Recombinant Human Serine/Threonine-Protein Phosphatase 2A Catalytic Subunit Alpha Isoform (PPP2CA) Protein (His&Myc)

Name: Recombinant Human Serine/Threonine-Protein Phosphatase 2A Catalytic Subunit Alpha Isoform (PPP2CA) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-00809P
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 Serine/Threonine-Protein Phosphatase 2A Catalytic Subunit Alpha Isoform (PPP2CA) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P67775
Target Symbol	PPP2CA
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	MDEKVFTKELDQWIEQLNECKQLSESQVKSLCEKAKEILTKESNVQEVRCPVTVCGDVHGQFHDLMELFRIGGKSPDTNYLFMGDYVDRGYYSVETVTLLVALKVRYRERITILRGNHESRQITQVYGFYDECLRKYGNANVWKYFTDLFDYLPLTALVDGQIFCLHGGLSPSIDTLDHIRALDRLQEVPHEGPMCDLLWSDPDDRGGWGISPRGAGYTFGQDISETFNHANGLTLVSRAHQLVMEGYNWCHDRNVVTIFSAPNYCYRCGNQAAIMELDDTLKYSFLQFDPAPRRGEPHVTRRTPDYFL
Expression Range	1-309aa
Protein Length	Full Length
Mol. Weight	43.0 kDa
Research Area	Cancer
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	PP2A is the major phosphatase for microtubule-associated proteins (MAPs). PP2A can modulate the activity of phosphorylase B kinase casein kinase 2, mitogen-stimulated S6 kinase, and MAP-2 kinase. Cooperates with SGO2 to protect centromeric cohesin from separase-mediated cleavage in oocytes specifically during meiosis I. Can dephosphorylate SV40 large T antigen and p53/TP53. Activates RAF1 by dephosphorylating it at 'Ser-259'. Mediates dephosphorylation of WEE1, preventing its ubiquitin-mediated proteolysis, increasing WEE1 protein levels, and promoting the G2/M checkpoint. Mediates dephosphorylation of MYC; promoting its ubiquitin-mediated proteolysis: interaction with AMBRA1 enhances interaction between PPP2CA and MYC. Mediates dephosphorylation of FOXO3; promoting its stabilization: interaction with AMBRA1 enhances interaction between PPP2CA and FOXO3.
Subcellular Location	Cytoplasm. Nucleus. Chromosome, centromere. Cytoplasm, cytoskeleton, spindle pole.
Protein Families	PPP phosphatase family, PP-1 subfamily
Database References	HGNC: 9299 OMIM: 176915 KEGG: hsa:5515 STRING: 9606.ENSP00000418447 UniGene: PMID: 30275201 PP2A overexpression is associated with lung metastasis in colorectal cancer . PMID: 30144452 Suspension survival mediated by PP2A-STAT3-Col XVII determines tumor initiation and metastasis in cancer stem cells. PMID: 27306323 alpha-Syn bound to PP2A Calpha by the hydrophobic interaction and upregulated its activity. Blocking the hydrophobic domain of alpha-Syn or hydrophilic mutation on the residue I123 in PP2A Calpha all reduced PP2A activity upregulation by alpha-Syn. PMID: 29996119 The results showed SNPs near PPP2CA were associated with decreased expression of PPP2CA mRNA in PBMCs from patients with SLE and suggested that the mRNA expression of the gene may be correlated with the pathogenesis of SLE. PMID: 28144936 This study demonstrated an association of PPP2CA (rs10491322 and rs7704116) with systemic lupus erythematosus susceptibility in a Chinese Han population. Furthermore, the minor allele of PPP2CA rs10491322 as a risk factor was correlated with immunologic disorders for systemic lupus erythematosus. PMID: 29979448 RAB9 competes with the catalytic subunit PPP2CA in binding to PPP2R1A. This competitive association has an important role in controlling the PP2A catalytic activity. PMID: 27611305 Results show that miR-199b is a tumor suppressor emerges as a potential contributing mechanism to inhibit PP2A via PP2A inhibitor SET (SET) overexpression in metastatic colorectal cancer (mCRC). PMID: 27517624 Data show that protein phosphatase-2A (PP2A) was upregulated in lung adenocarcinoma cell lines that were transfected with midline 1 E3 ubiquitin-protein ligase (MID1)-siRNA, suggesting MID1 negatively regulates PP2A in lung adenocarcinoma. PMID: 29450633 B55alpha-PP2A mutations in