Recombinant Human PI3K (p85 beta) Protein

Name: Recombinant Human PI3K (p85 beta) Protein
Brand: Beta LifeScience
SKU: BL-1278SG
Availability: InStock

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Tag	His
Host Species	Human
Accession	NM_005027
Synonym	PIK3R2, P85B, p85-BETA
Background	Phosphatidylinositol 3-kinase (PI3K) is a lipid kinase that phosphorylates the inositol ring of phosphatidylinositol and related lipid products at the 3-prime position. PI3K p85 subunit which is the regulatory subunit of PI3K and consists of 2 closely related proteins, p85-alpha and p85-beta (1). The activation of PI3K signaling in influenza A virus-infected cells is important for efficient virus replication (2). PI3K signaling in T cells can lead to organ-specific autoimmunity and the class IA PI3K-deficient mice manifest the cardinal features of human primary Sjogren-€™s syndrome-like disease (3).
Description	Recombinant full length human PI3K (p85beta) was produced by baculovirus in Sf9 insect cells, fused with a His tag at N-terminus.
Source	Sf9 insect cells
AA Sequence	Full Length
Molecular Weight	~88 kDa
Purity	For specific purity information on a given lot, see related COA.
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Formulation	Recombinant protein is supplied in 50mM Tris-HCl, pH 7.5, 50mM NaCl, 10mM Glutathione, 0.25mM DTT, 0.1mM EDTA, 0.1mM PMSF and 25% glycerol.
Stability	The recombinant protein is stable for up to 12 months at -70°C
Usage	For Research Use Only
Storage	Recombinant Human PI3K (p85 beta) Protein should be stored should be stored at < -70°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function	Regulatory subunit of phosphoinositide-3-kinase (PI3K), a kinase that phosphorylates PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Binds to activated (phosphorylated) protein-tyrosine kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane. Indirectly regulates autophagy. Promotes 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.
Protein Families	PI3K p85 subunit family
Database References	HGNC: 8980 OMIM: 603157 KEGG: hsa:5296 STRING: 9606.ENSP00000471914 UniGene: PMID: 27729613 this study shows that targeted depletion of PIK3R2 induces regression of lung squamous cell carcinoma PMID: 27835880 Data show that phosphoinositol-3 kinase regulatory subunit 2 (PIK3R2) mRNA is a direct target of miR-126-3p. PMID: 27191494 Data indicate that miR-126 expression negatively correlates with p85beta in CLL patients and that miR-126 can effectively target p85beta in a cell-line system. PMID: 28299881 Mosaic mutations in PIK3CA or PIK3R2 which activate class 1A PI3K cause severe non-ketotic hypoglycaemia in a subset of patients, with the metabolic phenotype presumably related to the extent of mosaicism within the liver PMID: 28566443 PIK3R2 D557H mutation causes polymicrogyria, corpus callosum hyperplasia and focal cortical dysplasia. PMID: 26860062 miR-3151 silencing by DNA methylation protected chronic lymphocytic leukemia cells from apoptosis by over-expression of its direct targets MADD and PIK3R2, constitutive activation of MEK/ERK and PI3K/AKT signaling , and over-expression of MCL1. PMID: 26517243 pik3r2 was confirmed to be a direct target of miR126 in prostate cancer. PMID: 26677064 indicated that miR-126 expression was negatively correlated with PIK3R2 mRNA expression PMID: 26723864 The miR-126 was found to act as proliferation suppressor targeting PIK3R2 gene and reducing p85beta (a regulatory subunit of PI3K kinase) protein translation and lower AKT kinase activity. PMID: 26384552 Constitutional and mosaic mutations in the PIK3R2 gene are associated with developmental brain disorders ranging from Bilateral perisylvian polymicrogyria with a normal head size to the megalencephaly-polymicrogyria-polydactyly-hydrocephalus syndrome. PMID: 26520804 The authors show that this potentiation involves reorganization of the natural CrkL-p85beta complex into a novel trimeric complex where influenza A virus NS1 serves as a bridging factor. PMID: 26099693 the metastasis and angiogenesis functions of miR-126-3p were mediated by LRP6 and PIK3R2. PMID: 25240815 Study indicates that miR-126 is a tumor suppressor that inhibits gastric cancer cells proliferation by targeting PI3KR2, Crk and PLK2. PMID: 24969300 FBXL2 mediates the ubiquitylation and degradation of p85beta on cell membranes. PMID: 23604317 miR-126-mediated phosphoinositide-3-kinase regulation, not only fine-tunes VEGF-signaling, but it strongly enhances the activities of Ang-1 on vessel stabilization and maturation. PMID: 22867989 p85beta phosphoinositide 3-kinase subunit regulates tumor progression PMID: 22733740 recombinant production, crystallization and X-ray structure determination at 2.0 A resolution of the SH3 domain of human p85beta is described PMID: 22102226 miR-126 could target both VEGFA and PIK3R2, and its expression was decreased in human breast cancer, implying that miR-126 may play a role in tumor genesis and growth by regulating the VEGF/PI3K/AKT signaling pathway PMID: 21249429 The crystal structure of human p85beta iSH2 determined to 3.3A resolution is reported. PMID: 21139197 Macropinocytosis is regulated by interactions between Abi1 pY213 and the C-terminal SH2 domain of p85-thereby linking Abl kinase signaling to p85-dependent regulation of macropinocytosis. PMID: 20598684 Overexpression of SH3 domain of p85beta inhibits influenza A virus replication. PMID: 20653952 the PTEN phosphatase is active against the PI3K p85beta subunit and dephosphorylates a protein involved in insulin signaling where known downstream consequences are increased cell migration, motility, and invasion. PMID: 20515662 oncogenic p85 mutations lead to a loss of a C2-iSH2 domain contact that is required for inhibition of p110alpha by p85. PMID: 19915146 NS5A mediates activation of beta-catenin in a phosphoinositide-3 kinase-dependent fashion. PMID: 19846673 Mutant viruses carrying NS1 with mutations in SH3 binding motif 1 failed to interact with p85ss and induce the subsequent activation of PI3K/Akt pathway. PMID: 17881440 in VSMCs exposed to hyperglycemia, IGF-I stimulation of Shc facilitates the transfer of Grb2 to p85 resulting in enhanced PI3K activation and AKT phosphorylation leading to enhanced cell proliferation and migration PMID: 18420583

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.