Analytical Data
-
Gene name
RNF1
- Application
-
Alternative Names
RING1; Polycomb complex protein RING1; Really interesting new gene 1 protein
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q06587
-
Expression Region
Met1~Lys406
-
Molecular Weight
43kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
RNF1, or RING finger protein 1, is a member of the RING-finger E3 ubiquitin ligase family, which plays a crucial role in regulating various cellular processes, including protein degradation, signal transduction, and cell cycle progression through the ubiquitin-proteasome pathway. Research on RNF1 has gained prominence due to its implications in multiple biological functions and disease mechanisms, particularly in cancer and neurodegenerative disorders. RNF1 is known to ubiquitinate key substrates involved in tumor suppression and cell survival, thereby influencing oncogenic signaling pathways. Given its significant involvement in cellular homeostasis, understanding the structure and function of RNF1 at a molecular level can provide insights into its potential as a therapeutic target. Recent studies have focused on the recombinant expression of RNF1 to elucidate its enzymatic activity and substrate specificity, enabling the development of inhibitors that can modulate its function in pathological contexts. Additionally, investigating the interactions of RNF1 with other cellular proteins contributes to a broader understanding of its role in the ubiquitin-proteasome system and its impact on cellular health. The exploration of RNF1 recombinant proteins promises to advance our knowledge in both fundamental biology and the development of innovative therapeutic strategies.
