SOR-C13 TFA, an extraordinary and highly specialized inhibitor deployed within the biomedical sphere for the purpose of combating cancer, embodies immense potency. Notably designed to single out sorafenib-resistant cells, it amplifies the efficacy of the widely employed sorafenib drug, primarily acclaimed for its profound impact against advanced renal cell carcinoma and liver malignancies.
CAT No: R2011
SOR-C13 TFA is a synthetic peptide compound derived from the C-terminus of soricidin, a natural peptide found in the saliva of the Northern Short-tailed Shrew. Characterized by its unique amino acid sequence and the presence of trifluoroacetate (TFA) as a counterion, SOR-C13 TFA has garnered significant attention in the field of ion channel research, particularly for its high affinity and selectivity toward the TRPV6 calcium channel. Its well-defined structure and bioactivity make it a valuable tool for elucidating the physiological and biochemical roles of TRPV6 in various cellular processes. Researchers utilize this peptide to investigate calcium homeostasis, signal transduction, and the molecular mechanisms underlying calcium-dependent pathways in both basic and applied biochemical studies.
Ion Channel Research: SOR-C13 TFA serves as a highly selective modulator of the TRPV6 calcium channel, allowing researchers to probe the specific functions of this channel in cellular calcium influx. By selectively binding to TRPV6, the peptide enables detailed investigations into ion transport mechanisms, channel gating properties, and the downstream effects of altered calcium entry in diverse cell types. Such studies are critical for advancing the understanding of calcium signaling networks and their roles in cell proliferation, differentiation, and apoptosis.
Peptide-Protein Interaction Studies: The unique sequence and binding properties of SOR-C13 TFA make it an excellent probe for examining peptide-protein interactions, especially those involving membrane-bound ion channels and their regulatory partners. Researchers employ this peptide in binding assays, structural analyses, and mutagenesis experiments to map interaction domains, elucidate conformational changes, and assess the impact of specific residues on functional activity. These studies contribute to a more comprehensive understanding of the molecular determinants governing ion channel modulation.
Calcium Signaling Pathway Analysis: By modulating TRPV6 activity, SOR-C13 TFA provides a powerful means to dissect calcium-dependent signaling pathways in various experimental systems. Its application in cell-based assays and biochemical models enables the selective perturbation of calcium influx, facilitating the analysis of downstream signaling cascades such as those involving calmodulin, kinases, and transcription factors. This targeted approach aids in identifying key nodes within complex signaling networks and enhances the resolution of pathway-specific responses.
Peptide Functional Studies: SOR-C13 TFA is widely utilized in functional assays designed to characterize the bioactivity of peptide modulators in vitro. Its well-defined interaction with TRPV6 allows for precise quantification of channel inhibition or activation, supporting the development of robust assay platforms for screening novel modulators or studying structure-activity relationships. These functional studies provide essential insights into the pharmacological properties and mechanistic basis of peptide-channel interactions.
Analytical and Method Development: The defined biochemical properties of SOR-C13 TFA make it a useful reference standard or positive control in analytical method development for peptide quantification and purity assessment. Researchers leverage its stability and specificity in validating chromatographic, mass spectrometric, and bioanalytical techniques aimed at detecting peptide-based modulators in complex biological matrices. Such applications are essential for ensuring data reliability and reproducibility in peptide research workflows.
2. Adipose tissue is a key organ for the beneficial effects of GLP-2 metabolic function
3. Store-operated Ca2+ entry sustains the fertilization Ca2+ signal in pig eggs
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