Analytical Data
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Gene name
CDC37
- Application
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Alternative Names
CDC37；CDC37A；Hsp90 co-chaperone Cdc37
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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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
1-378aa
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AA Sequence
MGHHHHHHMVDYSVWDHIEVSDDEDETHPNIDTASLFRWRHQARVERMEQ FQKEKEELDRGCRECKRKVAECQRKLKELEVAEGGKAELERLQAEAQQLR KEERSWEQKLEEMRKKEKSMPWNVDTLSKDGFSKSMVNTKPEKTEEDSEE VREQKHKTFVEKYEKQIKHFGMLRRWDDSQKYLSDNVHLVCEETANYLVI WCIDLEVEEKCALMEQVAHQTIVMQFILELAKSLKVDPRACFRQFFTKIK TADRQYMEGFNDELEAFKERVRGRAKLRIEKAMKEYEEEERKKRLGPGGL DPVEVYESLPEELQKCFDVKDVQMLQDAISKMDPTDAKYHMQRCIDSGLW VPNSKASEAKEGEEAGPGDPLLEAVPKTGDEKDVSV
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Molecular Weight
45 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
Related Products
Protein Description
CDC37, or Cell Division Cycle 37, is a crucial co-chaperone protein that plays a significant role in the maturation and stabilization of various client proteins, particularly those involved in cell cycle regulation and signal transduction pathways. It is known to interact with HSP90 (Heat Shock Protein 90) to facilitate the proper folding and activation of protein kinases and other signaling molecules. Research into CDC37 has gained momentum due to its implications in various diseases, including cancer, where abnormal expression or dysfunction of CDC37 can lead to unchecked cell proliferation and tumorigenesis. Studies have highlighted CDC37's involvement in processes such as phosphorylation and chaperone-assisted protein folding, making it a potential therapeutic target. The characterization of CDC37 through recombinant protein techniques has enabled researchers to better understand its structure-function relationship and explore its interactions with client proteins. Additionally, investigations into its regulatory mechanisms and post-translational modifications could provide insights into how CDC37 contributes to cellular homeostasis and response to stress conditions. As such, the study of CDC37 recombinant proteins not only enhances our comprehension of fundamental cellular processes but also opens pathways for developing novel treatments for diseases linked to its dysregulation.
