Analytical Data
-
Gene name
CDC37
-
简介
The CDC37 protein is a co-chaperone that binds to kinases and promotes their interaction with Hsp90 complexes, thereby stabilizing and activating them. It inhibits the ATPase activity of HSP90AA1. CDC37 Protein, Mouse (sf9) is the recombinant mouse-derived CDC37 protein, expressed by Sf9 insect cells, with tag free.
- Application
-
Alternative Names
Hsp90 co-chaperone Cdc37; CDC37; CDC37A
-
Species
Mouse
-
Source
Baculovirus
-
Tag
Tag Free
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q61081
-
Expression Region
Q61081 (N-G&P, M1-A379)
-
Protein Length
Full Length
-
Molecular Weight
46 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
CDC37 is a highly conserved co-chaperone that plays a crucial role in the maturation and stabilization of protein kinases, which are essential for various cellular signaling pathways. As a key component of the heat shock protein 90 (Hsp90) complex, CDC37 facilitates the proper folding and activation of oncogenic kinases, making it an attractive target for cancer research. The dysregulation of protein kinases is often implicated in various cancers, leading to uncontrolled cell growth and proliferation. Recent studies have demonstrated that CDC37 not only assists in the stability and activity of these kinases but also interacts with numerous other proteins involved in cell cycle regulation and stress response. Given its pivotal role in cancer cell biology, targeting CDC37 through the development of specific inhibitors could provide a novel therapeutic strategy to combat cancer. Moreover, the recombinant expression of CDC37 allows for detailed functional studies and the investigation of its interactions with client proteins, paving the way for a deeper understanding of its mechanism of action in both normal and cancerous cells. Understanding the structure and function of CDC37 can also inform the design of chaperone-based therapies, offering potential for improved treatment options in various malignancies. Thus, research on CDC37 recombinant protein not only enhances our fundamental knowledge of cellular mechanisms but also holds promise for its application in therapeutic development.
