PI3 Kinase p85 (Phospho Tyr458)/p55 (Phospho Tyr199) Rabbit mAb

Human,Mouse,Rat

WB,IF,ELISA

单克隆抗体

PIK3R1/PIK3R2/PIK3R3

Phosphatidylinositol 3-kinase regulatory subunit alpha/beta/gamma

85kD,55kD

PI3 Kinase p85 (Phospho Tyr458)/p55 (Phospho Tyr199) detects endogenous levels of PI3 kinase p85/p55 only when phosphorylated at Human:Y467/Y199, Mouse:Y467/Y199, Rat:Y467/Y199..The name of modified sites may be influenced by many factors, such as species (the modified site was not originally found in human samples) and the change of protein sequence (the previous protein sequence is incomplete, and the protein sequence may be prolonged with the development of protein sequencing technology). When naming, we will use the "numbers" in historical reference to keep the sites consistent with the reports. The antibody binds to the following modification sequence (lowercase letters are modification sites):RLyEE

PBS, 50% glycerol, 0.05% Proclin 300, 0.05%BSA

Monoclonal, Rabbit,IgG

WB 1:1000-1:5000; IF 1:200-1:1000; ELISA 1:5000-1:20000;

Protein A

1 mg/ml

-15°C to -25°C/1 year(Do not lower than -25°C)

PIK3R1 ; GRB1 ; Phosphatidylinositol 3-kinase regulatory subunit alpha ; PI3-kinase regulatory subunit alpha ; PI3K regulatory subunit alpha ; PtdIns-3-kinase regulatory subunit alpha ; Phosphatidylinositol 3-kinase 85 kDa regulatory subunit alpha ; PI3-kinase subunit p85-alpha ; PtdIns-3-kinase regulatory subunit p85-alpha ; PIK3R2 ; Phosphatidylinositol 3-kinase regulatory subunit beta ; PI3-kinase regulatory subunit beta ; PI3K regulatory subunit beta ; PtdIns-3-kinase regulatory subunit beta ;

Phosphatidylinositol 3-kinase phosphorylates the inositol ring of phosphatidylinositol at the 3-prime position. The enzyme comprises a 110 kD catalytic subunit and a regulatory subunit of either 85, 55, or 50 kD. This gene encodes the 85 kD regulatory subunit. Phosphatidylinositol 3-kinase plays an important role in the metabolic actions of insulin, and a mutation in this gene has been associated with insulin resistance. Alternative splicing of this gene results in four transcript variants encoding different isoforms. [provided by RefSeq, Jun 2011],

Disease:Defects in PIK3R1 are a cause of severe insulin resistance.,Domain:The SH3 domain mediates the binding to CBLB, and to HIV-1 Nef.,Function:Binds to activated (phosphorylated) protein-Tyr kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane. Necessary for the insulin-stimulated increase in glucose uptake and glycogen synthesis in insulin-sensitive tissues.,PTM:Polyubiquitinated in T-cells by CBLB; which does not promote proteasomal degradation but impairs association with CD28 and CD3Z upon T-cell activation.,similarity:Belongs to the PI3K p85 subunit family.,similarity:Contains 1 Rho-GAP domain.,similarity:Contains 1 SH3 domain.,similarity:Contains 2 SH2 domains.,subunit: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.,tissue specificity:Isoform 2 is expressed in skeletal muscle and brain, and at lower levels in kidney and cardiac muscle. Isoform 2 and isoform 4 are present in skeletal muscle (at protein level).,