Analytical Data
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Gene name
RNF215
- Application
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Alternative Names
RNF215; RING finger protein 215
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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
Q9Y6U7
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Expression Region
1-377 aa
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AA Sequence
MGPAARPALRSPPPPPPPPPSPLLLLLPLLPLWLGLAGPGAAADGSEPAAGAGRGGARAVRVDVRLPRQDALVLEGVRIGSEADPAPLLGGRLLLMDIVDAEQEAPVEGWIAVAYVGKEQAAQFHQENKGSGPQAYPKALVQQMRRALFLGASALLLLILNHNVVRELDISQLLLRPVIVLHYSSNVTKLLDALLQRTQATAEITSGESLSANIEWKLTLWTTCGLSKDGYGGWQDLVCLGGSRAQEQKPLQQLWNAILLVAMLLCTGLVVQAQRQASRQSQRELGGQVDLFKRRVVRRLASLKTRRCRLSRAAQGLPDPGAETCAVCLDYFCNKQWLRVLPCKHEFHRDCVDPWLMLQQTCPLCKFNVLGNRYSDD
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Molecular Weight
68.42 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
RNF215, a member of the RING finger protein family, is increasingly recognized for its significant role in various biological processes, including cell cycle regulation, DNA damage response, and tumorigenesis. This E3 ubiquitin ligase is involved in the modification of target proteins through ubiquitination, thereby influencing their stability and function. Recent studies have highlighted RNF215's potential involvement in cancer progression, as it has been shown to regulate the activity of key oncogenic pathways and interact with several tumor suppressors. Given the critical role of ubiquitination in cellular homeostasis and signal transduction, understanding the structure-function relationship of RNF215 and its interaction networks is crucial. Research into RNF215 recombinant protein offers insights into its mechanism of action, allowing for the potential development of therapeutic strategies targeting its pathways. Furthermore, elucidating the role of RNF215 in disease contexts may provide biomarkers for cancer prognosis and therapeutic response. As such, studying RNF215 not only enhances our fundamental understanding of cellular regulation but also paves the way for novel approaches in cancer treatment and biomarker discovery.