acute myeloid leukemia have roles in leukemogenesis by promoting AKT T308 phosphorylation and sensitivity to AKT inhibitor-induced growth arrest PMID: 27531894 This work has significantly advanced our understanding of the RACK1/PP2A complex and suggests a pro-carcinogenic role for the RACK1/PP2A interaction. This work suggests that approaches to target the RACK1/PP2A complex are a viable option to regulate PP2A activity and identifies a novel potential therapeutic target in the treatment of breast cancer. PMID: 27600565 Moreover, PP2Acalpha2-overexpressed cells demonstrated increased expression of IGBP1, activated mTORC1 signaling to reduce basal autophagy and increased anchorage-independent growth. Our study provides new insights into the complex mechanisms of PP2A regulation. PMID: 29066346 protein phosphatase 2A (PP2A)-mediated Raf-MEK-ERK signaling was involved in glutaminolysis in endothelial cells. PMID: 27612201 Studies indicate that protein phosphatase methylesterase-1 (PME-1) negatively regulates protein phosphatase 2A (PP2A) activity by highly complex mechanisms. PMID: 27913678 Binding of PP2A and Akt increased in response to cAMP or phosphatidic acid (PA), suggesting that their binding is directly responsible for the inactivation of Akt during decidualization. PMID: 27696687 Knockdown of Alpha4 preferentially impacts the expression of PP4c and PP6c compared to expression levels of PP2Ac. PMID: 27169767 these data support a role for the novel PP2Ac-CIN85 complex in supporting integrin-dependent platelet function by dampening the phosphatase activity. PMID: 27334924 PP2Ac upregulation has a poor prognostic impact on the overall survival of hepatocellular carcinoma (HCC) patients and contributes to the aggressiveness of HCC. PP2Ac may represent a potential therapeutic target for HCC. PMID: 26618405 Data show that downregulating proto-oncogene protein Akt (p-Akt) by inhibiting PP2A inhibitor SET-mediated protein phosphatase 2A (PP2A) inactivation determined the pro-apoptotic effects of EMQA and paclitaxel combination treatment. PMID: 26575017 Data suggest a critical role for the I2PP2A protein (SET)-protein phosphatase-2A (PP2A) signaling axis in Pten protein (Pten) deficient castration resistant prostate cancer (CRPC) progression. PMID: 26563471 that loss of glucocerebrosidase function may contribute to SNCA accumulation through inhibition of autophagy via PPP2A inactivation PMID: 26378614 Data show that loss of epithelial membrane protein 2 (EMP2) is involved in sphingosylphosphorylcholine (SPC)-induced phosphorylation of keratin 8 (K8) via ubiquitination of protein phosphatase 2 (PP2A) through alpha4 phosphoprotein by caveolin-1 (cav-1). PMID: 26876307 Data show that the protein phosphatase 2A (PP2A)/c-jun N-Terminal Kinase (JNK)/Sp1 transcription factor/CDK1 kinase pathway and the autophagy/cyclin kinase inhibitor p21 pathway participated in G2/M cell cycle arrest triggered by PP2A inhibitors. PMID: 26053095 Data indicate that LB100 attenuates protein phosphatase 2A (PP2A) activity alone and following radiation. PMID: 25939762 Concurrent mTORC1 inactivation and PP2A-B55alpha stimulation fuel ULK1-dependent autophagy. PMID: 26310906 Data show that the biogical effect of inhibitor-2 of protein phosphatase-2A (SET) on proliferation and invasion was mediated by the inhibition of the protein phosphatase 2A (PP2A). PMID: 25945834 Binding of calmodulin changes the calcineurin regulatory region to a less dynamic conformation. PMID: 25956027 MID1 catalyzes the ubiquitination of protein phosphatase 2A and mutations within its Bbox1 domain disrupt polyubiquitination of alpha4 but not of PP2Ac in X-linked Opitz syndrome. PMID: 25207814 Mutations in the structurally buried D38 residue of PP2Calpha (PPM1A) redefined the water-mediated hydrogen network in the active site and selectively disrupted M2 