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ABS234

Sigma-Aldrich

Anti-PI3 Kinase Antibody, p85

from rabbit, purified by affinity chromatography

Synonym(s):

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-al

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

rabbit

Quality Level

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

purified by

affinity chromatography

species reactivity

rat, human

species reactivity (predicted by homology)

mouse (based on 100% sequence homology), monkey (based on 100% sequence homology), bovine (based on 100% sequence homology)

technique(s)

immunoprecipitation (IP): suitable
western blot: suitable

NCBI accession no.

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

bovine ... Pik3R1(282307)
human ... PIK3R1(5295)
mouse ... Pik3R1(18708)
rat ... Pik3R1(25513)
rhesus monkey ... Pik3R1(698996)

General description

Phosphatidylinositol 3-Kinase (PI3 Kinase) is responsible for phosphorylation of the 3 position of the inositol ring of PI(4,5)P2, to generate PI(3,4,5)P3, a potent second messenger required for survival signaling, and insulin action. PI3 Kinase is a heterodimeric complex composed of an 85 kDa regulatory subunit and a 110 kDa catalytic subunit. Tyrosine phosphorylation of growth factor receptors creates docking sites for binding of p85 (through its SH2 domains) on the receptors; p85 brings with it p110, which is then proximal to its phospho-lipid substrate on the membrane. PI3 Kinase is also activated by Ras, and by the β,γ subunits of heterotrimeric G-proteins. PI3 Kinase is inhibited by wortmannin, a useful tool for the study of the PI3 Kinase signaling pathway.

Immunogen

GST-tagged recombinant protein corresponding to rat PI3 Kinase, p85.

Application

Detect PI3 Kinase, p85 using this rabbit polyclonal antibody, Anti-PI3 Kinase Antibody, p85 validated for use in western blotting & IP.
Immunoprecipitation Analysis: A representative lot immunoprecipitated PI3 Kinase, p85 in 0.5 mg of Jurkat cell lysate.

Quality

Evaluated by Western Blotting in Jurkat cell lysate.

Western Blotting Analysis: A 1:600 dilution of this antibody detected PI3 Kinase, p85 in 10 µg of Jurkat cell lysate.

Target description

~85 kDa observed

Linkage

Replaces: 06-497

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Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Bruna Gazzi de Lima-Seolin et al.
Oxidative medicine and cellular longevity, 2019, 6325424-6325424 (2019-07-31)
The increased circulation of norepinephrine, found in the diseased heart as a result of sympathetic nervous system overactivation, is responsible for its cardiotoxic effects including pathological hypertrophy, cell death, and oxidative stress. Bucindolol is a third generation adrenergic blocker, which
Anastasiia Stratiievska et al.
eLife, 7 (2018-12-19)
Although it has been known for over a decade that the inflammatory mediator NGF sensitizes pain-receptor neurons through increased trafficking of TRPV1 channels to the plasma membrane, the mechanism by which this occurs remains mysterious. NGF activates phosphoinositide 3-kinase (PI3K)
Flemming Dela et al.
Acta physiologica (Oxford, England), 226(2), e13245-e13245 (2018-12-27)
To examine the effect of high-intensity interval training (HIIT) on glucose clearance rates in skeletal muscle and explore the mechanism within the muscle. Ten males with type 2 diabetes mellitus (T2DM) and ten matched healthy subjects performed 2 weeks of one-legged
Scott E LeBlanc et al.
Nucleic acids research, 44(11), 5133-5147 (2016-03-05)
PPARγ2 is a critical lineage-determining transcription factor that is essential for adipogenic differentiation. Here we report characterization of the three-dimensional structure of the PPARγ2 locus after the onset of adipogenic differentiation and the mechanisms by which it forms. We identified
Mathews Valuparampil Varghese et al.
American journal of physiology. Lung cellular and molecular physiology, 320(4), L508-L521 (2021-01-28)
We have previously reported that several patients with idiopathic pulmonary hypertension (PH) had different types of G6PD deficiency. However, the role of G6PD in PH is multifactorial because G6PD is involved in controlling oxidative stress, metabolic switch, and red blood

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