Analytical Data
-
Gene name
CDC48
- Application
-
Alternative Names
Valosin-containing protein homolog Short name: VCP
-
Species
Glycine max
-
Source
E. coli
-
Tag
N- His-SUMO
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P54774
-
Expression Region
653-807aa
-
Molecular Weight
33.5 kDa
-
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
CDC48, also known as VCP (valosin-containing protein), is an essential member of the AAA+ ATPase family and plays a crucial role in various cellular processes, including protein degradation, membrane fusion, and cell cycle regulation. A growing body of research has highlighted its involvement in the ubiquitin-proteasome system, where it mediates the extraction of ubiquitinated substrates from protein complexes, facilitating their subsequent degradation. Dysregulation of CDC48 has been implicated in several diseases, including cancer, neurodegenerative disorders, and protein aggregation diseases, thus making it a vital target for therapeutic intervention. Understanding the structural and mechanistic nuances of CDC48 is key to elucidating its role in these diseases. Recent studies have focused on the reconstitution of CDC48’s functional activities in vitro, which has allowed for greater insights into its ATPase activity and substrate interactions. By employing various biochemical and biophysical techniques, researchers aim to dissect the protein's conformational changes during activation and substrate processing. Furthermore, exploring CDC48's interaction partners provides a broader understanding of its cellular network. Given its pivotal role in maintaining proteostasis and cellular homeostasis, elucidating the precise mechanisms by which CDC48 operates is essential for developing targeted therapies that could ameliorate the pathological consequences of its dysfunction. Overall, the study of CDC48 is crucial not only for basic biological understanding but also for uncovering novel therapeutic avenues for diseases associated with its malfunction.
