Analytical Data
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Gene name
PPP2R3C
- Application
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Alternative Names
Protein phosphatase subunit G5PR;Rhabdomyosarcoma antigen MU-RMS-40.6A/6C
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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
Q969Q6
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Expression Region
1-453 aa
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AA Sequence
MDWKEVLRRRLATPNTCPNKKKSEQELKDEEMDLFTKYYSEWKGGRKNTNEFYKTIPRFYYRLPAEDEVLLQKLREESRAVFLQRKSRELLDNEELQNLWFLLDKHQTPPMIGEEAMINYENFLKVGEKAGAKCKQFFTAKVFAKLLHTDSYGRISIMQFFNYVMRKVWLHQTRIGLSLYDVAGQGYLRESDLENYILELIPTLPQLDGLEKSFYSFYVCTAVRKFFFFLDPLRTGKIKIQDILACSFLDDLLELRDEELSKESQETNWFSAPSALRVYGQYLNLDKDHNGMLSKEELSRYGTATMTNVFLDRVFQECLTYDGEMDYKTYLDFVLALENRKEPAALQYIFKLLDIENKGYLNVFSLNYFFRAIQELMKIHGQDPVSFQDVKDEIFDMVKPKDPLKISLQDLINSNQGDTVTTILIDLNGFWTYENREALVANDSENSADLDDT
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Molecular Weight
60.2 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
PPP2R3C, a regulatory subunit of protein phosphatase 2A (PP2A), plays a crucial role in various cellular processes, including cell growth, division, and apoptosis. Research has shown that PP2A, comprising a core enzyme and regulatory subunits, is pivotal in controlling the phosphorylation state of numerous proteins, thereby influencing signaling pathways related to cancer, neurodegenerative diseases, and metabolic disorders. The PPP2R3C subunit is particularly interesting due to its potential impact on PP2A's specificity and activity, especially under pathological conditions. Recent studies have identified alterations in the expression and function of PPP2R3C in various cancer types, suggesting its involvement in tumorigenesis and as a potential biomarker or therapeutic target. Furthermore, understanding the molecular mechanisms by which PPP2R3C modulates PP2A activity can provide insights into the development of drugs that can re-establish normal phosphatase function in disease contexts. As such, the study of PPP2R3C recombinant proteins has become a focal point for elucidating the complex regulatory networks governed by PP2A, with implications for developing new strategies in cancer therapy and other diseases characterized by dysregulated phosphorylation.
