Analytical Data
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Gene name
PPP1R3D
- Application
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Alternative Names
PPP1R3D;Laforin
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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
O95685
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Expression Region
1-299aa
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AA Sequence
MSRGPSSAVL PSALGSRKLG PRSLSCLSDL DGGVALEPRA CRPPGSPGRA PPPTPAPSGC DPRLRPIILR RARSLPSSPE RRQKAAGAPG AACRPGCSQK LRVRFADALG LELAQVKVFN AGDDPSVPLH VLSRLAINSD LCCSSQDLEF TLHCLVPDFP PPVEAADFGE RLQRQLVCLE RVTCSDLGIS GTVRVCNVAF EKQVAVRYTF SGWRSTHEAV ARWRGPAGPE GTEDVFTFGF PVPPFLLELG SRVHFAVRYQ VAGAEYWDNN DHRDYSLTCR NHALHMPRGE CEESWIHFI
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Molecular Weight
32.5 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
PPP1R3D (Protein Phosphatase 1 Regulatory Subunit 3D) is a member of the PPP1R3 family, which plays a crucial role in regulating protein phosphatase 1 (PP1) activity, a key enzyme involved in various cellular processes, including glycogen metabolism, cell division, and signal transduction. Understanding PPP1R3D is essential because aberrations in its function have been linked to metabolic disorders and various diseases, including cancer and diabetes. The study of PPP1R3D recombinant protein has gained momentum in recent years as researchers seek to elucidate its structural and functional characteristics. Recombinant proteins enable detailed biochemical analyses and the exploration of interactions with other cellular components. Additionally, generating PPP1R3D in a recombinant form facilitates the development of therapeutic strategies aimed at modulating its activity in disease contexts. Characterizing this protein could offer insights into its regulatory mechanisms and contribute to the broader understanding of the PP1 holoenzyme's role in health and disease. Moreover, investigating the potential of PPP1R3D as a biomarker or therapeutic target could open new avenues for innovative treatment modalities for conditions associated with altered phosphatase signaling pathways. Overall, the research surrounding PPP1R3D recombinant protein holds significant promise in advancing our knowledge of cellular regulation and its implications for future biomedicine.











