Description
PI3K P85 (phospho Tyr467) Antibody | 79-505 | Gentaur UK, US & Europe Distribution
Host: Rabbit
Reactivity: Human, Mouse, Rat
Homology: N/A
Immunogen: PI3K P85 (phospho-Tyr467) antibody was raised against a peptide sequence around phosphorylation site of tyrosine 467 (L-Y (p) -E-E-Y) derived from Human PI3K P85.
Research Area: Phospho-Specific
Tested Application: WB
Application: Western Blot: 1:500~1:1000
Specificiy: This antibody detects endogenous level of total PI3K P85 only when phosphorylated at tyrosine 467.
Positive Control 1: N/A
Positive Control 2: N/A
Positive Control 3: N/A
Positive Control 4: N/A
Positive Control 5: N/A
Positive Control 6: N/A
Molecular Weight: 85 kDa
Validation: N/A
Isoform: N/A
Purification: Antibodies were purified by affinity-chromatography using epitope-specific phosphopeptide. Non-phospho specific antibodies were removed by chromatogramphy using non-phosphopeptide.
Clonality: Polyclonal
Clone: N/A
Isotype: N/A
Conjugate: Unconjugated
Physical State: Liquid
Buffer: Antibody supplied in phosphate buffered saline (without Mg2+ and Ca2+) , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
Concentration: 1 mg/mL
Storage Condition: Store antibody at -20˚C for up to one year.
Alternate Name: p85, AGM7, GRB1, p85-ALPHA, LHR, MDU2, MDU3, MIC4, PI3-kinase p85 subunit alpha, PtdIns-3-kinase p85-alpha
User Note: N/A
BACKGROUND: Binds to activated (phosphorylated) protein-Tyr kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane. Necessary for the insulin-stimulated increase in glucose uptake and glycogen synthesis in insulin-sensitive tissues. Binds to activated (phosphorylated) protein-tyrosine kinases through its SH2 domain and regulates their kinase activity. During insulin stimulation, it also binds to IRS-1./Binds to activated (phosphorylated) protein-tyrosine kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane.