Analytical Data
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Gene name
RNF39
- Application
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Alternative Names
RNF39；HZFW；RING finger Protein 39
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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
Q9H2S5
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Expression Region
1-420aa
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AA Sequence
MWWRDLTRLR LWLKREAIPG EGRKAAKVNA GVGEKGIYTA SSRGGPPSAR SKAVTVVAEG AASRSWLSMD APELGPGLVE RLEQLATCPL CGGSFEDPVL LACEHSFCRA CLARRWGTPP ATGTEASPTA CPCCGLPCPR RSLRSNVRLA VEVRISRELR EKLAEPGARA GRRRGGRIPT MGCLDLPGED MRKTWRRFEV PTSKSSNSED DLPEDYPVVK KMLHRLTADL TLDPGTAHRR LLISADRRSV QLAPPGTPAP PDGPKRFDQL PAVLGAQGFG AGRHCWEVET ADAASCRDSS GEDADDEESH YAVGAAGESV QRKGCVRLCP AGAVWAVEGR GGRLWALTAP EPTLLGGVEP PPRRIRVDLD WERGRVAFYD GRSLDLLYAF QAPGPLGERI FPLFCTCDPR APLRIVPAES
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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
RNF39, also known as a RING finger protein, has garnered significant interest in the field of molecular biology due to its potential roles in various cellular processes, including protein ubiquitination, DNA damage response, and regulation of gene expression. The protein is characterized by the presence of a RING finger domain, which is integral to its function as an E3 ubiquitin ligase, catalyzing the transfer of ubiquitin moieties to target proteins and thereby marking them for proteasomal degradation. Recent studies have suggested that RNF39 may be involved in the development of several diseases, including cancer, by modulating critical pathways related to cell cycle regulation and apoptosis. Additionally, its intricate involvement in post-translational modifications underscores the necessity for a deeper understanding of its mechanism of action. By generating recombinant RNF39 protein, researchers aim to elucidate its structure-function relationship and pave the way for potential therapeutic interventions that could disrupt its pathological roles in disease. Furthermore, exploring the interactions between RNF39 and its substrates could provide insights into novel regulatory networks, enhancing the understanding of cellular homeostasis and the implications of dysregulated ubiquitination in human health.
