Product Name: AKT1 (phospho Ser473) Antibody
Species Reactivity: Human, Mouse, Rat
Tested Applications: ELISA, IHC, WB
Applications: AKT1 antibody can be used in ELISA starting at 1:000 – 1:1000, and immunohistochemistry starting at 5 μg/mL.
User Note: Optimal dilutions for each application to be determined by the researcher.
Predicted Molecular Weight:
Immunogen: AKT1 antibody was raised against a peptide located in the phospho C-Terminus aa 460 – 480 of AKT1 (Human).
Host Species: Rabbit
Purification: Immunoaffinity Chromatography
Physical State: Liquid
CAS NO.: 1423186-80-4
Product: RIP2 kinase inhibitor 1
Buffer: 0.02 M potassium phosphate, 0.15 M sodium chloride, pH 7.2, 0.01% sodium azide.
Concentration:
Storage Conditions: Store AKT1 antibody at 4 ˚C or -20 ˚C. As with all antibodies avoid freeze/thaw cycles.
Clonality: Polyclonal
Conjugate: Unconjugated
Alternate Names: AKT1, AKT, AKT-1, C-AKT, Pan-AKT, PKB alpha, PKBalpha, Proto-oncogene c-Akt, Protein kinase B, Rac protein kinase alpha, PRKBA, Protein kinase B alpha, RAC-PK-alpha, PKB, PKB-ALPHA, RAC, RAC-ALPHA
Accession NO.: P31749
Protein Ino: 60391226
Official Symbol: AKT1
Geneid: 207
Background: AKT is a component of the PI-3 kinase pathway and is activated by phosphorylation at Ser 473 and Thr 308. AKT is a cytoplasmic protein also known as AKT1, Protein Kinase B (PKB) and rac (related to A and C kinases). AKT is a key regulator of many signal transduction pathways. AKT Exhibits tight control over cell proliferation and cell viability. Overexpression or inappropriate activation of AKT is noted in many types of cancer. AKT mediates many of the downstream events of PI 3-kinase (a lipid kinase activated by growth factors, cytokines and insulin). PI 3-kinase recruits AKT to the membrane, where it is activated by PDK1 phosphorylation. Once phos-phorylated, AKT dissociates from the membrane and phos-phorylates targets in the cytoplasm and the cell nucleus. AKT has two main roles: (i) inhibition of apoptosis; (ii) promotion of proliferation.
PubMed ID:http://aac.asm.org/content/52/8/2709.abstract
