Analytical Data
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Gene name
RNF175
- Application
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Alternative Names
RNF175; RING finger protein 175
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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
Q8N4F7
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Expression Region
1-328 aa
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AA Sequence
MAAGTAARKAAPVLEAPPQQEQLSHTKLSAEDTWNLQQERMYKMHRGHDSMHVEMILIFLCVLVIAQIVLVQWRQRHGRSYNLVTLLQMWVVPLYFTIKLYWWRFLSMWGMFSVITSYILFRATRKPLSGRTPRLVYKWFLLIYKLSYAFGVVGYLAIMFTMCGFNLFFKIKARDSMDFGIVSLFYGLYYGVMGRDFAEICSDYMASTIGFYSVSRLPTRSLSDNICAVCGQKIIVELDEEGLIENTYQLSCNHVFHEFCIRGWCIVGKKQTCPYCKEKVDLKRMISNPWERTHFLYGQILDWLRYLVAWQPVVIGIVQGINYSLGLE
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Molecular Weight
64.7 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
RNF175, also known as RING Finger Protein 175, is an E3 ubiquitin ligase that has garnered attention in recent years due to its potential roles in various cellular processes, including protein degradation, cell cycle regulation, and cellular response to stress. The study of RNF175 is critical as it is implicated in several diseases, including cancer, where dysregulation of ubiquitination pathways can lead to tumorigenesis. Research has shown that RNF175 interacts with various substrates, affecting their stability and localization within the cell. Its unique RING domain facilitates the transfer of ubiquitin moieties from E2 conjugating enzymes to target proteins, thereby marking them for proteasomal degradation or influencing their functional activity. Moreover, alterations in the expression levels or mutations in RNF175 have been associated with pathological conditions, emphasizing its potential as a therapeutic target. By producing recombinant RNF175 protein, scientists aim to elucidate its biological functions, understand its mechanisms of action, and explore its potential as a biomarker or therapeutic intervention in diseases characterized by aberrant protein homeostasis. Overall, the study of RNF175 not only enhances our understanding of the ubiquitin-proteasome system but also provides insights into the complex regulatory networks that govern cellular functions and their contributions to human health and disease.
