Analytical Data
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Gene name
RBX1
- Application
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Alternative Names
RBX1;RNF75;ROC1;E3 ubiquitin-Protein ligase RBX1
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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
P62877
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Expression Region
1-108aa
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AA Sequence
MAAAMDVDTPSGTNSGAGKKRFEVKKWNAVALWAWDIVVDNCAICRNHIMDLCIECQANQASATSEECTVAWGVCNHAFHFHCISRWLKTRQVCPLDNREWEFQKYGH
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Molecular Weight
43.8 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
RBX1, or Ring Box 1, is an E3 ubiquitin ligase that plays a crucial role in the ubiquitin-proteasome system, which regulates protein degradation and maintains cellular homeostasis. It facilitates the transfer of ubiquitin moieties to target proteins, marking them for degradation, thus influencing various cellular processes including cell cycle progression, DNA repair, and response to stress. Abnormalities in RBX1 expression and function have been implicated in several diseases, including cancer, where it can contribute to tumor progression by altering the degradation of oncogenic and tumor suppressor proteins. Research on RBX1 recombinant protein focuses on understanding its structure-function relationship and the molecular mechanisms underlying its role in ubiquitination. This knowledge is essential for the development of therapeutic interventions that could target aberrant RBX1 activity in disease contexts. Additionally, studying RBX1 in vitro through recombinant protein expression allows for the exploration of its interactions with specific substrates and regulators, providing insights into ubiquitin-mediated signaling pathways. Overall, RBX1 remains a promising target for further research in both basic biology and potential clinical applications.











