Analytical Data
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Gene name
PPM1M
- Application
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Alternative Names
PPM1M; PPM1E; Protein phosphatase 1M; EC 3.1.3.16; Protein phosphatase 2C isoform eta; PP2C-eta; PP2CE
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q96MI6
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Expression Region
1-270 aa
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AA Sequence
MHLNGRCICP SDPQFVEEKG IRAEDLVIGA LESAFQECDE VIGRELEASG QMGGCTALVA VSLQGKLYMA NAGDSRAILV RRDEIRPLSF EFTPETERQR IQQLAFVYPE LLAGEFTRLE FPRRLKGDDL GQKVLFRDHH MSGWSYKRVE KSDLKYPLIH GQGRQARLLG TLAVSRGLGD HQLRVLDTNI QLKPFLLSVP QVTVLDVDQL ELQEDDVVVM ATDGLWDVLS NEQVAWLVRS FLPGNQEDPH RYCSCWGPAW AWVGASSKPK
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Molecular Weight
51.1 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
PPM1M, a member of the protein phosphatase 2C (PP2C) family, plays a significant role in cellular regulation by modulating various signaling pathways, particularly those involved in stress response, inflammation, and cell survival. Its ability to dephosphorylate target proteins provides a critical balance to phosphorylation events mediated by kinases, thus impacting processes such as apoptosis and cell proliferation. The dysregulation of PPM1M has been associated with various pathological conditions, including cancer, making it a target of interest for therapeutic interventions. Recent studies have focused on the reconstitution and characterization of recombinant PPM1M to better understand its structural and functional properties. By utilizing recombinant DNA technology, scientists can produce this phosphatase in a controlled environment, allowing for detailed biochemical assays to elucidate its enzymatic mechanisms and interactions with substrates. Additionally, this research facilitates the exploration of PPM1M's role in specific cellular contexts, potentially leading to insights into how its modulation can influence disease outcomes. Understanding PPM1M's function at a molecular level could offer novel avenues for drug development, particularly in targeting diseases where its activity is altered. As such, the investigation of PPM1M's properties is not only vital for basic biological research but also for advancing therapeutic strategies that aim to restore proper signaling pathways in disease states.
