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Western blot analysis of Hsp90 on a HeLa cell lysate (Human cervical epitheloid carcinoma; ATCC CCL-2.2). Lane 1: 1:1000, lane 2: 1:2000, lane 3: 1:4000 dilution of the mouse anti-Hsp90 antibody.
Immunofluorescence staining of WI-38 cells (Human lung fibroblasts; ATCC CCL-75).
BD Transduction Laboratories™ Purified Mouse Anti-Hsp90
BD Transduction Laboratories™ Purified Mouse Anti-Hsp90
Regulatory Status Legend
Any use of products other than the permitted use without the express written authorization of Becton, Dickinson and Company is strictly prohibited.
Preparation And Storage
Recommended Assay Procedures
Western blot: Please refer to http://www.bdbiosciences.com/pharmingen/protocols/Western_Blotting.shtml
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
- Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
- Source of all serum proteins is from USDA inspected abattoirs located in the United States.
Companion Products
The 90 kDa heat shock protein (Hsp90), a highly conserved stress-induced protein, is abundantly expressed in most tissues under nonstress conditions and is required for eukaryotic cell viability. Hsp90 interacts with a number of signaling molecules, other heat shock proteins, and cytoskeletal proteins. However, the function of Hsp90 in these complexes remains unclear. It is thought that Hsp90 plays a common role in a number of diverse signaling systems due to its physical association with v-Src family tyrosine kinases, steroid hormone receptors, the Raf serine/threonine kinase, the basic-helix-loop-helix dioxin receptor, and the βγ subunits of G proteins.
Development References (5)
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Brouet A, Sonveaux P, Dessy C, Balligand JL, Feron O. Hsp90 ensures the transition from the early Ca2+-dependent to the late phosphorylation-dependent activation of the endothelial nitric-oxide synthase in vascular endothelial growth factor-exposed endothelial cells. J Biol Chem. 2001; 276(35):32663-32669. (Biology: Immunoprecipitation, Western blot). View Reference
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Miyamoto A, Nakayama K, Imaki H. Increased proliferation of B cells and auto-immunity in mice lacking protein kinase Cdelta. Nature. 2002; 416(6883):865-869. (Biology: Western blot). View Reference
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Murata T, Sato K, Hori M, Ozaki H, Karaki H. Decreased endothelial nitric-oxide synthase (eNOS) activity resulting from abnormal interaction between eNOS and its regulatory proteins in hypoxia-induced pulmonary hypertension. J Biol Chem. 2002; 277(46):44085-44092. (Biology: Western blot). View Reference
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Pritchard KA Jr, Ackerman AW. Heat shock protein 90 mediates the balance of nitric oxide and superoxide anion from endothelial nitric-oxide synthase. J Biol Chem. 2001; 276(21):17621-17624. (Biology: Western blot). View Reference
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Rebbe NF, Ware J, Bertina RM, Modrich P, Stafford DW. Nucleotide sequence of a cDNA for a member of the human 90-kDa heat-shock protein family. Gene. 1987; 53(2-3):235-245. (Biology). View Reference
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