Analytical Data
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Gene name
RNF4
- Application
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Alternative Names
RNF4;SNURF;E3 ubiquitin-Protein ligase RNF4
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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
P78317
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Expression Region
1-190aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSTRKRR GGAINSRQAQ KRTREATSTP EISLEAEPIE LVETAGDEIV DLTCESLEPV VVDLTHNDSV VIVDERRRPR RNARRLPQDH ADSCVVSSDD EELSRDRDVY VTTHTPRNAR DEGATGLRPS GTVSCPICMD GYSEIVQNGR LIVSTECGHV FCSQCLRDSL KNANTCPTCR KKINHKRYHP IYI
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Molecular Weight
24 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
RNF4 is a member of the RING finger E3 ubiquitin ligase family, playing a critical role in ubiquitin-mediated proteolysis and cellular signaling. Its primary function is to catalyze the ubiquitination of specific target proteins, regulating various cellular processes including protein degradation, DNA repair, and cell cycle progression. Research has indicated that RNF4 is involved in the cellular response to stress and is required for the proper functioning of the p53 tumor suppressor pathway. Additionally, RNF4 has been implicated in various diseases, particularly in cancer, where dysregulation of ubiquitin-mediated processes can lead to tumorigenesis. The exploration of recombinant RNF4 proteins has become essential to understand its mechanisms of action, potential interactions with other proteins, and its role in pathological conditions. Scientists are utilizing recombinant techniques to produce RNF4 for biochemical assays, structural studies, and to investigate its interaction networks, aiming to elucidate its biological significance and therapeutic potential. This research is paving the way for further studies on RNF4 as a promising target for drug development, particularly in cancer therapeutics, where modulation of the ubiquitin-proteasome system can be advantageous. Understanding the structure and function of RNF4 at a molecular level will contribute to the broader knowledge of ubiquitin biology and its implications in health and disease.
