产品名称
Akt Inhibitor VI, Akt-in, The Akt Inhibitor VI, Akt-in controls the biological activity of Akt. This small molecule/inhibitor is primarily used for Phosphorylation & Dephosphorylation applications.
Quality Level
assay
≥95% (HPLC)
form
lyophilized solid
manufacturer/tradename
Calbiochem®
storage condition
OK to freeze
desiccated (hygroscopic)
color
white
solubility
water: 1 mg/mL
shipped in
ambient
storage temp.
2-8°C
Biochem/physiol Actions
Cell permeable: no
Kd ~18 µM in binding to Akt-PH domain
Primary Target
Akt
Akt
Product does not compete with ATP.
Reversible: yes
Disclaimer
Toxicity: Carcinogenic / Teratogenic (D)
General description
A reversible 15-mer peptide derived from proto-oncogene TCL1 (amino acids 10-24) that acts as a specific inhibitor of Akt. Shown to bind to Akt-PH domain (Kd ~18 µM) and interfere with the Akt-phosphoinositide interaction, thus hindering membrane translocation from the cytosol and downstream biological responses.
A reversible 15-mer peptide derived from the amino acids 10-24 of the proto-oncogene TCL1 (TCL10-24) and acts as a specific inhibitor of Akt. Shown to bind to the Akt-PH domain (Kd ~18 µM) and interfere with the Akt-phosphoinositide interaction. This peptide, when made cell-permeable (Cat. No. 124014), has been shown to hinder Akt membrane translocation from the cytosol and subsequent downstream biological responses.
Other Notes
H-Ala-Val-Thr-Asp-His-Pro-Asp-Arg-Leu-Trp-Ala-Trp-Glu-Lys-Phe-OH
Hiromura, M., et al. 2004. J. Biol. Chem.279, 53407.
Packaging
Packaged under inert gas
Physical form
Supplied as an acetate salt.
Preparation Note
Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 3 months at -20°C.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
存储类别
11 - Combustible Solids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
Zahra Davoudi et al.
Asian Pacific journal of cancer prevention : APJCP, 15(10), 4353-4358 (2014-06-18)
PI3/AKT and NF-kB signaling pathways are constitutively active in acute myeloid leukemia and cross-talk between the two has been shown in various cancers. However, their role in acute myeloid leukemia has not been completely explored. We therefore used cell penetrating
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