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Validated All-in-One™ qPCR Primer for PIK3CB(NM_006219.2) Search again
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
Summary
Phosphoinositide 3-kinases (PI3Ks) phosphorylate the 3-prime OH position of the inositol ring of inositol lipids. They have been implicated as participants in signaling pathways regulating cell growth by virtue of their activation in response to various mitogenic stimuli. PI3Ks are composed of a 110-kD catalytic subunit, such as PIK3CB, and an 85-kD adaptor subunit (Hu et al., 1993 [PubMed 8246984]).[supplied by OMIM].
Gene References into function
- This paper reports the first purification of a phosphoinositide 3-kinase and shows that the protein is a heterodimer of an 85 kd regulatory subunit that mediates binding to phosphorylated proteins and a 110 kd catalytic subunit.
- These results indicate that in addition to their roles in recruiting the catalytic subunit of PI3K to the insulin receptor substrate proteins, both p85alpha and p85beta play negative roles in insulin signaling
- A function for phosphoinositide 3-kinase beta lipid products in coupling beta gamma to Ras activation in response to lysophosphatidic acid.
- It is unlikely that the promoter polymorphisms -359T/C and -303A/G of the catalytic subunit p110beta gene of human PI 3-kinase have a major impact on insulin secretion, insulin sensitivity, or the risk of type 2 diabetes
- p110 has a role in activation of PI3K gamma along with G beta gamma
- determinination of the involvement of PI3K and MAPK pathways and the importance of cross-talk between these pathways, in glucose-potentiated vascular smooth muscle cell chemotaxis to serum factors
- Data highlight the differential signaling by p110alpha and -beta isoforms.
- Introduction of a pH1 vector producing shRNA (short hairpin RNA) that targets p110beta abolished PIA [N6-(2-phenylisopropyl)adenosine]-induced Akt activation
- although introduction of activating mutations from p110alpha at the corresponding sites in p110beta failed to render the enzyme oncogenic in human cells, the possibility remains that other mutations might activate the beta isoform
- p110beta, -gamma, and -delta isoforms of class I phosphoinositide 3-kinase have roles in oncogenic transformation
- Reduced activation of NF-kappaB via impaired PI3K/Akt activation under increased TNF-alpha levels could result in increased apoptosis of vitiliginous keratinocytes.
- bFGF augments hypoxia induced VEGF release in breast cancer cells mainly through the PI3K pathway and partly depending on HIF-1 activity.
- C allele is a causal variant capable of attenuating insulin resistance in obese children.
- Our data indicate that different signalling pathways are involved in retinoic acid-induced up-regulation of the secretases.
- PI3Kalpha and -beta present distinct activation requirements and kinetics in G(1) phase, with a selective action of PI3Kalpha at the G(0)/G(1) phase transition
- Phosphoinositide 3-kinase p110beta inhibitor TGX-221 inhibited shear-induced platelet activation and protected platelet function during extracorporeal circulation.
- p85alpha and p110beta are essential for androgen-stimulated AR transactivation, and their aberrant expression or activation might play an important role in prostate cancer progression
- required for sphingosine-1-phosphate -induced endothelial cell migration through activation of Rac1
- Although p110alpha activation is required to sustain the proliferation of established PIK3CA-mutant tumors, PTEN-deficient tumors are dependent instead on p110beta signaling.
- Rs361072 promoter variant of PIK3CB is associated with insulin resistance not with type 2 diabetes.
