Recombinant Human Phosphatidylinositol 3-Kinase Regulatory Subunit Beta (PIK3R2) Protein (His-GST)

Name: Recombinant Human Phosphatidylinositol 3-Kinase Regulatory Subunit Beta (PIK3R2) Protein (His-GST)
Brand: Beta LifeScience
SKU: BLC-07473P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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

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Product Overview

Description	Recombinant Human Phosphatidylinositol 3-Kinase Regulatory Subunit Beta (PIK3R2) Protein (His-GST) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	O00459
Target Symbol	PIK3R2
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-GST
Target Protein Sequence	VEFLGPVALARPGPRPRGPRPLPARPRDGAPEPGLTLPDLPEQFSPPDVAP
Expression Range	75-125aa
Protein Length	Partial
Mol. Weight	36.9 kDa
Research Area	Immunology
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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.