Active • Host: Insect cells • AA: 1-480 (full length) • Tag: N-terminal His • MW: 60.3 kDa
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Akt1 (human, recombinant)

Item No. 10011209

Technical Information
Synonyms
  • PKBα
  • Protein Kinase Bα
  • RAC-α Serine/threonine-protein Kinase
  • RAC-PK-α
Purity
≥95% estimated by SDS-PAGE
Source
Active recombinant N-terminal His-tagged Akt1 expressed in insect cells
Amino Acids
1-480 (full length)
MW
60.3 kDa
50 mM HEPES, pH 8.0, with 150 mM sodium chloride, 1 mM DTT, and 10% glycerol
UniProt Accession №
P31749
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    Product Description

    Akt1, also known as protein kinase Bα (PKBα), is a serine/threonine kinase belonging to the AGC kinase family and one of three Akt isoforms in mammals.1,2 Akt kinases function downstream of activated tyrosine kinases and PI3K to regulate a variety of cellular processes, including cell size, growth, proliferation, and survival, as well as genome stability, glucose metabolism, and neovascularization.2 Akt1, like Akt2 and Akt3, is composed of an N-terminal pleckstrin homology (PH) domain, which binds to phosphatidylinositol-(3,4,5)-triphosphate (PIP3) and phosphatidylinositol-(3,4)-diphosphate (PIP2), a kinase domain, and a C-terminal regulatory hydrophobic motif. It is ubiquitously expressed and is the primary isoform in endothelial cells.3 Akt1 is activated via recruitment to the plasma membrane, which is mediated by the interaction of the Akt1 PH domain with PI3K-generated PIP3 and PIP2, and subsequent phosphorylation at threonine 308 and serine 473.2 Increased Akt1 kinase activity has been found in tumor tissue isolated from patients with prostate, breast, and ovarian cancers.4 Cayman’s Akt1 (human, recombinant) protein was phosphorylated by recombinant 3-phosphoinositide-dependent kinase 1 (PDK1) and can be used for enzyme activity assays.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Dummler, B., and Hemmings, B.A. Physiological roles of PKB/Akt isoforms in development and disease. Biochem. Soc. Trans. 35(Pt 2), 231-235 (2007).

    2. Bellacosa, A., Kumar, C.C., Di Cristofano, A., et alActivation of AKT kinases in cancer: Implications for therapeutic targeting. Adv. Cancer Res. 94, 29-86 (2005).

    3. Manning, B.D., and Cantley, L.C. AKT/PKB signaling: Navigating downstream. Cell 129(7), 1261-1274 (2007).

    4. Sun, M., Wang, G., Paciga, J.E., et alAKT1/PKBα kinase is frequently elevated in human cancers and its constitutive activation is required for oncogenic transformation in NIH3T3 cells. Am. J. Pathol. 159(2), 431-437 (2001).