Application

Anti-Nitrated Hsp90, clone 44.23, Cat. No. MABN788, is a highly specific mouse monoclonal antibody that targets nitrated HSP90 and has been tested in Dot Blot, ELISA, Immunohistochemistry (Paraffin), and Western Blotting.

Research CategoryNeuroscience

Western Blotting Analysis: A representative lot detected nitrated HSP90 in Western Blotting applications (Ye, Y., et. al. (2007). J Biol Chem. 282(9):6324-37).

ELISA Analysis: A representative lot detected nitrated HSP90 in ELISA applications (Ye, Y., et. al. (2007). J Biol Chem. 282(9):6324-37).

Dot Blot Analysis: A representative lot detected nitrated HSP90 in Dot Blot applications (Franco, M.C., et. al. (2013). Proc Natl Acad Sci U S A. 110(12):E1102-11).

Immunohistochemistry Analysis: A representative lot detected nitrated HSP90 in Immunohistochemistry applications (Franco, M.C., et. al. (2013). Proc Natl Acad Sci U S A. 110(12):E1102-11).

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

General description

Heat shock protein HSP 90-beta (UniProt: P34058; also known as Heat shock 84 kDa, HSP 84, HSP84) is encoded by the Hsp90ab1 (also known as Hsp84, Hspcb) gene (Gene ID: 301252) in rat. HSP90 is a ubiquitous chaperone protein with multiple functions in the cell. It promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. HSP90 undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, such as transcription factors, hormone receptors, and protein kinases, thereby causing their activation. HSP90 is abundant protein in the cell and may account for up to 2% of the total cytosolic protein. HSP90 is considered to be absolutely essential for cell survival. Its anti-apoptotic activity involves the inhibition of Apaf-1 oligomerization and caspase activation. Apart from its chaperone activity, HSP90 also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription by altering the steady-state levels of certain transcription factors in response to various physiological cues and also modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases. HSP90 can also participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression. Nitration of HSP90 results in decreased chaperone activity and intracellular release of the nitrated HSP90 is shown to induce induces death of PC12 cells. (Ref.: Ye, Y et al (2007). J. Biol. Chem. 282(9); 6324-6337).

Immunogen

Purified, nitrated HSP90 from rat liver.

Other Notes

Concentration: Please refer to lot specific datasheet.

Physical form

Protein G purified

Purified mouse monoclonal antibody IgG1 in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Format: Purified

Quality

Evaluated by Western Blotting in PC12 cells treated with pyroxynitrite.

Western Blotting Analysis: 0.25 µg/mL of this antibody detected nitrated HSP90 in PC12 cells treated with pyroxynitrite.

Specificity

Clone 44.23 detects nitrated HSP90 in rat, but not HSP90. It specifically targets nitrotyrosine 56.

Storage and Stability

Stable for 1 year at 2-8°C from date of receipt.

Target description

90 kDa observed; 83.28 kda calculated. Uncharacterized bands may be observed in some lysate(s).