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All of our services and products are intended for preclinical research use only and cannot be used to diagnose, treat or manage patients.

Phospho-Akt (Ser473) (587F11) Mouse Antibody

INQUIRY

CAT. NO.: AMA-0598

Target Information
UniProt ID	P31751

Product Details
Size	100 µl/300 µL
Reactivity	Human, Mouse, Rat, Hamster
Host	Mouse
Source/Isotype	Mouse IgG2b
Storage	Store at -20°C. Do not aliquot the antibody.
Purification	Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues around Ser473 of mouse Akt.

Usage
Application	WB, IP
Product Usage Information Dilution	Western Blotting (1:1000); Immunoprecipitation (1:200)
MW (Target)	60 kDa

Background
Akt, also referred to as PKB or Rac, plays a critical role in controlling survival and apoptosis This protein kinase is activated by insulin and various growth and survival factors to function in a wortmannin-sensitive pathway involving PI3 kinase Akt is activated by phospholipid binding and activation loop phosphorylation at Thr308 by PDK1 and by phosphorylation within the carboxy terminus at Ser473. The previously elusive PDK2 responsible for phosphorylation of Akt at Ser473 has been identified as mammalian target of rapamycin (mTOR) in a rapamycin-insensitive complex with rictor and Sin1 Akt promotes cell survival by inhibiting apoptosis through phosphorylation and inactivation of several targets, including Bad forkhead transcription factors c-Raf and caspase-9. PTEN phosphatase is a major negative regulator of the PI3K/Akt signaling pathway. LY294002 is a specific PI3 kinase inhibitor. Another essential Akt function is the regulation of glycogen synthesis through phosphorylation and inactivation of GSK-3α and β. Akt may also play a role in insulin stimulation of glucose transport. In addition to its role in survival and glycogen synthesis, Akt is involved in cell cycle regulation by preventing GSK-3β-mediated phosphorylation and degradation of cyclin D1 and by negatively regulating the cyclin-dependent kinase inhibitors p27 Kip1 and p21 Waf1/Cip1. Akt also plays a critical role in cell growth by directly phosphorylating mTOR in a rapamycin-sensitive complex containing raptor. More importantly, Akt phosphorylates and inactivates tuberin (TSC2), an inhibitor of mTOR within the mTOR-raptor complex.

Background

Akt, also referred to as PKB or Rac, plays a critical role in controlling survival and apoptosis This protein kinase is activated by insulin and various growth and survival factors to function in a wortmannin-sensitive pathway involving PI3 kinase Akt is activated by phospholipid binding and activation loop phosphorylation at Thr308 by PDK1 and by phosphorylation within the carboxy terminus at Ser473. The previously elusive PDK2 responsible for phosphorylation of Akt at Ser473 has been identified as mammalian target of rapamycin (mTOR) in a rapamycin-insensitive complex with rictor and Sin1 Akt promotes cell survival by inhibiting apoptosis through phosphorylation and inactivation of several targets, including Bad forkhead transcription factors c-Raf and caspase-9. PTEN phosphatase is a major negative regulator of the PI3K/Akt signaling pathway. LY294002 is a specific PI3 kinase inhibitor. Another essential Akt function is the regulation of glycogen synthesis through phosphorylation and inactivation of GSK-3α and β. Akt may also play a role in insulin stimulation of glucose transport. In addition to its role in survival and glycogen synthesis, Akt is involved in cell cycle regulation by preventing GSK-3β-mediated phosphorylation and degradation of cyclin D1 and by negatively regulating the cyclin-dependent kinase inhibitors p27 Kip1 and p21 Waf1/Cip1. Akt also plays a critical role in cell growth by directly phosphorylating mTOR in a rapamycin-sensitive complex containing raptor. More importantly, Akt phosphorylates and inactivates tuberin (TSC2), an inhibitor of mTOR within the mTOR-raptor complex.

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All of our services and products are intended for preclinical research use only and cannot be used to diagnose, treat or manage patients.