Analytical Data
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Gene name
RNF148
- Application
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Alternative Names
RNF148; RING finger protein 148
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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
Q8N7C7
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Expression Region
1-305 aa
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AA Sequence
MSFLRITPSTHSSVSSGLLRLSIFLLLSFPDSNGKAIWTAHLNITFQVGNEITSELGESGVFGNHSPLERVSGVVALPEGWNQNACHPLTNFSRPKQADSWLALIERGGCTFTHKINVAAEKGANGVIIYNYQGTGSKVFPMSHQGTENIVAVMISNLKGMEILHSIQKGVYVTVIIEVGRMHMQWVSHYIMYLFTFLAATIAYFYLDCVWRLTPRVPNSFTRRRSQIKTDVKKAIDQLQLRVLKEGDEELDLNEDNCVVCFDTYKPQDVVRILTCKHFFHKACIDPWLLAHRTCPMCKCDILKT
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Molecular Weight
60.8 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
RNF148 is an E3 ubiquitin ligase that plays a critical role in the regulation of protein degradation and signal transduction pathways, making it essential for various cellular processes, including DNA damage response, immune signaling, and cell proliferation. Recent studies have shown that RNF148 might be involved in modifying the stability of key proteins linked to cancer progression and other diseases. Its ability to regulate the ubiquitination process has drawn significant attention in the field of molecular biology and therapeutic research, as targeting RNF148 could provide novel strategies for cancer treatment and enhancement of immune responses. The characterization of recombinant RNF148 protein is crucial for understanding its ubiquitin ligase activity, substrate specificity, and structural properties. By producing this protein in a recombinant form, researchers aim to elucidate its functional mechanisms, interactions with various substrates, and its potential as a therapeutical target. This research is not only pivotal for uncovering the biological roles of RNF148 but also for developing drugs that could modulate its activity in pathological conditions. Therefore, the study of RNF148 recombinant protein is a promising avenue for advancing our knowledge of cellular regulation and for paving the way towards innovative treatment options in oncology and immunotherapy.











