A fluorogenic peptide substrate that can be used to monitor 20S Immunoproteasome activity, which is excited at 345 nm and emits at 445 nm. This substrate is specific to the immunoproteasome, and is not hydrolyzed efficiently by the constitutive proteasome.
CAT No: R1032
CAS No:163515-35-3
Synonyms/Alias:Chlorotoxin;163515-35-3;Chlorotoxin TFA;PCN-4282-V;AS-82547;DA-51860;H-DL-Met-DL-Cys(1)-DL-Met-DL-Pro-DL-Cys(2)-DL-Phe-DL-xiThr-DL-xiThr-DL-Asp-DL-His-DL-Gln-DL-Met-DL-Ala-DL-Arg-DL-Lys-DL-Cys(3)-DL-Asp-DL-Asp-DL-Cys(1)-DL-Cys(4)-Gly-Gly-DL-Lys-Gly-DL-Arg-Gly-DL-Lys-DL-Cys(2)-DL-Tyr-Gly-DL-Pro-DL-Gln-DL-Cys(3)-DL-Leu-DL-Cys(4)-DL-Arg-NH2;Met-Cys-Met-Pro-Cys-Phe-Thr-Thr-Asp-His-Gln-Met-Ala-Arg-Lys-Cys-Asp-Asp-Cys-Cys-Gly-Gly-Lys-Gly-Arg-Gly-Lys-Cys-Tyr-Gly-Pro-Gln-Cys- Leu-Cys-Arg-NH2;
Chlorotoxin is a peptide toxin originally isolated from the venom of the deathstalker scorpion, well known for its unique ability to selectively interact with certain chloride channels and matrix metalloproteinases. As a disulfide-rich peptide comprising 36 amino acids, it displays remarkable specificity for glioma and other tumor cell types, making it a valuable molecular tool in neurobiology and oncology research. The structural stability and high binding affinity of chlorotoxin for particular cellular targets have established it as a prominent agent for probing cellular ion channel function, tumor biology, and molecular imaging applications in a variety of experimental settings.
Ion channel research: Chlorotoxin is widely utilized as a selective probe for the study of voltage-gated chloride channels, particularly those expressed in neuronal and glial cells. Its high affinity and specificity enable researchers to dissect the physiological roles of chloride channels in maintaining cellular homeostasis, neurotransmission, and signal transduction. The peptide's ability to inhibit chloride conductance provides critical insight into the mechanisms underlying neuronal excitability and the modulation of synaptic activity, supporting fundamental investigations in neurophysiology.
Tumor marker identification: The preferential binding of chlorotoxin to matrix metalloproteinase-2 (MMP-2) and certain chloride channels overexpressed in malignant gliomas and other tumor cells underpins its use in tumor marker research. By conjugating the peptide to fluorescent or radiolabeled tags, investigators can visualize and map the distribution of tumor-specific biomarkers in vitro and in vivo. This application is instrumental in advancing the understanding of tumor microenvironments and the molecular signatures associated with cancer progression.
Targeted molecular imaging: Due to its selective affinity for tumor cells, chlorotoxin serves as a targeting ligand in the development of advanced molecular imaging agents. When linked to imaging probes such as near-infrared dyes or nanoparticles, it enables sensitive detection and delineation of tumor margins in preclinical models. This approach supports the refinement of imaging modalities, contributing to improved accuracy in tumor localization, surgical planning, and the evaluation of novel diagnostic strategies.
Drug delivery system development: The high specificity of chlorotoxin for certain cancer cell types has inspired its integration into targeted drug delivery platforms. By coupling the peptide to therapeutic payloads, researchers can enhance the selective delivery of drugs to tumor cells while minimizing off-target effects. This strategy is particularly valuable in the design and optimization of nanoparticle-based delivery systems, facilitating the study of targeted therapeutic approaches and the assessment of delivery efficiency in experimental oncology.
Peptide engineering and structure-function analysis: Chlorotoxin's well-defined structure, stability, and target selectivity make it a model system for peptide engineering and structure-activity relationship studies. Researchers employ the peptide as a scaffold for the design of novel analogs with altered binding properties or enhanced functional characteristics. Investigations into its disulfide bonding patterns, folding kinetics, and receptor interactions contribute to the broader field of peptide therapeutics and the rational development of bioactive molecules for research applications.
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