Description
Cdc37 was initially identified as a cell division cycle control protein of Saccharomyces cerevisiae (1) and was later found to have a much broader role as a molecular chaperone required for folding of protein kinases (2). It forms a complex with Hsp90 and a variety of protein kinases and is thought to play a critical role in directing Hsp90 to its target kinases (3). Cdc37 has a molecular weight of 58.4 kD.
Applications
Western blot (2,000 fold dilution)
Immunoprecipitation
Indirect immuno-staining
Not tested for other applications.
Specification
Product: Rabbit polyclonal antibody
Immunogen: Recombinant yeast Cdc37 expressed in E. coli
Form: Antiserum with 0.09% sodium azide
Reactivity: S. cerevisiae Cdc37, not tested with other species
Storage: -20°C. For long term storage, -70°C
Data Link
SGD CDC37/YDR168W
References
Reed SI “The selection of S. cerevisiae mutants defective in the start event of cell division” Genetics 95: 561-577 (1980) PMID: 7002718
Kimura Y et al “Cdc37 is a molecular chaperone with specific functions in signal transduction” Genes Dev 11: 1775-1785 (1997) PMID: 9242486
Stepanova L et al “Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4” Genes Dev 10: 1491-1502 (1996) PMID: 8666233
Fig. 1 Detection of Cdc37 protein in the crude extract of S. cerevisiae by Western blot using this antibody. Lane 1: x 1000 dilution; Lane 2: x 5000 dilution; Cdc37 protein has a molecular weight of 58.4 kD, but appeared as a 68 kD band in SDS-PAGE.
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