Recombinant Human Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform (PPP2R1A)

Code CSB-YP018562HU
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Source Yeast
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Code CSB-EP018562HU
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Source E.coli
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Code CSB-EP018562HU-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP018562HU
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Source Baculovirus
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Code CSB-MP018562HU
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
PPP2R1A
Uniprot No.
Alternative Names
2AAA_HUMAN; 6330556D22Rik; Alpha isoform of regulatory subunit A; protein phosphatase; DKFZp470L0914; Medium tumor antigen-associated 61 kDa protein; MGC128399; MGC786; MGC83000; MGC95083; PP2A Aalpha; PP2A; PP2A subunit A isoform PR65-alpha; PP2A subunit A isoform R1-alpha; PP2A; subunit A; PR65-alpha isoform; PP2A; subunit A; R1-alpha isoform; PP2AAALPHA; Ppp2r1a; ppp2r1a-b; PR65; PR65-alpha; PR65A; Protein phosphatase 2 (formerly 2A); regulatory subunit A (PR 65); alpha isoform; Protein phosphatase 2 (Formerly 2A); regulatory subunit A (PR 65); alpha isoform; isoform CRA_a; Protein phosphatase 2 (formerly 2A); regulatory subunit A,; Protein phosphatase 2 regulatory subunit A alpha; Protein phosphatase 2; 65-KD regulatory subunit A; alpha; Protein phosphatase 2; regulatory subunit A; alpha isoform; Protein phosphatase 2; structural/regulatory subunit A; alpha; PPP2R1A; Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
Species
Homo sapiens (Human)
Expression Region
2-589
Target Protein Sequence
AAADGDDSL YPIAVLIDEL RNEDVQLRLN SIKKLSTIAL ALGVERTRSE LLPFLTDTIY DEDEVLLALA EQLGTFTTLV GGPEYVHCLL PPLESLATVE ETVVRDKAVE SLRAISHEHS PSDLEAHFVP LVKRLAGGDW FTSRTSACGL FSVCYPRVSS AVKAELRQYF RNLCSDDTPM VRRAAASKLG EFAKVLELDN VKSEIIPMFS NLASDEQDSV RLLAVEACVN IAQLLPQEDL EALVMPTLRQ AAEDKSWRVR YMVADKFTEL QKAVGPEITK TDLVPAFQNL MKDCEAEVRA AASHKVKEFC ENLSADCREN VIMSQILPCI KELVSDANQH VKSALASVIM GLSPILGKDN TIEHLLPLFL AQLKDECPEV RLNIISNLDC VNEVIGIRQL SQSLLPAIVE LAEDAKWRVR LAIIEYMPLL AGQLGVEFFD EKLNSLCMAW LVDHVYAIRE AATSNLKKLV EKFGKEWAHA TIIPKVLAMS GDPNYLHRMT TLFCINVLSE VCGQDITTKH MLPTVLRMAG DPVANVRFNV AKSLQKIGPI LDNSTLQSEV KPILEKLTQD QDVDVKYFAQ EALTVLSLA
Protein Length
Full Length of Mature Protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

