AKT1
Reactivity: Human
WB, ELISA, IHC, IF, IP
Host: Rabbit
Monoclonal
4H12
unconjugated
Recombinant Antibody
Application Notes
This antibody detects Akt (pT308) in human and mouse cell lines. We have been unable to detect upregulated phosphorylation of Akt in activated leukocytes, such as whole blood and peripheral blood mononuclear cells.
Sample Volume
20 μL
Restrictions
For Research Use only
Format
Liquid
Buffer
Aqueous buffered solution containing BSA and ≤0.09 % sodium azide.
Preservative
Sodium azide
Precaution of Use
This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage
4 °C
Storage Comment
Store undiluted at 4°C and protected from prolonged exposure to light. Do not freeze. The antibody was conjugated with R-PE under optimum conditions, and unconjugated antibody and free PE were removed.
De Falco, Avitabile, Totta, Straino, Spallotta, Cencioni, Torella, Rizzi, Porcelli, Zacheo, Di Vito, Pompilio, Napolitano, Melillo, Capogrossi, Pesce: "Altered SDF-1-mediated differentiation of bone marrow-derived endothelial progenitor cells in diabetes mellitus." in: Journal of cellular and molecular medicine, Vol. 13, Issue 9B, pp. 3405-14, (2010) (PubMed).
Cantley, Neel: "New insights into tumor suppression: PTEN suppresses tumor formation by restraining the phosphoinositide 3-kinase/AKT pathway." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 96, Issue 8, pp. 4240-5, (1999) (PubMed).
Ferrigno, Silver: "Regulated nuclear localization of stress-responsive factors: how the nuclear trafficking of protein kinases and transcription factors contributes to cell survival." in: Oncogene, Vol. 18, Issue 45, pp. 6129-34, (1999) (PubMed).
Kandel, Hay: "The regulation and activities of the multifunctional serine/threonine kinase Akt/PKB." in: Experimental cell research, Vol. 253, Issue 1, pp. 210-29, (1999) (PubMed).
Alessi, Andjelkovic, Caudwell, Cron, Morrice, Cohen, Hemmings: "Mechanism of activation of protein kinase B by insulin and IGF-1." in: The EMBO journal, Vol. 15, Issue 23, pp. 6541-51, (1997) (PubMed).
Akt [also known as PKB (Protein kinase B) or RAC-PK (Related to the A and C kinases)] is a family of serine/threonine kinases that contains a pleckstrin homology (PH) domain. PH domains play important roles in signal transduction. There are three known isoforms of Akt in mammalian cells [Akt1 (alpha), Akt2 (beta) and Akt3 (gamma)], they are thought to be regulated similarly. Akt is activated by insulin and growth factors by a mechanism involving phosphoinositide 3-OH kinase. Phosphoinositide 3-OH kinase products bind to the PH domain, resulting in translocation of Akt to the plasma membrane and activation of Akt to phospho-Akt by upstream kinases. Akt is phosphorylated within the activation loop at threonine 308 (T308) and the C-terminus at serine 473. Phospho-Akt promotes cell survival by inhibiting apoptosis. Specifically, phospho-Akt1 has been shown to phosphorylate Bad, a member of the Bcl-2 family that promotes cell death. This phosphorylation results in the inactivation of the proapoptotic function of Bad. The Akt molecule is thus considered to link extracellular survival signals (growth factors) with the apoptotic machinery (Bad). Akt is also a key mediator of the metabolic effects of insulin. Additionally, Akt has been referred to as an oncogene because it has increased activity in a number of tumors. The J1-223.371 antibody recognizes Akt phosphorylated at T308.