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Recombinant Mouse Hsp90 co-chaperone Cdc37 (Cdc37)

Recombinant Mouse Hsp90 co-chaperone Cdc37 (Cdc37)

Code
MSDS	MSDS Datasheet
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Source
Conjugate
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Product Details
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Target Background

Product Details

Abbreviation

Cdc37

Purity

>85% (SDS-PAGE)

Target Names

Cdc37

Uniprot NO.

Q61081

Alternative Names

Cdc37Hsp90 co-chaperone Cdc37; Hsp90 chaperone protein kinase-targeting subunit; p50Cdc37) [Cleaved into: Hsp90 co-chaperone Cdc37; N-terminally processed]

Species

Mus musculus (Mouse)

Source

Yeast

Expression Region

1-379

Target Protein Sequence

MVDYSVWDHI EVSDDEDETH PNIDTASLFR WRHQARVERM EQFQKEKEEL DRGCRECKRK VAECQRKLKE LEVAESDGQV ELERLRAEAQ QLRKEERSWE QKLEDMRKKE KNMPWNVDTL SKDGFSKSMV NTKPEKAEED SEEAREQKHK TFVEKYEKQI KHFGMLHRWD DSQKYLSDNV HLVCEETANY LVIWCIDLEV EEKCALMEQV AHQTMVMQFI LELAKSLKVD PRACFRQFFT KIKTADHQYM EGFKYELEAF KERVRGRAKL RIEKAMKEYE EEERKKRLGP GGLDPVEVYE SLPEELQKCF DVKDVQMLQD AISKMDPTDA KYHMQRCIDS GLWVPNSKSG EAKEGEEAGP GDPLLEAVPK AGNEKDVSA
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Protein Length

full length protein

Tag Info

N-terminal His-tagged/Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Storage Condition

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Shelf Life

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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Target Background

Function(From Uniprot)

Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity. Inhibits HSP90AA1 ATPase activity.

Gene References into Functions

Results showed that Cdc37 acts as a bridge to direct Hsp90 to the transcription factor viral P proteins of all lyssaviruses. Although Cdc37 can load P proteins onto Hsp90, with or without binding to Hsp90, the interaction between Cdc37 and Hsp90 appears to provide additional allosterical regulation of its chaperone activity. Notably, both phosphorylated and non-P Cdc37 could facilitate Hsp90-mediated protein maturation. PMID:27251758
Niclosamide ethanolamine disrupted the interaction between cell division cycle 37 and heat shock protein 90 in hepatocellular carcinoma, reducing tumor growth. PMID:28284560
A series of tyrosine phosphorylation events, involving both p50(Cdc37) and Hsp90, are minimally sufficient to provide directionality to the chaperone cycle. PMID:22727666
Hsp90-Cdc37 complex acta as an endogenous regulator of noncanonical p38alpha activity. PMID:20299663
CDC37 binds to Akt and HSP90 in the signal transduction pathway in human tumor cells PMID:12176997
The interaction between mouse Pem and Cdc37 homolog was then confirmed by glutathione S-transferase pull-down assay, and the possible interaction model was suggested. PMID:16270159
JAK1/2 are client proteins of Hsp90 alpha and beta; Hsp90 and CDC37 play a critical role in types I and II interferon pathways PMID:16280321
This growth inhibition is partially rescued by expression of ectopic Gli1, suggesting that Fu may contribute to enhance Hh signaling activity in cancer cells. PMID:17054904