Recombinant Human Serine/Threonine-Protein Phosphatase 2A 55 Kda Regulatory Subunit B Beta Isoform (PPP2R2B) Protein (His&Myc)

Beta LifeScience SKU/CAT #: BLC-06799P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.

Recombinant Human Serine/Threonine-Protein Phosphatase 2A 55 Kda Regulatory Subunit B Beta Isoform (PPP2R2B) Protein (His&Myc)

Beta LifeScience SKU/CAT #: BLC-06799P
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Product Overview

Description Recombinant Human Serine/Threonine-Protein Phosphatase 2A 55 Kda Regulatory Subunit B Beta Isoform (PPP2R2B) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 85% as determined by SDS-PAGE.
Uniprotkb Q00005
Target Symbol PPP2R2B
Species Homo sapiens (Human)
Expression System E.coli
Tag N-10His&C-Myc
Target Protein Sequence MEEDIDTRKINNSFLRDHSYATEADIISTVEFNHTGELLATGDKGGRVVIFQREQESKNQVHRRGEYNVYSTFQSHEPEFDYLKSLEIEEKINKIRWLPQQNAAYFLLSTNDKTVKLWKVSERDKRPEGYNLKDEEGRLRDPATITTLRVPVLRPMDLMVEATPRRVFANAHTYHINSISVNSDYETYMSADDLRINLWNFEITNQSFNIVDIKPANMEELTEVITAAEFHPHHCNTFVYSSSKGTIRLCDMRASALCDRHTKFFEEPEDPSNRSFFSEIISSISDVKFSHSGRYIMTRDYLTVKVWDLNMENRPIETYQVHDYLRSKLCSLYENDCIFDKFECVWNGSDSVIMTGSYNNFFRMFDRNTKRDVTLEASRENSKPRAILKPRKVCVGGKRRKDEISVDSLDFSKKILHTAWHPSENIIAVAATNNLYIFQDKVN
Expression Range 1-443aa
Protein Length Full Length
Mol. Weight 56.7 kDa
Research Area Neuroscience
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 The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment. Within the PP2A holoenzyme complex, isoform 2 is required to promote proapoptotic activity. Isoform 2 regulates neuronal survival through the mitochondrial fission and fusion balance.
Subcellular Location [Isoform 1]: Cytoplasm. Cytoplasm, cytoskeleton. Membrane.; [Isoform 2]: Cytoplasm. Mitochondrion. Mitochondrion outer membrane.
Protein Families Phosphatase 2A regulatory subunit B family
Database References