Function
The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit. Upon interaction with GNA12 promotes dephosphorylation of microtubule associated protein TAU/MAPT. Required for proper chromosome segregation and for centromeric localization of SGO1 in mitosis.
Gene References into Functions
  1. PP2A controls mitotic exit through EG5 dephosphorylation. PMID: 28487562
  2. Total PP2A activity and PPP2R1A-associated PP2Ac activity were significantly increased in cells overexpressing PPP2R1A-WT. In addition, overexpression of PPP2R1A-WT increased cell proliferation in vitro and tumor growth in vivo PMID: 27272709
  3. PPP2R1A mutations occur in a subset of gastrointestinal stromal tumors and are associated with a high malignant potential that leads to decreased disease-free survival and overall survival PMID: 27469332
  4. Results demonstrated that the promotive effect of eEF-2K on glycolysis resulted from the kinase-mediated restriction of synthesis of the protein phosphatase 2A-A (PP2A-A). PMID: 27181208
  5. PPP2R1A mutation is associated with endometrial carcinoma progression and abdominopelvic metastasis. PMID: 27348297
  6. PPP2R1A mutations affect PP2A function and oncogenic signaling, illuminating the genetic basis for serous EC development. PMID: 27485451
  7. PR65A phosphorylation regulates PP2A complex signaling. PMID: 24465463
  8. Our results suggest that IH-induced ROS generation increases PP2A activation and subsequently downregulates ERK1/2 activation, which results in inhibition of PC12 cell proliferation through G0/G1 phase arrest and NGF-induced neuronal differentiation. PMID: 24885237
  9. The two functional variants in PPP2R1A and PPP2R5E and their combinations are associated with lung cancer risk in the Chinese. PMID: 24204789
  10. Partial unfolding of PR65/A impacts catalysis by altering the proximity of bound catalytic subunit and substrate. PMID: 24120762
  11. For PPP2R1A, a heterozygous, somatic mutation (c.771G>T, p.W257C) was identified in 1 out of 37 patients (2.7%) with primary ovarian endometrioid carcinoma. PMID: 23588898
  12. gene transcription of PPP2R1A regulated by the polymorphism and methylation in the promoter region PMID: 23555712
  13. This study indicates that the PPP2R1A mutation occurs at a lower frequency compared to other gynecological malignancies, irrespective of the histological subtype PMID: 23267135
  14. the frequent mutation of PPP2R1A in the serous type of uterine cancer, a low frequency of mutation in endometrioid endometrial cancer and absence of mutation in uterine carcinosarcoma. PMID: 21882256
  15. Our findings suggest that functional genetic variants in the proximal promoter of the PP2A-Aalpha gene and their haplotypes are critical in the regulation of transcriptional activation. PMID: 21889517
  16. identified somatic missense mutations in 40.8% of high-grade serous endometrial tumours and 5% of endometrial endometrioid carcinomas; mutations identified in ovarian tumours at lower frequencies;no mutations found in high- or low-grade serous carcinoma PMID: 21381030
  17. PPP2R1A somatic mutations occur in certain types of uterine and ovarian neoplastic lesions, especially uterine serous carcinomas PMID: 21435433
  18. PP2A-mediated dephosphorylation of Carma1 is a critical step to limit T-cell activation and effector cytokine production. PMID: 21157432
  19. genes mutated in ovarian clear cell carcinoma(OCCC);data suggest PPP2R1A functions as an oncogene and ARID1A as tumor-suppressor gene; in 42 OCCCs, 7% had mutations in PPP2R1A and 57% in ARID1A; suggests aberrant chromatin remodeling contributes to OCCC PMID: 20826764
  20. Data show that upon hypoxia, the TGF-beta-induced phosphorylation of Smad3 was inhibited, although Smad2 remained phosphorylated, and Smad3 was dephosphorylated by PP2A. PMID: 19951945
  21. PP2A-A alpha transcriptional regulation is mediated by multiple factors including AP-2alpha, CREB, ETS-1, and SP-1 PMID: 19750005
  22. Data show that DSB promote PP2A to associate with Ku 70 and Ku 86. PMID: 19794960
  23. PP2A-A has a role in the failure of beta1 integrin dephosphorylation at threonines 788 and 789 in tumor cell lines PMID: 14532964
  24. PP2A-mediated dephosphorylation of BCL-2 is required to protect BCL-2 from proteasome-dependent degradation, affecting resistance to ER stress PMID: 16717086
  25. dysfunction of E-cadherin due to its endocytosis may occur in some proportion of human breast carcinomas in which the PP2A-A protein is lost or significantly reduced PMID: 16930554
  26. protein phosphatase 2a recruitment to I-kappaB kinase gamma/NF-kappaB essential modulator is regulated by heptad repeats, which are targeted by HTLV-I tax PMID: 17314097
  27. The results of these experiments indicate that the HSF2 region comprising amino acids 343-363 is important for A subunit interaction. PMID: 17688198

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Involvement in disease
Mental retardation, autosomal dominant 36 (MRD36)
Subcellular Location
Cytoplasm. Nucleus. Chromosome, centromere. Lateral cell membrane. Cell projection, dendrite.
Protein Families
Phosphatase 2A regulatory subunit A family
Database Links

HGNC: 9302

OMIM: 605983

KEGG: hsa:5518

STRING: 9606.ENSP00000324804

UniGene: Hs.467192

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