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AB159130

Recombinant Human PI 3 Kinase p85 (SH2) protein (GST tag N-Terminus)

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Recombinant Human PI 3 Kinase p85 (SH2) protein (GST tag N-Terminus) is a Human Full Length protein, in the 1 to 454 aa range, expressed in Wheat germ, suitable for ELISA, WB.

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

1 Images
SDS-PAGE - Recombinant Human PI 3 Kinase p85 (SH2) protein (GST tag N-Terminus) (AB159130)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human PI 3 Kinase p85 (SH2) protein (GST tag N-Terminus) (AB159130)

ab159130 on a 12.5% SDS-PAGE stained with Coomassie Blue.

Key facts

Expression system

Wheat germ

Tags

GST tag N-Terminus

Applications

ELISA, WB

applications

Biologically active

No

Accession

P27986

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 0.79% Tris HCl, 0.31% Glutathione

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "ELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"MYNTVWNMEDLDLEYAKTDINCGTDLMFYIEMDPPALPPKPPKPTTVANNGMNNNMSLQDAEWYWGDISREEVNEKLRDTADGTFLVRDASTKMHGDYTLTLRKGGNNKLIKIFHRDGKYGFSDPLTFSSVVELINHYRNESLAQYNPKLDVKLLYPVSKYQQDQVVKEDNIEAVGKKLHKYNTQFQEKSREYDRLYEEYTRTSQEIQMKRTAIEAFNETIKIFEEQCQTQERYSKEYIEKFKREGNEKEIQRIMHNYDKLKSRISEIIDSRRRLEEDLKKQAAEYREIDKRMNSIKPDLIQLRKTRDQYLMWLTQKGVRQKKLNEWLGNENTEDQYSLVEDDEDLPHHDEKTWNVGSSNRNKAENLLRGKRDGTFLVRESSKQGCYACSVVVDGEVKHCVINKTATGYGFAEPYNLYSSLKELVLHYQHTSLVQHNDSLNVTLAYPVYAQQRR","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":454,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Wheat germ","accessionNumber":"P27986","tags":[{"tag":"GST","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

PI 3 Kinase p85 also known as the regulatory subunit of phosphoinositide 3-kinase forms part of the PI3K complex which plays an important role in cellular functions. The p85 subunit with an approximate molecular mass of 85 kDa binds to and regulates the catalytic p110 subunit. This binding is necessary for the activation of the PI3K enzyme complex. PI 3 Kinase p85 is widely expressed across a variety of tissues particularly abundant in immune cells where it contributes to signaling pathways that regulate cell growth and survival.
Biological function summary

PI 3 Kinase p85 acts to stabilize the catalytic subunit allowing for proper signal transduction in response to external stimuli. As part of the PI3K complex it is essential for the regulation of the enzyme's substrate specificity and activity. This complex facilitates the conversion of PIP2 to PIP3 a lipid second messenger that is important in various signalling pathways. Through its actions PI 3 Kinase p85 supports cell proliferation differentiation and metabolism impacting numerous cellular processes.

Pathways

PI 3 Kinase p85 plays significant roles within the PI3K/AKT and mTOR signaling pathways. These pathways are fundamental to regulating processes like cell metabolism apoptosis and protein synthesis. In the PI3K/AKT pathway the p85 subunit collaborates closely with the catalytic p110 subunit to phosphorylate and activate AKT an important downstream effector. In the mTOR pathway it influences cellular response to growth factors. These interactions of PI 3 Kinase p85 with other proteins display its centrality to critical cellular activities.

PI 3 Kinase p85 has a significant association with cancer and insulin resistance. Over-activation of PI3K signaling often results in oncogenesis where the deregulation of cell growth and division occurs. Aberrant activity of PI 3 Kinase p85 particularly alterations in its regulatory role is linked to tumorigenesis via interactions with AKT protein in the cancer context. In insulin resistance defective signaling reduces the effectiveness of insulin-mediated glucose uptake. The connection of PI 3 Kinase p85 with these proteins and disorders highlights its importance in pathological conditions.

Specifications

Form

Liquid

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.

Product protocols

Target data

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).
See full target information PIK3R1

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