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Immunohistochemical staining of formalin fixed and paraffin embedded human breast cancer tissue sections using Anti-Phospho-Akt (Ser473) RM251 at a 1:400 dilution.
Immunohistochemical staining of formalin fixed and paraffin embedded human breast cancer tissue sections using Anti-Phospho-Akt (Ser473) RM251 at a 1:400 dilution.
Immunohistochemical staining of formalin fixed and paraffin embedded human breast cancer tissue sections using Anti-Phospho-Akt (Ser473) RM251 at a 1:400 dilution.

anti-Phospho-Akt (Ser473) (human), Rabbit Monoclonal (RM251)

Research Use Only
REV-31-1131-00
RevMAb Biosciences
ApplicationsWestern Blot, ImmunoHistoChemistry
Product group Antibodies
ReactivityHuman
TargetAKT1
Price on request
Packing Size
Large volume orders?
Order with a bulk request

Overview

  • Supplier
    RevMAb Biosciences
  • Product Name
    anti-Phospho-Akt (Ser473) (human), Rabbit Monoclonal (RM251)
  • Delivery Days Customer
    5
  • Antibody Specificity
    This antibody reacts to Akt only when phosphorylated at Ser473. There is no cross-reactivity with Akt without phosphorylation at Ser473. This antibody may also react to bovine, mouse or rat Phospho-Akt (Ser473), as predicted by immunogen homology.
  • Applications
    Western Blot, ImmunoHistoChemistry
  • Certification
    Research Use Only
  • Clonality
    Monoclonal
  • Clone ID
    RM251
  • Formulation
    Liquid
  • Gene ID207
  • Target name
    AKT1
  • Target description
    AKT serine/threonine kinase 1
  • Target synonyms
    AKT; AKT1m; PKB; PKB alpha; PKB-ALPHA; PRKBA; protein kinase B alpha; proto-oncogene c-Akt; RAC; rac protein kinase alpha; RAC-ALPHA; RAC-alpha serine/threonine-protein kinase; RAC-PK-alpha; serine-threonine protein kinase; v-akt murine thymoma viral oncogene homolog 1; v-akt murine thymoma viral oncogene-like protein 1
  • Host
    Rabbit
  • Isotype
    IgG
  • Protein IDP31749
  • Protein Name
    RAC-alpha serine/threonine-protein kinase
  • Scientific Description
    Akt, also referred to as PKB or Rac, plays a critical role in controlling survival and apoptosis. This protein kinase is activated at 2 phosphorylation sites Thr308 and Ser473. Akt promotes cell survival by inhibiting apoptosis through phosphorylation and inactivation of several targets, including Bad, forkhead transcription factors, c-Raf and caspase-9. In addition to its role in survival and glycogen synthesis, Akt is involved in cell cycle regulation. Akt also plays a critical role in cell growth by directly phosphorylating mTOR in a rapamycin-sensitive complex containing raptor. Mutation of the glutamic acid at residue 17 to lysine (E17K) of Akt was initially identified in human breast, colorectal and ovarian cancers. This conserved glutamic acid residue is located at the lipid-binding pocket of the Akt plextrin homology domain. The E17K mutation increases the affinity between Akt and phospholipids at the plasma membrane, leading to increased Akt recruitment, super-activation of the Akt pathway, cellular transformation and tumor formation. Additional studies detect the presence of the Akt (E17K) mutation in multiple cancers, including lung cancer, prostate cancer, endometrial carcinoma and several melanomas. - Recombinant Antibody. This antibody reacts to Akt only when phosphorylated at Ser473. There is no cross-reactivity with Akt without phosphorylation at Ser473. This antibody may also react to bovine, mouse or rat Phospho-Akt (Ser473), as predicted by immunogen homology. Applications: WB, IHC. Source: Rabbit. Liquid. 50% Glycerol/PBS with 1% BSA and 0.09% sodium azide. Akt, also referred to as PKB or Rac, plays a critical role in controlling survival and apoptosis. This protein kinase is activated at 2 phosphorylation sites Thr308 and Ser473. Akt promotes cell survival by inhibiting apoptosis through phosphorylation and inactivation of several targets, including Bad, forkhead transcription factors, c-Raf and caspase-9. In addition to its role in survival and glycogen synthesis, Akt is involved in cell cycle regulation. Akt also plays a critical role in cell growth by directly phosphorylating mTOR in a rapamycin-sensitive complex containing raptor. Mutation of the glutamic acid at residue 17 to lysine (E17K) of Akt was initially identified in human breast, colorectal and ovarian cancers. This conserved glutamic acid residue is located at the lipid-binding pocket of the Akt plextrin homology domain. The E17K mutation increases the affinity between Akt and phospholipids at the plasma membrane, leading to increased Akt recruitment, super-activation of the Akt pathway, cellular transformation and tumor formation. Additional studies detect the presence of the Akt (E17K) mutation in multiple cancers, including lung cancer, prostate cancer, endometrial carcinoma and several melanomas.
  • Reactivity
    Human
  • Storage Instruction
    -20°C,2°C to 8°C
  • UNSPSC
    12352203