Analytical Data
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Gene name
RNF152
- Application
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Alternative Names
RNF152; E3 ubiquitin-protein ligase RNF152; RING finger protein 152; RING-type E3 ubiquitin transferase RNF152
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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
Q8N8N0
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Expression Region
1-203 aa
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AA Sequence
METLSQDSLLECQICFNYYSPRRRPKLLDCKHTCCSVCLQQMRTSQKDVRCPWCRGVTKLPPGFSVSQLPDDPEVLAVIAIPHTSEHTPVFIKLPSNGCYMLPLPISKERALLPGDMGCRLLPGSQQKSVTVVTIPAEQQPLQGGAPQEAVEEEQDRRGVVKSSTWSGVCTVILVACVLVFLLGIVLHNMSCISKRFTVISCG
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Molecular Weight
48.8 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
Related Products
Protein Description
RNF152, a member of the RING finger protein family, has gained increasing attention in recent years due to its potential role in various biological processes and diseases. This E3 ubiquitin ligase is involved in regulating protein degradation, cellular signaling pathways, and immune responses, making it a critical player in maintaining cellular homeostasis. Research has suggested that RNF152 may be implicated in tumorigenesis and the progression of certain cancers, as its dysregulation can lead to aberrant protein accumulation and altered cellular functions. Furthermore, RNF152 is thought to participate in the modulation of inflammation and immune responses, with potential implications for autoimmune diseases. The expression and activity of RNF152 can be influenced by various stressors, highlighting its role as a regulator of cellular responses to environmental changes. Given its multifaceted functions, understanding the mechanisms underlying RNF152’s actions could provide valuable insights into therapeutic targets for treating diseases associated with its dysregulation. Consequently, studies focusing on the recombinant production of RNF152 are essential for elucidating its structure-function relationship, regulatory mechanisms, and potential applications in drug development and therapeutic interventions.
