BTK-IN-50
BTK-IN-50 is a covalent BTK inhibitor with an IC50 of 6 nM. BTK-IN-50 blocks collagen-induced platelet aggregation by inhibiting the GPVI-mediated BTK-PLCγ2-PKC signaling cascade, and attenuates CRP-XL-induced phosphorylation of BTK, PLCγ2 and PKC substrates in platelets. BTK-IN-50 can be used for research related to thrombosis.
For research use only. We do not sell to patients.
- Formula: C25H24ClN5O5
- Molecular Weight:509.94
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Storage:
Please store the product under the recommended conditions in the Certificate of Analysis.
Biological Activity
Description
In Vitro
BTK-IN-50 (19b) acts as a covalent inhibitor of wild-type BTK with an IC50 of 6 nM, and its activity is predominantly dependent on covalent bond formation with BTK's Cys481 residue[1].
BTK-IN-50 (19b) potently inhibits collagen-induced aggregation of human platelets with an IC50 of 16 nM[1].
BTK-IN-50 (19b) (3-30 nM; 15 min preincubation) dose-dependently inhibits the GPVI-mediated BTK-PLCγ2-PKC signaling cascade in washed human platelets at concentrations of 3 nM, 10 nM, and 30 nM[1].
MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only. Further protocols information, click here.
Chemical Information
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Molecular Weight 509.94
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Formula C25H24ClN5O5
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SMILES
NC1=NC=NC2=C1C(C3=CC=C(OC4=CC=CC=C4)C=C3)=CN2[C@H]5[C@H](O)[C@H](O)[C@H](CNC(CCl)=O)O5
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Shipping
Room temperature in continental US; may vary elsewhere.
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Storage
Please store the product under the recommended conditions in the Certificate of Analysis.
Protocols
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Kinase activity and phosphorylation assays
Kinase activity assays measure the ability of kinases to transfer phosphate groups from ATP to specific substrates, while phosphorylation assays detect the presence and levels of phosphorylated proteins. Common methods include radiolabeled ATP incorporation (e. g. ,), ADP release detection via bioluminescence (e. g. ,[3]), enzyme-linked immunosorbent assays (ELISA) for phospho-specific epitopes (e. g. ,[6]), and microtiter-based formats for high-throughput screening (e. g. ,[8]). The ADP-Glo assay quantifies kinase activity by measuring ADP produced during phosphorylation using a luciferase-based system. Radiometric assays involve autoradiography or scintillation counting after incorporation of 32P-labeled ATP into substrate proteins. ELISA-based approaches rely on phospho-specific antibodies to detect activated kinases in cell lysates or purified samples.
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Western Blot
Western blotting (WB) is a commonly used experimental method in molecular biology, biochemistry, and immunogenetics for identifying and quantifying target proteins. It combines gel electrophoresis with immunoassay, enabling researchers to analyze protein expression, post-translational modifications, and molecular weight.
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Cell Cytotoxicity Assay
Cytotoxicity assays are usually based on the assessment of cell membrane damage, which can also be indirectly detected by measuring cell viability. Detection methods include MTT assay, CKK-8 assay, LDH assay and ATP assay, etc.
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Protocol for Kinase activity and phosphorylation assays
Kinase activity assays measure transfer of phosphate from ATP to a protein or peptide substrate, generating phosphorylated substrate, ADP, or incorporated radiolabeled phosphate as the readout; phosphorylation assays measure site-specific phosphorylation in cells or tissues as a proxy for kinase-pathway activation, inhibition, or substrate regulation. Phosphorylation can be detected by phospho-specific Western blot, immunoprecipitation kinase assay, phospho-immunofluorescence, phospho-flow cytometry, luminescent ADP detection, radiolabeled ATP incorporation, or reporter-based pathway assays, and these readouts can be applied to cancer cells, primary neurons, mouse tumors, organoids, inflammatory macrophages, ferroptosis studies, and mitophagy studies when the kinase target is biologically relevant.
Purity & Documentation
References
Calculators
Concentration (start) × Volume (start) = Concentration (final) × Volume (final)