HGNC: 9305

OMIM: 604325

KEGG: hsa:5521

STRING: 9606.ENSP00000336591

UniGene: PMID: 29275362

  • New pathogenic threshold of PPP2R2B CAG-43 to be pathogenic for SCA12 diagnosis. PMID: 27864267
  • CAG triplet repeat expansion has been found in untranslated region of SCA12 gene in Indian spinocerebellar ataxia 12 patients. PMID: 27350687
  • Thus, Fcp1 coordinates Cdk1 and Gwl inactivation to derepress PP2A-B55, generating a dephosphorylation switch that drives mitosis progression. PMID: 26653855
  • investigated CAG copies within PPP2R2B in 29 patients with spinocerebellar ataxia who are excluded from the most common subtypes; 3 patients carried 53, 46 and 54 CAG repeats respectively, while the other 26 cases harbored CAG repeats less than 30 PMID: 25634432
  • IER5 functions as a positive feedback regulator of HSF1 and that this process involves PP2A/B55 and HSF1 dephosphorylation. PMID: 25816751
  • Bcl-2 phosphorylation at Ser70 by selective tyrosine nitration of PP2A-B56delta stabilizes its antiapoptotic activity PMID: 25082878
  • Inactivation of protein-phosphatase 2A causing hyperphosphorylation of paraprotein targets in monoclonal gammopathy of undetermined significance, multiple myeloma and Waldenstrom's macroglobulinemia is due to an exchange of its regulatory subunits PMID: 24676687
  • We demonstrate that PP2A/B55 is required for Gwl dephosphorylation at the essential Cdk site Thr194. Ensa/ARPP19 dephosphorylation is mediated by the RNA PMID: 24391510
  • PP2A-B55beta promotes cyclin E1 overexpression by antagonizing its degradation and its inhibition could represent a therapeutic mechanism for abrogating cyclin E1 function in cancers PMID: 24509904
  • Bod1 regulates protein phosphatase 2A at mitotic kinetochores. PMID: 24157919
  • Differential autophagic neuronal cell death under stress is determined by the cytoplasmic and mitochondrial-specific PPP2R2B isoforms. PMID: 23381641
  • Single nucleotide polymorphisms in PPP2R2B is associated with drug response in breast cancer. PMID: 23034890
  • Data indicate that PPP2R2B gene product PP2A/Bbeta2 activates the mitochondrial fission enzyme dynamin-related protein 1 (Drp1) by dephosphorylating Ser656. PMID: 22583914
  • This study suggested that PPP2R2B CAG expansion mutation might lead increase induction of Spinocerebellar ataxia type 12. PMID: 21827912
  • defective production of PP2A Bbeta upon IL-2 deprivation results in apoptosis resistance and longer survival of autoreactive T cells, in a subset of SLE patients PMID: 21746932
  • oxidative stress induced by mitochondrial dysfunction causes elevated expression of ppp2r2b and plays a causal role in SCA12; and reduction of ROS is a potential therapeutic intervention for this neuropathy PMID: 21471219
  • results indicate that the A variant of the rs319217 SNP of the PPP2R2B gene is a marker of better prognosis in breast cancer PMID: 20669227
  • CAG repeat lengths in the PPP2R2B gene may be potential genetic markers for Alzheimer disease susceptibility in the Japanese population. PMID: 21029765
  • PPP2R2B, encoding the B55beta regulatory subunit of the PP2A complex, is epigenetically inactivated by DNA hypermethylation in colorectal cancer. PMID: 21075311
  • Autosomal dominant cerebellar ataxia mapping to 5q31-q33.1 has no CAG repeat expansion or other mutations of the PPP2R2B gene. PMID: 20937954
  • Quantitative methylation analysis identified ABCB1, FOXC1, PPP2R2B and PTEN as novel genes to be methylated in ductal carcinoma in situ. PMID: 20056007
  • The CAG repeat in SCA12 functions as a cis element to up-regulate PPP2R2B expression. PMID: 20533062
  • We investigated methylation patterns in the promoter regions of ABCB1, ATM, BRCA1, CDH3, CDKN2A, CXCR4, ESR1, FBXW7, FOXC1, GSTP1, IGF2, HMLH1, PPP2R2B, and PTEN75 in well-described pre-treatment samples from locally advanced breast cancer PMID: 20338046
  • Cells with ectopically expressed PPP2R2B were shown predisposed to autophagy and oxidative stress induced cell death. PMID: 20017961
  • a novel ATM-dependent mechanism is regulating association of B55 subunits with nuclear PP2A in response to IR PMID: 11723136
  • Cyclin G recruits PP2A in order to modulate the phosphorylation of Mdm2 and thereby to regulate both Mdm2 and p53. PMID: 11983168
  • Phosphorylation of bestrophin is regulated by PP2A. PMID: 12058047
  • SCA12 triplet expansion rate in Italian ataxia patients PMID: 12140678
  • Analysis of CTA/CTG and CAG polymorphism in a Polish control group. PMID: 14960773
  • phospholipase D suppresses protein phosphatase 2A and is involved in the mTOR survival pathway in the transformation of human cells PMID: 16109716
  • PP2A plays a positive rather than a negative role in the regulation of IKKbeta PMID: 16126728
  • analysis of a founder for SCA12 in the Indian population PMID: 16138911
  • We therefore propose that PP2A plays a crucial role in the maintenance of cell-cell adhesion through recruitment of IQGAP1 to the Rac-bound E-cadherin-catenins complex. PMID: 16245300
  • The tumor suppressor PP2A is functionally inactivated in blast crisis CML through the inhibitory activity of the BCR/ABL-regulated SET protein. PMID: 16286244
  • PP2A-mediated dephosphorylation of HSP27 and tau correlated with PP2A-induced preservation of endothelial cell cytoskeleton PMID: 16475161
  • Cyclin G2 may modulate the cell cycle and cellular division processes through modulation of PP2A and centrosomal associated activities. PMID: 17123511
  • The small t antigen (ST) of DNA tumor virus SV40 inhibits PP2A phosphatase activity through its N-terminal J domain. PMID: 17529992
  • results suggest that the PPP2R2B gene CAG repeat polymorphism may be functional and may, in part, play a role in conferring susceptibility to Alzheimer disease and essential tremor in Taiwan PMID: 18484086
  • Adenovirus E4orf4 protein downregulates MYC expression through interaction with the PP2A-B55 subunit PMID: 18653458
  • Results suggest that Parkinsonism (PD) and multiple system atrophy (MSA) are not associated with spinocerebellar ataxia 12 (SCA12) and it is not necessary to screen SCA12 in PD and MSA patients. PMID: 18973067
  • Clinical trial and genome-wide association study of gene-disease association, gene-environment interaction, and pharmacogenomic / toxicogenomic. (HuGE Navigator) PMID: 18519826

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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.

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