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CBA062  PhosphoDetect™ FAK (pTyr397) ELISA Kit

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01 Juni 2012

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Detects and quantifies the level of FAK (Focal Adhesion Kinase) phosphorylated at Tyr397. FAK is a non-receptor tyrosine kinase that has been implicated in several cell processes including the regulation of cell motility, cell morphology and cell adhesion.
Produktinformationen
Format 96-well plate
Form 96 Tests
Detection method Colorimetric
Species reactivity human, mouse
Unit definition One unit is defined as the amount of FAK (pTyr397) autophosphorylated from 300 pg total FAK.
Sensitivity < 0.9 Units/ml
Assay range 1.6-100 Units/ml
Assay time 4 h
Sample type Cell lysate
Positive control 3T3L1 cells
Kit contains FAK (pTyr397) Standard, Standard Diluent Buffer, FAK Antibody-Coated 96-Well Plate, Rabbit Anti-FAK(pTyr397) Detector Antibody, Goat Anti-Rabbit IgG-HRP Concentrate, HRP Diluent, Wash Buffer Concentrate, TMB, Stop Solution, Plate Covers, and a user protocol.
Lager- und Versandinformationen
Lagerkategorie +2°C to +8°C
Ship Blue Ice Only
Multiple Toxicity Values, refer to MSDS
Canadian export regulations Due to the country and/or U.S. state of origin of the animal material used in this product, this product may not be exported to Canada.
Daten


The sensitivity of this ELISA was compared to immunoblotting using known quantities of FAK (pTyr<sup>397</sup>). The data show that the sensitivity of the ELISA is approximately 4x greater than that of immunoblotting. The bands shown in the immunoblot data were developed using anti-FAK (pTyr<sup>397</sup>) and chemiluminescent detection.

Samples were assayed 48 times times in multiple assays to determine precision between assays.

The specificity of this assay for phosphorylated FAK (Tyr<sup>397</sup>) was confirmed by peptide competition. The data show that only the phospho-peptide containing the phosphorylated (Tyr<sup>397</sup>) could block the ELISA signal. The nonphosphorylated peptide sequence or other phosphopeptides from the FAK sequence did not block the signal.

© Merck KGaA, Darmstadt, Deutschland, 2012


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