Recombinant Human Protein phosphatase 1A(PPM1A)

Code CSB-EP018489HU
Size US$1726
Image
  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

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Product Details

Purity Greater than 90% as determined by SDS-PAGE.
Target Names PPM1A
Uniprot No. P35813
Research Area Signal Transduction
Alternative Names Protein phosphatase 2C isoform alpha; EC 3.1.3.16; FLJ42306; IA; MGC9201; Mpp alpha ; PP2C alpha; PP2C-alpha; PP2CA; PP2Calpha; PPM 1A; PPM1A; PPM1A_HUMAN; PPPM1A; Protein phosphatase 1A (formerly 2C) magnesium dependent alpha isoform; Protein phosphatase 1A; Protein phosphatase 1A magnesium dependent alpha ; Protein phosphatase 2C alpha; Protein phosphatase 2C alpha isoform; Protein phosphatase 2C isoform alpha; Protein phosphatase IA; Protein phosphatase, Mg2+/Mn2+ dependent, 1A
Species Homo sapiens (Human)
Source E.coli
Expression Region 1-382aa
Target Protein Sequence GAFLDKPKMEKHNAQGQGNGLRYGLSSMQGWRVEMEDAHTAVIGLPSGLESWSFFAVYDGHAGSQVAKYCCEHLLDHITNNQDFKGSAGAPSVENVKNGIRTGFLEIDEHMRVMSEKKHGADRSGSTAVGVLISPQHTYFINCGDSRGLLCRNRKVHFFTQDHKPSNPLEKERIQNAGGSVMIQRVNGSLAVSRALGDFDYKCVHGKGPTEQLVSPEPEVHDIERSEEDDQFIILACDGIWDVMGNEELCDFVRSRLEVTDDLEKVCNEVVDTCLYKGSRDNMSVILICFPNAPKVSPEAVKKEAELDKYLECRVEEIIKKQGEGVPDLVHVMRTLASENIPSLPPGGELASKRNVIEAVYNRLNPYKNDDTDSTSTDDMW
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight 69.3kDa
Protein Length Full Length
Tag Info N-terminal GST-tagged
Form Liquid or 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 If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is 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°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting
and FAQs
Protein FAQs
Storage Condition Store at -20°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.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA Please contact us to get it.

