Old Browser
Looks like you're visiting us from {countryName}.
Would you like to stay on the current country site or be switched to your country?
Western blot analysis of Akt on HCT-8 cell lysate. Lane 1: 1:500, lane 2: 1:1000, lane 3: 1:2000 dilution of anti-Akt.
Immunofluorescent staining of WI-38 cells with anti-Akt.
BD Transduction Laboratories™ Purified Mouse anti-Akt
BD Transduction Laboratories™ Purified Mouse anti-Akt
규제 상태 범례
Becton, Dickinson and Company의 명시적인 서면 승인 없이는 사용 하실 수 없습니다.
준비 및 보관
제품 고시
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
- Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
- Source of all serum proteins is from USDA inspected abattoirs located in the United States.
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 (α), Akt2 (β) and Akt3 (γ)]; 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 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 55/PKBa/Akt monoclonal antibody recognizes Akt1, regardless of phosphorylation status.
This antibody is routinely tested by western blot analysis. Other applications were tested at BD Biosciences Pharmingen during antibody development only or reported in the literature.
개발 참고 자료 (5)
-
Alessi DR, Andjelkovic M, Caudwell B, et al. Mechanism of activation of protein kinase B by insulin and IGF-1. EMBO J. 1996; 15(23):6541-6551. (Biology). 참조 보기
-
Cantley LC, Neel BG. New insights into tumor suppression: PTEN suppresses tumor formation by restraining the phosphoinositide 3-kinase/AKT pathway. Proc Natl Acad Sci U S A. 1999; 96(8):4240-4245. (Biology). 참조 보기
-
Datta SR, Dudek H, Tao X, et al. Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery. Cell. 1997; 91:231-241. (Biology). 참조 보기
-
Ferrigno P, Silver PA. Regulated nuclear localization of stress-responsive factors: how the nuclear trafficking of protein kinases and transcription factors contributes to cell survival. Oncogene. 1999; 18(45):6129-6134. (Biology). 참조 보기
-
Kandel ES, Hay N. The regulation and activities of the multifunctional serine/threonine kinase Akt/PKB. Exp Cell Res. 1999; 253(1):210-229. (Biology). 참조 보기
Please refer to Support Documents for Quality Certificates
Global - Refer to manufacturer's instructions for use and related User Manuals and Technical data sheets before using this products as described
Comparisons, where applicable, are made against older BD Technology, manual methods or are general performance claims. Comparisons are not made against non-BD technologies, unless otherwise noted.
For Research Use Only. Not for use in diagnostic or therapeutic procedures.
Report a Site Issue
This form is intended to help us improve our website experience. For other support, please visit our Contact Us page.