PI3 kinase (p110β/p85α), FLAG-tag Recombinant

Catalog #
40622
$425 *
Size: 20 µg
Qty
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Description

Complex of human PI3 kinase p110β, full-length, and human p85α, full length. The p110β construct contains an N-terminal FLAG-tag whereas p85α has no tag. The two recombinant proteins were co-expressed and affinity purified as a complex.

Synonyms
PIK3CB, p110beta, Phosphoinositide-3-Kinase Catalytic Beta

PIK3R1, Phosphoinositide-3-Kinase Regulatory Subunit 1 (Alpha), GRB1, p85alpha

Product Info
Storage and Usage
Citations
Species
Human
Construct
PI3 kinase (p110β (FLAG-2-1070(end)) / p85α (1-724(end)))
Host Species/Expression System
Sf9
Purity

≥85%

Format
Aqueous buffer solution
Formulation
25 mM Tris, pH 8.0, 69 mM NaCl, 1.35 mM KCl, 0.025% Tween-20, 3 mM DTT, 50% glycerol, and 0.05 mg/ml FLAG peptide.
MW
p110β: 124 kDa; p85α: 84 kDa
Amino Acids
p110β : 2-1070(end); p85α: 1-724(end)
Specific Activity

250 pmole/min/μg

Genbank #
p110β: NM_006219; p85α: NM_181523
UniProt #
p110ß: P42338; p85α: P27986
Tag(s)
p110β: N-terminal FLAG-Tag
Background

PI3 (phosphoinositide 3) kinases, or phosphatidylinositol 3 kinases, are a family of proteins that can be subdivided into four classes: I, II, III and IV. Class I is involved in converting PI (4, 5) P2 (phosphatidylinositol (4, 5)-biphosphate) into PI (3, 4, 5) P3 (phosphatidylinositol (3, 4, 5)-triphosphate) when activated by tyrosine kinase receptors and G-protein coupled receptors. They are heterodimeric proteins with a regulatory and a catalytic subunit. The heterodimer between p110 (catalytic subunit) and p85 (regulatory subunit) belongs to class IA. p110 and p85 have three variants each. Class I PI3K participates in cell signaling, mostly via the activation of PKB (protein kinase B) and the PI3K/AKT/mTOR pathway. Dysfunction of these kinases impacts cell growth and differentiation, and mutations in p110α have been linked to cancer. At least three isoform-specific inhibitors are approved by FDA for the treatment of lymphoma and leukemia. Further studies will help identify more selective inhibitors with a good tolerance that can bypass the development of drug resistance.

References
1. Marques M. et al., (2008). Mol. Cell. Biol. 28 (8), 2803-2814.
2. Straub A. et al., (2008). Thromb. Haemost. 99 (3), 609-615.