Immunofluorescent analysis of Cdc37 in A431 cells. Cells were grown on chamber slides and fixed with formaldehyde prior to staining. Cells were probed without (control) or with a Cdc37 monoclonal antibody (Product # MA3-029) at a dilution of 1:200 overnight at 4 C, washed with PBS and incubated with a DyLight-488 conjugated secondary antibody (Product # 35503). Cdc37 staining (green), F-Actin staining with Phalloidin (red) and nuclei with DAPI (blue) is shown. Images were taken at 60X magnification.
|Tested species reactivity||Hamster, Human, Mouse, Rat|
|Published species reactivity||Rabbit, Yeast, Fruit fly, Mouse, Human|
|Host / Isotype||Mouse / IgG2b|
|Immunogen||Purified mouse Cdc37 fusion protein.|
|Contains||0.05% sodium azide|
|Storage Conditions||-20° C, Avoid Freeze/Thaw Cycles|
|Tested Applications||Dilution *|
|Flow Cytometry (Flow)||1:50|
|Immunohistochemistry (Paraffin) (IHC (P))||1:200|
|Immunoprecipitation (IP)||Assay dependent|
|Western Blot (WB)||1:5,000|
* 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.
MA3-029 detects Cdc37 from hamster, human, mouse and rat cells and tissues.
MA3-029 has been successfully used in Western blot, FACS, immunofluorescence, immunocytochemistry and immunoprecipitation (under denaturing conditions) procedures. By Western blot, this antibody recognizes a single 50 kDa protein representing Cdc37 in HeLa cell extract. Immunofluorescence staining of Cdc37 in Hepa1 cells with MA3-029 results in mostly cytoplasmic staining concentrated around the nuclear membrane. This antibody detects some weak non-specific bands in Jurkat, A431 and NIH-3T3 cell lysates.
The MA3-029 antigen is purified mouse Cdc37 fusion protein.
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 and 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.
PDLIM1 inhibits NF-?B-mediated inflammatory signaling by sequestering the p65 subunit of NF-?B in the cytoplasm.
MA3-029 was used in western blot to study how PDLIM1 suppresses NF-kappaB activation
|Ono R,Kaisho T,Tanaka T||Scientific reports (5:null)||2015|
Hsp90 cochaperones p23 and FKBP4 physically interact with hAgo2 and activate RNA interference-mediated silencing in mammalian cells.
MA3-029 was used in western blot to study the interaction of p23 and FKBP4 with hAgo2 and their roles in the mechanism of mammalian cell RNAi silencing
|Pare JM,LaPointe P,Hobman TC||Molecular biology of the cell (24:2303)||2013|
|Fruit fly||Not Cited||
Functioning of the Hsp90 machine in chaperoning checkpoint kinase I (Chk1) and the progesterone receptor (PR).
MA3-029 was used in western blot to investigate the role of Hsp90 in the funcation of checkpoint kinase I and progesterone receptor
|Felts SJ,Karnitz LM,Toft DO||Cell stress and chaperones (12:353)||2008|
Chaperoning checkpoint kinase 1 (Chk1), an Hsp90 client, with purified chaperones.
MA3-029 was used in western blot to investigate the relationship between chaperoning checkpoint kinase 1 and Hsp90.
|Arlander SJ,Felts SJ,Wagner JM,Stensgard B,Toft DO,Karnitz LM||The Journal of biological chemistry (281:2989)||2006|
Cdc37 is a molecular chaperone with specific functions in signal transduction.
MA3-029 was used in western blot to investigate the important roles of Cdc37 in signal transduction
|Kimura Y,Rutherford SL,Miyata Y,Yahara I,Freeman BC,Yue L,Morimoto RI,Lindquist S||Genes and development (11:1775)||1997|
p50(cdc37) is a nonexclusive Hsp90 cohort which participates intimately in Hsp90-mediated folding of immature kinase molecules.
MA3-029 was used in immunoprecipitation to investigate the role of p50(cdc37) in heat shock protein 90 molecular chaperone function
|Hartson SD,Irwin AD,Shao J,Scroggins BT,Volk L,Huang W,Matts RL||Biochemistry (39:7631)||2000|