Analytical Data
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Gene name
RNF144
- Application
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Alternative Names
E3 ubiquitin-protein ligase RNF144A. EC:2.3.2.31. RING finger protein 144A. UbcM4-interacting protein 4. Ubiquitin-conjugating enzyme 7-interacting protein 4
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P50876
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Expression Region
1-292 aa
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AA Sequence
MTTARYRPTWDLALDPLVSCKLCLGEYPVEQMTTIAQCQCIFCTLCLKQHVELLIKEGLETAISCPDAACPKQGHLQENEIECMVAAEIMQRYKKLQFEREVLFDPCRTWCPASTCQAVCQLRDVGLQTPQPVQCKACRMEFCSTCKASWHPGQGCPETMPITFLPGETSAAFKMEEDDAPIKRCPKCKVYIERDEGCAQMMCKNCKHAFCWYCPESLDDDFLLIHCDKGPCRNKLGHSRASVIWHRTQVVGIFAGFGLLLLVASPFLLLATPFVLCCKCKCSKGDDDPLPT
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Molecular Weight
57.86 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
Related Products
Protein Description
RNF144 is a member of the RING finger E3 ubiquitin ligase family, which plays a crucial role in regulating various biological processes through the ubiquitin-proteasome system. Research into RNF144 has gained momentum due to its involvement in cellular signaling pathways, and its potential implications in cancer development and progression. Dysregulation of the ubiquitin-proteasome system is often linked to tumorigenesis, making RNF144 a candidate for therapeutic interventions. Recent studies have demonstrated that RNF144 participates in the modulation of key oncogenic pathways, and its expression levels have been correlated with patient prognosis in several cancers. Furthermore, RNF144's unique structural features, including its RING domain, enable it to interact with specific substrates, influencing their stability and function. Understanding the mechanisms by which RNF144 exerts its effects on protein regulation and cellular homeostasis could provide insights into novel cancer treatment strategies and biomarkers for disease monitoring. As such, the study of recombinant RNF144 proteins is pivotal for elucidating its biological role, exploring its interactions with other proteins, and assessing its potential as a therapeutic target.