metal ion binding. PMID: 25708299 possible role of an miR-155-PP2Ac loop in regulating IL-2 release PMID: 25253569 Increased PP2A activity and reduced phosphorylation of PP2A were observed in alpha-synuclein overexpression primary cortex neurons. PMID: 25567480 Idiopathic pulmonary fibrosis fibroblast interaction with polymerized type I collagen results in an aberrant PP2A/HDAC4 axis, which suppresses miR-29, causing a pathologic increase in type I collagen expression. PMID: 25612003 Alterations affecting PP2A subunits together with the deregulation of endogenous PP2A inhibitors such as CIP2A and SET have been described as contributing mechanisms to inactivate PP2A in prostate cancer. PMID: 26234767 GSK-3b and PP2A regulate each other and control tau phosphorylation both directly and indirectly through each other. PMID: 25219467 Reduced expression of PP2A/PR65 in ameloblastoma compared with normal oral mucosa indicates that PP2A/PR65 is involved in the occurrence and development of ameloblastoma. PMID: 24054836 HSP105 depletion disrupts the integration of protein phosphatase 2A into the beta-catenin degradation complex, favoring the hyperphosphorylation and degradation of beta-catenin. PMID: 25645927 Data suggest that expression of PP2A (protein phosphatase 2 catalytic subunit alpha) and PTEN (phosphatase and tensin homolog) is down-regulated in adenomyosis as compared to normal endometrium; expression of survivin appears to be up-regulated. PMID: 25152517 Studies indicate that oncoprotein CIP2A (KIAA1524) controls oncogenic cellular signals by suppressing protein phosphatase 2A (PP2A). PMID: 25015035 Findings suggest the possible contribution of SET protein to the tumor progression and the utility of protein phosphatase 2A (PP2A) activator, FTY720 for treatment of alveolar soft part sarcoma (ASPS). PMID: 24621013 this study suggests that the tightly linked regulatory loop comprised of the SIK2-PP2A and CaMKI and PME-1 networks may function in fine-tuning cell proliferation and stress response. PMID: 24841198 These results suggest that the aberrant expression of PP2A in human clear cell renal cell carcinoma PMID: 24696731 decreased eEF2 phosphorylation, mediated by increased PP2A activity, contributes to resistance to HER2 inhibition and may provide novel targets for therapeutic intervention in HER2 positive breast cancer which is resistant to HER2 targeted therapies. PMID: 24958351 PPP2AC activity is required for SREBP-2 DNA binding. PMID: 24770487 Phosphorylated PP2A is an alteration that determines poor outcome in metastatic colorectal cancer. PMID: 25003662 the alpha4 N-terminus binding to endogenous PP2Ac and PABP, and the C-terminus to EDD, is reported. PMID: 24145130 Our findings suggest that PPP2CA downregulation serves as a molecular link between gain of castration-resistance and aggressive PCa phenotype, and its restoration could be an effective preventive/therapeutic approach against the advanced disease. PMID: 24642616 This result combined with a number of biophysical analyses provide evidence that the coiled coil domain of striatin 3 and the PP2A A subunit form a stable core complex with a 2:2 stoichiometry PMID: 24550388 Inhibition of PP2A by okadaic acid curtailed the free fatty acids induced upregulation of SREBP1 expression, fatty acid synthase promoter transcriptional activity and lipid accumulation in HepG2 cells PMID: 23184344 PP2A constitutively dephosphorylates dCK in cells and negatively regulates its activity. PMID: 24462681 Data indicate that TCDD or omeprazole caused protein phosphatase 2A (PP2A)-mediated dephosphorylation of Sp1 transcription factor at Ser-59 and induced CYP1A1 transcription. PMID: 24382322

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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.

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