Analytical Data
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Gene name
RNF36
- Application
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Alternative Names
E3 ubiquitin-protein ligase TRIM69. EC:2.3.2.27. RFP-like domain-containing protein trimless. RING finger protein 36. RING-type E3 ubiquitin transferase TRIM69. Tripartite motif-containing protein 69
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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
Q86WT6
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Expression Region
1-341 aa
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AA Sequence
MEEELAIQQGQLETTLKELQTLRNMQKEAIAAHKENKLHLQQHVSMEFLKLHQFLHSKEKDILTELREEGKALNEEMELNLSQLQEQCLLAKDMLVSIQAKTEQQNSFDFLKDITTLLHSLEQGMKVLATRELISRKLNLGQYKGPIQYMVWREMQDTLCPGLSPLTLDPKTAHPNLVLSKSQTSVWHGDIKKIMPDDPERFDSSVAVLGSRGFTSGKWYWEVEVAKKTKWTVGVVRESIIRKGSCPLTPEQGFWLLRLRNQTDLKALDLPSFSLTLTNNLDKVGIYLDYEGGQLSFYNAKTMTHIYTFSNTFMEKLYPYFCPCLNDGGENKEPLHILHPQ
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Molecular Weight
65.7 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
The RNF36 protein, a member of the RING-type E3 ubiquitin ligase family, has garnered significant interest in recent years due to its potential implications in various biological processes and diseases. Ubiquitination, the process mediated by RING E3 ligases, plays a critical role in regulating protein stability, signaling pathways, and cellular responses to stress by marking proteins for degradation by the proteasome. Studies have suggested that RNF36 may be involved in cellular processes such as cell cycle regulation, DNA damage response, and apoptosis, indicating its importance in maintaining cellular homeostasis. Furthermore, aberrations in the function of RNF36 have been linked to several pathologies, including cancer and neurodegenerative diseases, highlighting its role as a potential therapeutic target. The recombinant production of RNF36 allows for a comprehensive analysis of its structure, function, and mechanisms of action, enabling researchers to unravel its biological significance and explore its potential as a biomarker or target for drug development. Understanding the intricate workings of RNF36 could pave the way for novel therapeutic strategies aimed at modulating its activities in disease contexts. Overall, the study of RNF36 recombinant protein is crucial for advancing our knowledge of ubiquitin-mediated regulation and its implications in health and disease.
