PE anti-Syk Phospho (Tyr296) Recombinant Antibody, Syk Phospho, QA20B02,BioLegend,949304

When Syk is phosphorylated at tyrosine 296, the protein may display a slightly higher observed molecular weight by western blot.

Host

Mouse

Reactivity

Human, Mouse

Application

ICFC - Quality tested

Platform ID

BAB815510420

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Product Specifications
Scientific Background

Specifications

NamePE anti-Syk Phospho (Tyr296) Recombinant Antibody, Syk Phospho, QA20B02
Cat. No.949304
HostMouse
RRIDAB_3716900 (BioLegend Cat. No. 949303)AB_3716900 (BioLegend Cat. No. 949304)
IsotypeMouse IgG2b, κ
ReactivityHuman, Mouse
ApplicationICFC - Quality tested
ClonalityRecombinant
Clone NumberQA20B02
ConcentrationLot-specific (to obtain lot-specific concentration and expiration, please enter the lot number in ourCertificate of Analysisonline tool.)
TargetSyk Phospho
ImmunogenSynthetic peptide corresponding to Syk phosphorylated at tyrosine 296
PurityThe antibody was purified by affinity chromatography and conjugated with PE under optimal conditions.
FormulationPhosphate-buffered solution, pH 7.2, containing 0.09% sodium azide and BSA (origin USA)
StorageThe antibody solution should be stored undiluted between 2°C and 8°C, and protected from prolonged exposure to light.Do not freeze.
Regulatory StatusResearch Use Only

Scientific Background

Syk is a non-receptor tyrosine kinase that is a member of the Syk family of tyrosine kinases, with broad expression in hematopoietic cells. Upon immune receptor engagement, phosphorylated ITAM motifs within the cytosolic region of the activated receptor become phosphorylated and recruit Syk to the activated receptor via SH2 domains. ITAM-bound Syk is catalytically active, transmitting signals to multiple downstream signaling partners that drives processes such as phagocytosis, proliferation, and differentiation.Recent evidence also suggests a role for Syk in non-immune cells. Elevated Syk activation is associated with B-cell malignancies, rheumatoid arthritis, and Alzheimer’s disease, and multiple Syk inhibitors are being developed in clinical trials. Syk activity and function are both regulated by tyrosine phosphorylation at multiple sites. Tyr323 and Tyr352 phosphorylation facilitate binding to downstream effectors, and phosphorylation of Tyr525/Tyr526 in the activation loop is required for kinase activity. Tyr296 phosphorylation has been reported in lung epithelial cancer cells, and has been shown to occur as part of an autophosphorylation mechanismin vitro. This site is embedded within a larger N-terminal linker region that is required for nuclear localization in breast cancer cells. Despite rapid autophosphorylation of this site upon Syk activation, it is not required for Syk activity.

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