Volume : 50 µL
Clone Number : 10D6
Aliases : Heat shock protein HSP 90-alpha, Heat shock 86 kDa, HSP 86, HSP86, Lipopolysaccharide-associated protein 2, LAP-2, LPS-associated protein 2, Renal carcinoma antigen NY-REN-38, HSP90AA1 HSP90A, HSPC1 HSPCA, Heat shock protein HSP 90-beta, HSP 90, Heat shock 84 kDa, HSP 84, HSP84, HSP90AB1 HSP90B, HSPC2, HSPCB
Product Type : Recombinant Antibody
Immunogen Species : Human
UniProt ID : P07900/P08238
Immunogen : A syntheVolumed peptide derived from human HSP90AA1/HSP90AB1
Raised in :
Species Reactivity : Human, Rat
Tested Applications : ELISA, WB, FC, IP; Recommended dilution : WB : 1 : 500-1 : 5000, IP : 1 : 200-1 : 1000
Background : Molec µLar chaperone that promotes the maturation, structural maintenance and proper reg µLation 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 mod µLate its substrate recognition, ATPase cycle and chaperone function (PubMed : 11274138, PubMed : 15577939, PubMed : 15937123, PubMed : 27353360, PubMed : 29127155). Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, sim µLtaneously 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). Apart from its chaperone activity, it also plays a role in the reg µLation of the transcription machinery. HSP90 and its co-chaperones mod µLate 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 mod µLate 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).
Clonality : Monoclonal
Isotype : Rabbit IgG
Purification Method : Affinity-chromatography
Conj µgate : Non-conj µgated
Buffer : Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
Form : Liquid
Stroage : Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Target Names : HSP90AA1/HSP90AB1
Research Areas : Signal Transduction