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|Tested species reactivity||Human, Mouse, Rat|
|Host / Isotype||Rabbit / IgG|
|Immunogen||A synthetic phosphopeptide derived from human CDC37 around the phosphorylation site of Ser13 (E-V-SP-D-D)|
|Purification||Antigen affinity chromatography|
|Storage buffer||Dulbecco's PBS, pH 7.4, with 150mM NaCl, 50% glycerol|
|Contains||0.02% sodium azide|
|Tested Applications||Dilution *|
|Immunohistochemistry (Paraffin) (IHC (P))||1:50-1:100|
|Western Blot (WB)||1:500-1:1000|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
In S. cerevisiae, Cdc37 has been shown to be an important regulator of cell division cycle through its action on cyclin-dependent kinases (CDK's). Cdc37 has also been associated with signaling pathways and kinases unrelated to cell cycle control, including v-Src, casein kinase II, MPS1 kinase and the sevenless receptor tyrosine kinase. Interestingly, HSP90 has also been shown to be associated with many of the same cellular targets as Cdc37. It has now been shown that Cdc37 is the same protein previously described as p50 which has been found to be associated with many of the same proteins as HSP90. Among others, Cdc37/p50 has been found complexed with Src-family kinases (Fyn, Yes, Fes, Lck & Fgr), Raf and pp60v-src. More recently, Cdc37 has been shown to be a chaperone independently and in concert with HSP90. In fact, Cdc37 is necessary for the binding of HSP90 to Cdk4.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
CDC37; CDC37 (cell division cycle 37 S. cerevisiae homolog); CDC37 (cell division cycle 37, S. cerevisiae, homolog); CDC37 cell division cycle 37 homolog; CDC37A; cell division cycle 37 homolog; hsp90 chaperone protein kinase-targeting subunit; hsp90 co-chaperone Cdc37; N-terminally processed; p50Cdc37
CDC37; CDC37A; p50; P50CDC37