Phospho-AKT1 Mouse Antibody [Clone ID: M114]

Specifications

Product Data
Clone Name	M114
Applications	IP, WB
Recommend Dilution	WB: 1:250
Reactivity	Human, Rat, Mouse
Host	Mouse
Immunogen	Clone M114 was generated from a peptide containing amino acid residues surrounding Serine 473 in human Akt1. This sequence is highly conserved in human and mouse Akt, and may recognize Akt2 and Akt3.
Specificity	This antibody detects a 60 kDa* protein corresponding to the apparent molecular mass of Akt on SDS-PAGE immunoblots of mouse NIH3T3 cells treated with PDGF and human A431 cells treated with EGF.
Formulation	PBS + 0.02% NaN3
Concentration	lot specific
Purification	Protein G Purified
Conjugation	Unconjugated
Storage Condition	Recommended that the undiluted antibody be aliquoted into smaller working volumes (10-30 uL/vial depending on usage) upon arrival and stored long term at -20° C or -80° C, while keeping a working aliquot stored at 4° C for short term. Avoid freeze/thaw cycles. Stable for at least 1 year.
Predicted Protein Size	60
Database Link	UniProt ID P31749
Background	Akt (PKB, Rac kinase) is a 60kDa ser/thr kinase critical for controlling diverse cellular functions, including glucose metabolism, gene transcription, cell proliferation, and apoptosis. Akt phosphorylates a number of substrates including MBP, glycogen synthetase, PKA RII subunit, and histone H1. Akt is activated in response to insulin and growth factors in a PI3-kinase dependent manner. Activation of PI3-Kinase generates phosphatidylinositol 3,4-bisphosphate, which induces membrane translocation of Akt coincident with its phosphorylation at Thr-308 and Ser-473. Upon activation, Akt associates with members of the PKC family of kinases, such as PKCδ and PKCζ. Ceramide-activated PKCζ leads to phosphorylation of Thr-34 within the pleckstrin homology domain of Akt. This phosphorylation inhibits PIP3 binding to Akt preventing activation of the kinase and may lead to cermide-induced cell death.
Note	Protein G purified tissue culture supernatant.
Reference Data

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