Anti-Hsp90 alpha / HSP90AA1, clone BAD-8

Anti-Hsp90 alpha / HSP90AA1, clone BAD-8
Item number Size Datasheet Manual SDS Delivery time Quantity Price
NSJ-RQ5192 100 µl - -

3 - 10 business days*

755.00€
 
Antibody in PBS with 0.02% sodium azide, 50% glycerol and 0.4-0.5mg/ml BSA. The protein encoded... more
Product information "Anti-Hsp90 alpha / HSP90AA1, clone BAD-8"
Antibody in PBS with 0.02% sodium azide, 50% glycerol and 0.4-0.5mg/ml BSA. The protein encoded by the HSP90AA1 gene is an inducible molecular chaperone that functions as a homodimer. The encoded protein aids in the proper folding of specific target proteins by use of an ATPase activity that is modulated by co-chaperones. [RefSeq] Protein function: 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). [The UniProt Consortium]
Keywords: Anti-HSP86, Anti-LAP-2, Anti-HSP90A, Anti-HSP 86, Anti-Heat shock 86 kDa, Anti-LPS-associated protein 2, Anti-Heat shock protein HSP 90-alpha, Anti-Renal carcinoma antigen NY-REN-38, Anti-Lipopolysaccharide-associated protein 2, Hsp90 alpha Antibody / HSP
Supplier: NSJ Bioreagents
Supplier-Nr: RQ5192

Properties

Application: WB
Antibody Type: Monoclonal
Clone: BAD-8
Conjugate: No
Host: Rabbit
Species reactivity: human
Immunogen: A synthetic peptide specific to human HSP90 alpha / HSP90AA1
Format: Purified

Handling & Safety

Storage: -20°C
Shipping: -20°C (International: -20°C)
Caution
Our products are for laboratory research use only: Not for administration to humans!
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