Purified anti-ZAP70 Phospho Tyr292 Antibody anti-ZAP70 - A16038B,BioLegend,693802

During development, reactivity was observed with mouse phospho-SYK.

Host

Mouse

Reactivity

Human

Application

ICFC -Quality testedDirect ELISA -Reported in the literature, not verified in house

Platform ID

BAB423031314

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Product Specifications
Scientific Background

Specifications

NamePurified anti-ZAP70 Phospho Tyr292 Antibody anti-ZAP70 - A16038B
Cat. No.693802
HostMouse
RRIDAB_2686945 (BioLegend Cat. No. 693802)
IsotypeMouse IgG1, κ
ReactivityHuman
ApplicationICFC -Quality testedDirect ELISA -Reported in the literature, not verified in house
ClonalityMonoclonal
Clone NumberA16038B
Concentration0.5 mg/ml
TargetZAP70 Phospho Tyr292
ImmunogenHuman ZAP70 peptide phosphorylated at Tyr292. Complete Freund's adjuvant.
PurityThe antibody was purified by affinity chromatography.
FormulationPhosphate-buffered solution, pH 7.2, containing 0.09% sodium azide.
StorageThe antibody solution should be stored undiluted between 2°C and 8°C.
Regulatory StatusResearch Use Only

Scientific Background

ZAP70 was identified in TCR-stimulated Jurkat cells. It is an inactive cytosolic tyrosine kinase that is recruited to a transmembrane receptor lacking intrinsic catalytic activity. ZAP70 and the related spleen tyrosine kinase (Syk) play a critical role in T-cell development and activation. This enzyme, which is phosphorylated on tyrosine residues upon T-cell antigen receptor (TCR) stimulation, functions in the initial step of TCR-mediated signal transduction in combination with the Src family kinases, Lck and Fyn.ZAP70 activation can be regulated by binding to phosphorylated ITAMs of the TCR and by phosphorylation of multiple tyrosine residues on ZAP70. Phosphorylation of Tyr315 and Tyr319 are essential for ZAP70 positive regulation of T-lymphocyte activation whereas Tyr292 has a negative regulatory role.Mutation of Tyr292 to phenylalanine enhanced NFAT induction in response to BCR stimulation, indicating phosphorylation of Tyr292 may promote association of ZAP-70 with a negative regulatory protein. ZAP-70 has been reported to bind Cbl following TCR stimulation and phosphorylation of Tyr292 was required for this interaction, as well as for the negative effect of Cbl on signaling.

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