Analytical Data
-
Gene name
CUL1-RBX1
- Application
-
Alternative Names
Cullin-1; CUL1; Homo sapiens; Human; CUL-1
-
Species
Human
-
Source
Baculovirus
-
Tag
Tag Free
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q13616 (S2-A776)&P62877
-
Expression Region
Q13616 (S2-A776)&P62877 (M1-H108)
-
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
CUL1-RBX1 is a crucial component of the ubiquitin-proteasome system, playing a significant role in cellular protein degradation and regulation of various biological processes. CUL1 (Cullin-1) is a scaffold protein that forms a complex with RBX1 (Ring Box 1), which functions as a ubiquitin ligase. This complex facilitates the attachment of ubiquitin molecules to target proteins, signaling them for degradation by the proteasome. Dysregulation of the CUL1-RBX1 complex has been implicated in various diseases, including cancer, where abnormal protein degradation can lead to uncontrolled cell proliferation and tumor progression. Consequently, studying the CUL1-RBX1 complex is paramount for understanding its roles in cellular homeostasis and its potential as a therapeutic target. Researchers have been increasingly focused on the structural and functional aspects of this complex, employing techniques such as X-ray crystallography and cryo-electron microscopy to elucidate its mechanisms. A deeper understanding of CUL1-RBX1 could provide insights into novel drug developments aimed at modulating its activity, offering new avenues for treating diseases associated with protein homeostasis disruptions.
