activity.
Peptide Functional Studies: The biotinylated ZIP peptide is frequently employed in functional assays aimed at probing the biological activity of PKMζ and related kinases. By introducing the modified peptide into cellular or in vitro systems, researchers can assess its impact on kinase signaling, phosphorylation events, or downstream gene expression. The biotin tag not only aids in tracking the peptide's localization and uptake but also allows for subsequent recovery and analysis, supporting comprehensive studies of kinase inhibition and signal transduction modulation.
Peptide Synthesis and Assay Development: The availability of ZIP in a biotinylated format streamlines the design and optimization of novel peptide-based assays. Its well-characterized sequence and functional tag make it an ideal standard or control in method development, calibration, and validation procedures. Researchers developing new detection platforms or screening assays for kinase modulators can leverage the biotinylated peptide's robust performance and compatibility with a wide range of analytical technologies, enhancing both assay sensitivity and reproducibility.
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