Analytical Data
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Gene name
CDC37
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简介
The CDC37 protein is a co-chaperone that binds multiple kinases and promotes their interaction with the Hsp90 complex, resulting in stability and enhanced activity. CDC37 Protein, Human (sf9, GST) is the recombinant human-derived CDC37 protein, expressed by Sf9 insect cells , with C-GST labeled tag.
- Application
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Alternative Names
Hsp90 co-chaperone Cdc37; CDC37; CDC37A
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Species
Human
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Source
Baculovirus
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Tag
C-GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q16543
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Expression Region
M1-V378
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Protein Length
Full Length
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Molecular Weight
70.7 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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
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Protein Description
CDC37 (Cell Division Cycle 37) is a crucial co-chaperone that plays a significant role in the proper folding and activation of various protein kinases and other client proteins, contributing to the regulation of cell cycle progression. Research has shown that CDC37 interacts with heat shock protein 90 (Hsp90), forming a complex that aids in the stabilization and maturation of client proteins, which are often implicated in cancer signaling pathways. Given its vital role in cellular processes and its association with several malignancies, CDC37 has garnered considerable attention as a potential therapeutic target. Studies have investigated the structural characteristics of CDC37, revealing insights into its domain organization and interaction mechanisms. The generation of recombinant CDC37 protein in laboratory settings has facilitated in-depth biochemical analyses, enabling researchers to explore its function, binding affinity, and the consequences of its dysregulation in oncogenesis. Furthermore, understanding CDC37’s role in the chaperone network provides valuable information for the development of inhibitors that could disrupt its interaction with Hsp90, potentially leading to novel cancer treatment strategies. Thus, the study of CDC37 recombine proteins is crucial for advancing our knowledge of cellular dynamics and identifying new therapeutic avenues for cancer and other diseases linked to protein misfolding and misfolded protein stress responses.
