Recombinant Human Protein Phosphatase 1A (PPM1A) Protein (GST)

Name: Recombinant Human Protein Phosphatase 1A (PPM1A) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-09253P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Protein Phosphatase 1A (PPM1A) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P35813
Target Symbol	PPM1A
Synonyms	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)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	GAFLDKPKMEKHNAQGQGNGLRYGLSSMQGWRVEMEDAHTAVIGLPSGLESWSFFAVYDGHAGSQVAKYCCEHLLDHITNNQDFKGSAGAPSVENVKNGIRTGFLEIDEHMRVMSEKKHGADRSGSTAVGVLISPQHTYFINCGDSRGLLCRNRKVHFFTQDHKPSNPLEKERIQNAGGSVMIQRVNGSLAVSRALGDFDYKCVHGKGPTEQLVSPEPEVHDIERSEEDDQFIILACDGIWDVMGNEELCDFVRSRLEVTDDLEKVCNEVVDTCLYKGSRDNMSVILICFPNAPKVSPEAVKKEAELDKYLECRVEEIIKKQGEGVPDLVHVMRTLASENIPSLPPGGELASKRNVIEAVYNRLNPYKNDDTDSTSTDDMW
Expression Range	1-382aa
Protein Length	Full Length
Mol. Weight	69.3kDa
Research Area	Signal Transduction
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	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.
Subcellular Location	Nucleus. Cytoplasm, cytosol. Membrane; Lipid-anchor.
Protein Families	PP2C family
Database References	HGNC: 9275 OMIM: 606108 KEGG: hsa:5494 STRING: 9606.ENSP00000327255 UniGene: Hs.130036

Gene Functions References

PPM1A as a negative threshold regulator of M1-type monocyte-to-macrophage differentiation. PMID: 29343725
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
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
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
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
establish PPM1A as a novel repressor of the SMAD3 pathway in renal fibrosis PMID: 27328942
Report a tumor-suppressive function of PPM1A and an independent relationship to Smad4 in pancreatic ductal adenocarcinoma. PMID: 27195906
hydrogen/deuterium exchange-mass spectrometry and molecular dynamics to characterize conformational changes in PP2Calpha between the active and inactive states PMID: 28481111
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
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
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
Loss of PPM1A is associated with the development of tumor invasion in bladder cancer patients. PMID: 25026293
PPM1A is a RelA phosphatase that regulates NF-kappaB activity and that PPM1A has tumor suppressor-like activity. PMID: 23812431
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
phosphatase activity toward phosphopeptide substrates by PP2Calpha and Wip1 requires the binding of a Mg(2)+ ion to the low-affinity site. PMID: 23906386
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
Studies indicate that phosphatase PPM1G is a component of the spliceosome and binds to protein YB-1 to affect alternative splicing. PMID: 22519956
PPM1A inhibits HIV-1 infection and gene expression. PPM1A depletion in resting CD4+ T cells increases HIV-1 gene expression. PMID: 22727189
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
This work demonstrates that PPM1A/PP2Calpha, through dephosphorylation of Smad2/3, plays a critical role in terminating TGFbeta signaling. PMID: 16751101
PPM1A plays an important role in controlling BMP signaling through catalyzing Smad1 dephosphorylation PMID: 16931515
Aberrant location of expression/staining intensity of PTEN, PPM1A and P-Smad2 in hepatocellular carcinoma may impact disease progression. PMID: 17729405
PTEN abrogates TGF-beta-induced Smad2/3 phosphorylation. This study establishes a novel role for nuclear PTEN in the stabilization of PPM1A. PMID: 18482992
Overexpression of PPM1A and the related PPM1B greatly reduced Cdk9 T-loop phosphorylation PMID: 18829461
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
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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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.