Recombinant human Pik3ca + PIK3R1 protein
Be the first to review this product! Submit a review
|
(0 Publication)
Recombinant human Pik3ca + PIK3R1 protein is a Human Full Length protein, expressed in Baculovirus infected Sf9 cells, with >90%, suitable for SDS-PAGE, WB, FuncS.
View Alternative Names
GRB1, PIK3R1, 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
- FuncS
Unknown
Functional Studies - Recombinant human Pik3ca + PIK3R1 protein (AB85833)
The Specific activity of ab85833 was determined to be 5147 RLU/min/mg.
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant human Pik3ca + PIK3R1 protein (AB85833)
SDS-PAGE showing ab85833 with bands at approximately 111 (Pik3ca) and 86kDa (PIK3R1).
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
These proteins mediate important cell signaling pathways and participate as parts of the PI3K/AKT/mTOR complex. This complex controls key cellular functions including growth survival and metabolism. The PIK3CA-PIK3R1 interaction activates downstream signaling events necessary for cell division and differentiation. By modulating signal transduction they enable cellular responses to growth factors and nutrients.
Pathways
The role of PIK3CA and PIK3R1 extends to interfacing with the PI3K/AKT and mTOR pathways. These pathways monitor cellular nutrient levels and energy status ensuring that cells respond appropriately to environmental cues. PIK3R1 associates with proteins like AKT and mTOR serving as a bridge between these pathways. These interactions promote critical cellular activities such as autophagy angiogenesis and apoptosis regulation.
Specifications
Form
Liquid
Additional notes
Affinity purified.
General info
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. Plays an important role in signaling in response to FGFR1, FGFR2, FGFR3, FGFR4, KITLG/SCF, KIT, PDGFRA and PDGFRB. Likewise, plays a role in ITGB2 signaling (PubMed : 17626883, PubMed : 19805105, PubMed : 7518429). Modulates the cellular response to ER stress by promoting nuclear translocation of XBP1 isoform 2 in a ER stress- and/or insulin-dependent manner during metabolic overloading in the liver and hence plays a role in glucose tolerance improvement (PubMed : 20348923).
Sequence similarities
Belongs to the PI3K p85 subunit family.
Post-translational modifications
Polyubiquitinated in T-cells by CBLB; which does not promote proteasomal degradation but impairs association with CD28 and CD3Z upon T-cell activation.. In adipose tissue, polyubiquitinated by the BCR(KBTBD2) E3 ubiquitin ligase complex; recognized by KBTBD2 through the SH2 domains, undergoes 'Lys-48'-linked polyubiquitination leading to its degradation.. Phosphorylated. Tyrosine phosphorylated in response to signaling by FGFR1, FGFR2, FGFR3 and FGFR4. Phosphorylated by CSF1R. Phosphorylated by ERBB4. Phosphorylated on tyrosine residues by TEK/TIE2. Dephosphorylated by PTPRJ. Phosphorylated by PIK3CA at Ser-608; phosphorylation is stimulated by insulin and PDGF. The relevance of phosphorylation by PIK3CA is however unclear (By similarity). Phosphorylated in response to KIT and KITLG/SCF. Phosphorylated by FGR.
Target data
Additional targets
Product promise
Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.
For licensing inquiries, please contact partnerships@abcam.com