PI 3 Kinase p85 alpha [U13]

U13

Baculovirus expressed (recombinant) Bovine p85 alpha subunit of PI 3 Kinase.

Recognizes the SH3 domain of the p85 alpha subunit of bovine PI 3 kinase.

Tissue Culture Supernatant Storage

For IP: Use at a neat dilution. For WB: Use at a dilution of 1:200. Not tested in other applications. Optimal dilutions/concentrations should be determined by the researcher. Myeloma: NS1 The enzyme PI-3-K phosphorylates at the D-3 position of the inositol ring of PI PI-4- phosphate and PI-4 5-biphosphate (PI-4 5-P2) to produce their respective PI3-phosphorylated derivatives. PI-3-K exists as a heterodimer of 85 kDa (p85) and 110 kDa (p110) subunits. The p85 subunit contains two SH2 domains and an SH3 domain. It has been shown to associate with and serve as a substrate for activated growth factor receptor tyrosine kinases. p85 may serve as regulator of the catalytic subunit p110 by acting as the link between PI-3-K and the ligand-activated receptor. Two distinct forms of the p85 subunit are described: p85 alpha which binds tightly to the catalytic subunit and p85 beta a protein of unknown function. Both isoforms bind to activated receptors and serve as tyrosine kinase substrates.

Heterodimer of a p110 (catalytic) and a p85 (regulatory) subunits. Interacts with phosphorylated TOM1L1. Interacts with phosphorylated LIME1 upon TCR and/or BCR activation. Interacts with SOCS7. Interacts with RUFY3 (By similarity). Interacts with phosphorylated LAT LAX1 and TRAT1 upon TCR activation. Interacts with CBLB. Interacts with HIV-1 Nef to activate the Nef associated p21-activated kinase (PAK). This interaction depends on the C-terminus of both proteins and leads to increased production of HIV. Interacts with HCV NS5A. The SH2 domains interact with the YTHM motif of phosphorylated INSR in vitro. Also interacts with tyrosine-phosphorylated IGF1R in vitro. Interacts with CD28 and CD3Z upon T-cell activation. Interacts with IRS1 and phosphorylated IRS4 as well as with NISCH and HCST.

The SH3 domain mediates the binding to CBLB and to HIV-1 Nef.

Defects in PIK3R1 are a cause of severe insulin resistance.

Contains 1 Rho-GAP domain.

Contains 1 SH3 domain.