Analytical Data
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Gene name
RNF13
- Application
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Alternative Names
RNF13；RZF；E3 ubiquitin-Protein ligase RNF13
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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
O43567
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Expression Region
1-381aa
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AA Sequence
MLLSIGMLMLSATQVYTILTVQLFAFLNLLPVEADILAYNFENASQTFDDLPARFGYRLPAEGLKGFLINSKPENACEPIVPPPVKDNSSGTFIVLIRRLDCNFDIKVLNAQRAGYKAAIVHNVDSDDLISMGSNDIEVLKKIDIPSVFIGESSANSLKDEFTYEKGGHLILVPEFSLPLEYYLIPFLIIVGICLILIVIFMITKFVQDRHRARRNRLRKDQLKKLPVHKFKKGDEYDVCAICLDEYEDGDKLRILPCSHAYHCKCVDPWLTKTKKTCPVCKQKVVPSQGDSDSDTDSSQEENEVTEHTPLLRPLASVSAQSFGALSESRSHQNMTESSDYEEDDNEDTDSSDAENEINEHDVVVQLQPNGERDYNIANTV
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Molecular Weight
42.8 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
RNF13, also known as RING finger protein 13, is a member of the RING-type E3 ubiquitin ligase family, which plays a crucial role in post-translational modifications through ubiquitination, a process that regulates protein stability, localization, and activity. The significance of RNF13 in cellular processes, such as cell proliferation, DNA repair, and apoptosis, makes it a subject of interest in cancer research and other diseases characterized by dysregulated ubiquitin-proteasome systems. Previous studies have indicated that alterations in RNF13 expression levels may correlate with tumorigenesis and progression in various cancers, suggesting its potential as a biomarker or therapeutic target. Additionally, RNF13 has been implicated in the immune response, further highlighting its multifaceted roles in health and disease. Understanding the functional mechanisms of RNF13, particularly through the study of its recombinant protein, can provide insights into its regulatory roles at the molecular level. This research paves the way for elucidating the pathways in which RNF13 is involved, ultimately contributing to the development of novel therapeutic strategies that could exploit its function in disease modulation. As such, the study of RNF13 recombinant protein holds promise for uncovering new dimensions of E3 ligase biology and its applications in targeted therapies.
