Analytical Data
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Gene name
RNF122
- Application
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Alternative Names
RNF122; RING finger protein 122
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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
Q9H9V4
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Expression Region
1-155 aa
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AA Sequence
MHPFQWCNGCFCGLGLVSTNKSCSMPPISFQDLPLNIYMVIFGTGIFVFMLSLIFCCYFISKLRNQAQSERYGYKEVVLKGDAKKLQLYGQTCAVCLEDFKGKDELGVLPCQHAFHRKCLVKWLEVRCVCPMCNKPIASPSEATQNIGILLDELV
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Molecular Weight
43.9 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
RNF122, a member of the RING finger protein family, has garnered significant attention in recent years due to its pivotal role in various cellular processes, including protein ubiquitination and regulation of immune responses. It is characterized by its RING finger domain, which is essential for its E3 ubiquitin ligase activity, enabling it to mediate the transfer of ubiquitin moieties to target proteins, thus influencing their stability and function. Dysregulation of RNF122 has been implicated in various diseases, particularly cancer, where it may contribute to tumorigenesis through the modulation of oncogenic and tumor suppressor pathways. Recent studies have shown that RNF122 can interact with key signaling molecules involved in immune response, suggesting its potential involvement in the modulation of inflammation and autoimmunity. As research progresses, the synthesis and functional characterization of recombinant RNF122 protein are crucial for elucidating its molecular mechanisms and interactions, paving the way for therapeutic strategies targeting RNF122-related pathways. Understanding the precise function and regulation of RNF122 could provide insights into its role in health and disease, highlighting its potential as a biomarker or therapeutic target in oncology and immunological disorders.
