Analytical Data
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Gene name
RNF113A
- Application
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Alternative Names
RNF113A; RNF113; ZNF183; E3 ubiquitin-protein ligase RNF113A; EC 2.3.2.27; Cwc24 homolog; RING finger protein 113A; Zinc finger protein 183
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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
O15541
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Expression Region
2-343 aa
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AA Sequence
AEQLSPGKA VDQVCTFLFK KPGRKGAAGR RKRPACDPEP GESGSSSDEG CTVVRPEKKR VTHNPMIQKT RDSGKQKAAY GDLSSEEEEE NEPESLGVVY KSTRSAKPVG PEDMGATAVY ELDTEKERDA QAIFERSQKI QEELRGKEDD KIYRGINNYQ KYMKPKDTSM GNASSGMVRK GPIRAPEHLR ATVRWDYQPD ICKDYKETGF CGFGDSCKFL HDRSDYKHGW QIERELDEGR YGVYEDENYE VGSDDEEIPF KCFICRQSFQ NPVVTKCRHY FCESCALQHF RTTPRCYVCD QQTNGVFNPA KELIAKLEKH RATGEGGASD LPEDPDEDAI PIT
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Molecular Weight
38.7 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
RNF113A, a member of the RING finger protein family, has garnered research interest due to its potential roles in cellular regulation and signaling pathways. Initially identified through genomic studies, this protein is believed to participate in important cellular processes such as ubiquitination, which is crucial for protein degradation, cell cycle regulation, and stress responses. Preliminary studies suggest that RNF113A may be involved in modulating immune responses and maintaining cellular homeostasis. Its structure, characterized by a RING finger domain responsible for E3 ubiquitin ligase activity, highlights its significance in post-translational modifications of target proteins. Given the pivotal role of ubiquitination in various diseases, including cancer and neurodegenerative disorders, understanding RNF113A's function could unveil new therapeutic targets. Moreover, insights into RNF113A’s interactions and mechanisms may contribute to the broader understanding of the ubiquitin-proteasome system. Investigating RNF113A as a recombinant protein enables researchers to explore its functional properties, interactome, and regulatory mechanisms, thereby providing a foundation for future studies aimed at elucidating its biological significance and potential applications in biomedicine.