Target Data

Function Enzyme with a broad specificity. Negatively regulates TGF-beta signaling through dephosphorylating SMAD2 and SMAD3, resulting in their dissociation from SMAD4, nuclear export of the SMADs and termination of the TGF-beta-mediated signaling. Dephosphorylates PRKAA1 and PRKAA2. Plays an important role in the termination of TNF-alpha-mediated NF-kappa-B activation through dephosphorylating and inactivating IKBKB/IKKB.
Gene References into Functions
  1. PPM1A as a negative threshold regulator of M1-type monocyte-to-macrophage differentiation. PMID: 29343725
  2. Here the authors establish PPM1A as a checkpoint target used by Mycobacterium tuberculosis to suppress macrophage apoptosis. Overproduction of PPM1A suppressed apoptosis of Mycobacterium tuberculosis-infected macrophages by a mechanism that involves inactivation of the c-Jun N-terminal kinase (JNK). PMID: 28176854
  3. Present study suggests that HBx-induced degradation of PPM1a is a novel mechanism for over-activation of TGF-beta pathway in HCC development. PMID: 27121309
  4. Findings show that HCV infection and replication decreased PPM1A abundance, mediated by NS3, in hepatoma cells. Compared to normal liver tissues, the expression of PPM1A was significantly decreased in the HCC tumor tissues and adjacent non-tumor tissues through its regulation by NS3 which promotes its ubiquitination and proteasomal degradation. PMID: 28283039
  5. These data suggest that PPM1A, which had previously been shown to play a role in the antiviral response to Herpes Simplex virus infection, also governs the antibacterial response of macrophages to bacteria, or at least to Mycobacterium tuberculosis infection PMID: 27004401
  6. establish PPM1A as a novel repressor of the SMAD3 pathway in renal fibrosis PMID: 27328942
  7. Report a tumor-suppressive function of PPM1A and an independent relationship to Smad4 in pancreatic ductal adenocarcinoma. PMID: 27195906
  8. hydrogen/deuterium exchange-mass spectrometry and molecular dynamics to characterize conformational changes in PP2Calpha between the active and inactive states PMID: 28481111
  9. In a nested case control study of ischemic stroke, there was an epigenome-wide association for cg04985020 (PPM1A; P=1.78x10(-07)) with vascular recurrence in patients treated with aspirin. PMID: 27301936
  10. findings demonstrate a novel regulatory circuit in which STING and TBK1 reciprocally regulate each other to enable efficient antiviral signaling activation, and PPM1A dephosphorylates STING and TBK1 PMID: 25815785
  11. The TGF-beta/Smad signaling system decreases its activity through strong negative regulation. We provide evidence for a new negative feedback loop through PPM1A upregulation. PMID: 24901250
  12. Loss of PPM1A is associated with the development of tumor invasion in bladder cancer patients. PMID: 25026293
  13. PPM1A is a RelA phosphatase that regulates NF-kappaB activity and that PPM1A has tumor suppressor-like activity. PMID: 23812431
  14. a nuclear envelope-localized mechanism of inactivating TGF-beta signaling in which MAN1 competes with transcription factors for binding to Smad2 and Smad3 and facilitates their dephosphorylation by PPM1A. PMID: 23779087
  15. phosphatase activity toward phosphopeptide substrates by PP2Calpha and Wip1 requires the binding of a Mg(2)+ ion to the low-affinity site. PMID: 23906386
  16. PPM1A negatively regulates ERK by directly dephosphorylating its pThr202 position early in epidermal growth factor stimulation. Additional kinetic studies reveal that key residues participate in phospho-ERK recognition by PPM1A. PMID: 23560844
  17. Studies indicate that phosphatase PPM1G is a component of the spliceosome and binds to protein YB-1 to affect alternative splicing. PMID: 22519956
  18. PPM1A inhibits HIV-1 infection and gene expression. PPM1A depletion in resting CD4+ T cells increases HIV-1 gene expression. PMID: 22727189
  19. High expression of LMP2 and low expression of PPM1A might play an important role in the motility and invasiveness of trophoblast cells and malignant transformation of hydatidiform mole. PMID: 22041443
  20. This work demonstrates that PPM1A/PP2Calpha, through dephosphorylation of Smad2/3, plays a critical role in terminating TGFbeta signaling. PMID: 16751101
  21. PPM1A plays an important role in controlling BMP signaling through catalyzing Smad1 dephosphorylation PMID: 16931515
  22. Aberrant location of expression/staining intensity of PTEN, PPM1A and P-Smad2 in hepatocellular carcinoma may impact disease progression. PMID: 17729405
  23. PTEN abrogates TGF-beta-induced Smad2/3 phosphorylation. This study establishes a novel role for nuclear PTEN in the stabilization of PPM1A. PMID: 18482992
  24. Overexpression of PPM1A and the related PPM1B greatly reduced Cdk9 T-loop phosphorylation PMID: 18829461
  25. Protein phosphatase 1A is essential to terminate I-kappa B Kinase-mediated NF-kappaappaB activation through binding to the activated form of I-kappa B Kinase and dephosphorylating I-kappa B Kinase at the conserved residues Ser177 and Ser181. PMID: 18930133
  26. The present data indicate that PPM1A plays a critical role in the regulation of normal placentation by inhibiting trophoblast migration and invasion. PMID: 19404668

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Subcellular Location Nucleus, Cytoplasm, cytosol, Membrane, Lipid-anchor
Protein Families PP2C family
Database Links

HGNC: 9275

OMIM: 606108

KEGG: hsa:5494

STRING: 9606.ENSP00000327255

UniGene: Hs.130036

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