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HSP90AA1 (Heat Shock Protein 90) Antibody [HSP90AA1/7247]

In Stock
Catalog Number Formulation Size Price
3320-MSM7-P0
Purified Ab with BSA and Azide at 200ug/ml
20ug
$229.00
3320-MSM7-P1
Purified Ab with BSA and Azide at 200ug/ml
100ug
$519.00
3320-MSM7-P1ABX
Purified Ab WITHOUT BSA or Azide at 1.0mg/ml
100ug
$519.00
Flat Rate Domestic: $60 | Orders outside the US - Contact Us for Order Information | Ships next business day
Formalin-fixed, paraffin-embedded human kidney stained with HSP90AA1 Mouse Monoclonal Antibody (HSP90AA1/7247). Inset: PBS instead of primary antibody; secondary only negative control.

Formalin-fixed, paraffin-embedded human kidney stained with HSP90AA1 Mouse Monoclonal Antibody (HSP90AA1/7247). Inset: PBS instead of primary antibody; secondary only negative control.

Formalin-fixed, paraffin-embedded human prostate stained with HSP90AA1 Mouse Monoclonal Antibody (HSP90AA1/7247). HIER: Tris/EDTA, pH9.0, 45min. 2°C: HRP-polymer, 30min. DAB, 5min.

Formalin-fixed, paraffin-embedded human prostate stained with HSP90AA1 Mouse Monoclonal Antibody (HSP90AA1/7247). HIER: Tris/EDTA, pH9.0, 45min. 2°C: HRP-polymer, 30min. DAB, 5min.

Applications & Dilutions

Applications Tested Dillution Protocol Note
Immunohistochemistry (IHC)
1-2ug/ml
IHC Protocol
30 min at RT. Staining of formalin-fixed tissues requires heating tissue sections in 10mM Tris with 1mM EDTA, pH 9.0, for 45 min at 95°C followed by cooling at RT for 20 minutes

Summary

The heat shock response was first described for Drosophila salivary gland cells and morphologically consists of a change in their polytene chromosome puffing patterns that involves de novo synthesis of a few proteins. Similar heat shock proteins were later discovered in bacterial chicken and mammalian cells, and have been subsequently studied in other organisms. A series of proteins including HSP 90, HSP 70, HSP 20-30 and ubiquitin are induced by insults such as temperature shock, chemicals and other environmental stress. A major function of HSP 90 and other HSPs is to act as molecular chaperones. HSP 90 forms a complex with glucocorticoid receptor (GR), rendering the non ligand-bound receptor transcriptionally inactive. HSP 90 binds the GR as a heterocomplex composed of either HSP 56 or Cyclophilin D, forming an aporeceptor comiplex. HSP 90 also exists as a dimer with other proteins such as p60/sti1 and p23, forming an apo-receptor complex with estrogen and androgen receptors.

Product Properties & Targets

Antibody Type
Mouse Monoclonals
Host
Mouse
Applications
Immunohistochemistry
Species Reactivity
Human
Research Areas
Cardiovascular, Developmental Biology, Immunology, AKT Signaling, Cytokine Signaling, Infectious Disease, Signal Transduction, Transcription Factors
Isotype / Light Chain
IgG1 / Kappa
Cellular Localization
Cytoplasm. Melanosome.
Gene Name
HSP90AA1
Positive Control
Human spleen|stomach or pancreas tissue. MCF-7 cells.
Immunogen
Recombinant fragment (around aa500-700) of human HSP90AA1 protein (exact sequence is proprietary)
Alternate Names
Heat shock protein HSP 90-alpha, Heat shock 86 kDa, Lipopolysaccharide-associated protein 2, Renal carcinoma antigen NY-REN-38, Heat shock protein 90kDa alpha cytosolic class A member 1; Heat shock protein HSP 90 alpha; HSP 84; HSP 86; Hsp 90; HSP86; HSP90A; HSP90AA1; HSPC1; HSPC2; HSPCAL1; HSPCAL4; Renal carcinoma antigen NY-REN-38

Database Links

Entrez Gene ID
3320
SwissProt
P07900

Additional Information

Clone
HSP90AA1/7247
Chromosome Location
14q32.31
Mol. Weight of Antigen
90kDa

Related Antibodies

View All HSP90AA1 Antibodies

Functions

  • Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (PubMed:11274138, PubMed:15577939, PubMed:15937123, PubMed:27353360, PubMed:29127155, PubMed:12526792). Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself (PubMed:29127155). Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle (PubMed:27295069, PubMed:26991466). Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70 (PubMed:12526792). Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels (PubMed:25973397). In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues(PubMed:25973397). Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment (PubMed:25973397). Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed:25973397). Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:11276205). Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385). Mediates the association of TOMM70 with IRF3 or TBK1 in mitochondrial outer membrane which promotes host antiviral response (PubMed:20628368, PubMed:25609812).
  • (Microbial infection) Seems to interfere with N.meningitidis NadA-mediated invasion of human cells. Decreasing HSP90 levels increases adhesion and entry of E.coli expressing NadA into human Chang cells; increasing its levels leads to decreased adhesion and invasion.

Key References

  • Toft, D.O., et al. Biochemistry 24.23 (1985 Nov 5): 6586-91.

PubMed Links

Storage & Stability

Antibody with azide - store at 2 to 8°C. Antibody is stable for 24 months.,Non-hazardous. No MSDS required.

Limitations

This antibody is available for research use only and is not approved for use in diagnosis.

Supplied as

200ug/ml of Ab purified from Bioreactor Concentrate by Protein A/G. Prepared in 10mM PBS with 0.05% BSA & 0.05% azide. Also available WITHOUT BSA at 1.0mg/ml.

Warranty

There are no warranties, expressed or implied, which extend beyond this description. Company is not liable for any personal injury or economic loss resulting from this product.

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