Analytical Data
-
Gene name
CUL9
- Application
-
Alternative Names
PARC; H7AP1; P53-Associated Parkin-Like Cytoplasmic Protein; UbcH7-associated protein 1
-
Species
Human
-
Source
E. coli
-
Tag
N- His & GST
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q8IWT3
-
Expression Region
Ile1144~Ala1322
-
Molecular Weight
50kDa
-
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
CUL9 (Cullin 9) is a member of the cullin family of proteins, which play critical roles in ubiquitin-mediated proteasomal degradation, a key cellular mechanism for regulating protein levels and maintaining cellular homeostasis. The interest in CUL9 has surged in recent years due to its involvement in various biological processes and its potential implications in diseases, including cancer and neurodegenerative disorders. Unlike other cullins, CUL9 exhibits unique properties, such as its ability to function independently of certain cofactors and its engagement in alternative pathways that influence cell signaling and stress responses. Research has demonstrated that CUL9 can mediate the degradation of specific substrates, including tumor suppressors and proteins involved in DNA repair, thereby impacting cell cycle regulation and apoptosis. Moreover, its expression levels and activity have been found to be altered in various malignancies, suggesting a role in tumorigenesis. The study of CUL9 recombinant proteins aims to elucidate its precise mechanisms of action, interactions with other cellular components, and potential therapeutic targets. By producing and characterizing CUL9 in a recombinant form, researchers can investigate its structural properties, binding affinities, and functional roles in cellular pathways. Understanding CUL9's dynamics not only enhances our knowledge of cellular regulation but also opens avenues for developing novel strategies in treating diseases associated with its dysregulation. As research progresses, CUL9 is poised to be a significant focus in both basic science and clinical studies, fostering exploration into its dual roles as a regulator of cellular functions and a potential biomarker or therapeutic target in disease contexts.
