Immunofluorescence analysis of Hsp90 beta was done on 70% confluent log phase HeLa cells. The cells were fixed with 4% paraformaldehyde for 10 minutes, permeabilized with 0.1% Triton™ X-100 for 10 minutes, and blocked with 1% BSA for 1 hour at room temperature. The cells were labeled with Hsp90 beta (H9010) Mouse Monoclonal Antibody (Product # 37-9400) at 1:250 dilution in 0.1% BSA and incubated for 3 hours at room temperature and then labeled with Goat anti-Mouse IgG (H+L) Superclonal™ Secondary Antibody, Alexa Fluor® 488 conjugate (Product # A28175) at a dilution of 1:2000 for 45 minutes at room temperature (Panel a: green). Nuclei (Panel b: blue) were stained with SlowFade® Gold Antifade Mountant with DAPI (Product # S36938). F-actin (Panel c: red) was stained with Rhodamine Phalloidin (Product # R415, 1:300). Panel d is a merged image showing cytoplasmic localization. Panel e is a no primary antibody control. The images were captured at 60X magnification.
|Tested species reactivity||Chicken, Human, Mouse, Rabbit|
|Published species reactivity||Human, Mouse, Not Applicable|
|Host / Isotype||Mouse / IgG2a, kappa|
|Immunogen||Recombinant human HSP90-beta|
|Storage buffer||tissue culture supernatant|
|Contains||0.1% sodium azide|
|Tested Applications||Dilution *|
|ELISA (ELISA)||Assay Dependent|
|Flow Cytometry (Flow)||1:20|
|Immunohistochemistry (Paraffin) (IHC (P))||1:20|
|Immunoprecipitation (IP)||Assay Dependent|
|Western Blot (WB)||Assay Dependent|
* 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.
HSP90 proteins are highly conserved molecular chaperones that have key roles in signal transduction, protein folding, protein degradation, and morphologic evolution. HSP90 proteins normally associate with other cochaperones and play important roles in folding newly synthesized proteins or stabilizing and refolding denatured proteins after stress. There are 2 major cytosolic HSP90 proteins, HSP90AA1, an inducible form, and HSP90AB1, a constitutive form. Other HSP90 proteins are found in endoplasmic reticulum (HSP90B1; MIM 191175) and mitochondria (TRAP1; MIM 606219) (Chen et al., 2005).
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
PMCA2 regulates HER2 protein kinase localization and signaling and promotes HER2-mediated breast cancer.
37-9400 was used in immunocytochemistry and western blot to study the interactions between PMCA2 and HER2 in breast cancer cells
|Jeong J,VanHouten JN,Dann P,Kim W,Sullivan C,Yu H,Liotta L,Espina V,Stern DF,Friedman PA,Wysolmerski JJ||Proceedings of the National Academy of Sciences of the United States of America (113:E282)||2016|
The Inhibition of Heat Shock Protein 90 Facilitates the Degradation of Poly-Alanine Expanded Poly (A) Binding Protein Nuclear 1 via the Carboxyl Terminus of Heat Shock Protein 70-Interacting Protein.
37-9400 was used in immunocytochemistry and western blot to discuss factors that contribute to the onset and progression of oculopharyngeal muscular dystrophy.
|Shi C,Huang X,Zhang B,Zhu D,Luo H,Lu Q,Xiong WC,Mei L,Luo S||PloS one (10:null)||2015|
A C-terminal HSP90 inhibitor restores glucocorticoid sensitivity and relieves a mouse allograft model of Cushing disease.
37-9400 was used in western blot to investigate how HSP90 affects the glucocorticoid receptor in corticotroph cells.
|Riebold M,Kozany C,Freiburger L,Sattler M,Buchfelder M,Hausch F,Stalla GK,Paez-Pereda M||Nature medicine (21:276)||2015|
Heat shock protein 90ß stabilizes focal adhesion kinase and enhances cell migration and invasion in breast cancer cells.
37-9400 was used in immunocytochemistry and western blot to study the role of heat shock protein 90beta in cell migration and invasion of breast cancer cells
|Xiong X,Wang Y,Liu C,Lu Q,Liu T,Chen G,Rao H,Luo S||Experimental cell research (326:78)||2014|
|Human||Not Cited||Proteomic identification of putative biomarkers of radiotherapy resistance: a possible role for the 26S proteasome?||Smith L,Qutob O,Watson MB,Beavis AW,Potts D,Welham KJ,Garimella V,Lind MJ,Drew PJ,Cawkwell L||Neoplasia (New York, N.Y.) (11:1194)||2009|
|Mouse||Not Cited||HSP90 beta regulates rapsyn turnover and subsequent AChR cluster formation and maintenance.||Luo S,Zhang B,Dong XP,Tao Y,Ting A,Zhou Z,Meixiong J,Luo J,Chiu FC,Xiong WC,Mei L||Neuron (60:97)||2008|
||HSP90 beta regulates rapsyn turnover and subsequent AChR cluster formation and maintenance.||Luo S,Zhang B,Dong XP,Tao Y,Ting A,Zhou Z,Meixiong J,Luo J,Chiu FC,Xiong WC,Mei L||Neuron (60:97)||2008|
Pseudovacuoles--immobilized by high-pressure freezing--are associated with blebbing in walker carcinosarcoma cells.
37-9400 was used in immunocytochemistry to characterize the large inclusions present in front of locomoting Walker carcinosarcoma cells
|Vanhecke D,Bellmann R,Baum O,Graber W,Eggli P,Keller H,Studer D||Journal of microscopy (230:253)||2008|