Catalog No: OPED00071
Size:50 ug
Price: $463.00
SKU
OPED00071
Availability: Domestic: within 1-2 week delivery | International: 1-2 week
Bulk
Order
Aviva's
Satisfaction
Guarantee
Contact Us:
Shipping Info:
  • $55: Antibody & Protein in US
  • $55 + $25/Kit in US
  • Contact us for international orders.
Datasheets/ManualsPrintable datasheet for HSP90AA1 Recombinant Protein (Human) (OPED00071) (OPED00071)
Please click here to view the MSDS.
Product Info
Predicted Species ReactivityHomo sapiens|Human
Product FormatLiquid 50mM Tris-HCl (pH 7.5) containing 1mM DTT and 100mM sodium chloride
HostHeLa cells
ApplicationELISA, WB, Antigen microarray
Reconstitution and StorageShipped on Dry Ice. Store at -80°C.
PurificationPurified by multi-step chromatography.
ConcentrationVaries by lot. See vial for concentration.
Purity≥90% (SDS-PAGE; Western blot)
SpecificityImmunoreactive with antibodies specific for Hsp90 Beta as well as those which do not discriminate between isoforms.
Application InfoWB: 100 ng, colorimetric. Western Blot control.
ReferenceCpG-A stimulates Hsp72 secretion from plasmacytoid dendritic cells, facilitating cross-presentation: T. Tanaka, et al.; Immunol. Lett. 167, 34 (2015), Application(s): ELISAusing human or murine DCs , Abstract;
The Effects of Acute Waterborne Exposure to Sublethal Concentrations of Molybdenum on the Stress Response in Rainbow Trout, Oncorhynchus mykiss: C.D. Ricketts, et al.; PLoS One 10, e0115334 (2015), Application(s): Western Blotting, Abstract; Full Text
Antigen microarrays identify unique serum autoantibody signatures inclinical and pathologic subtypes of multiple sclerosis: H. Weiner, et al. ; PNAS 105, 18889 (2008), Application(s): Antigen Microarray , Abstract;
CAIR-1/BAG-3 abrogates heat shock protein-70 chaperone complex-mediated protein degradation: accumulation of poly-ubiquitinated Hsp90 client proteins: E.C. Kohn, et al. ; J. Biol. Chem. 278, 28490 (2003), Application(s): WB , Abstract;
Development of a purine-scaffold novel class of Hsp90 binders that inhibit the proliferation of cancer cells and induce the degradation of Her2 tyrosine kinase: N. Rosen, et al. ; Bioorg. Med. Chem. 10, 3555 (2002), Abstract;
Hsp90 makes the human HBV Pol competent for in vitro priming rather than maintaining the human HBV Pol/pregenomic RNA complex: G. Jung, et al. ; Arch. Biochem. Biophys. 401, 99 (2002), Application(s): WB , Abstract;
Identification of heat shock protein90 and other proteins as tumour antigens by serological screening of an ovarian carcinoma expression library: E.P. Diamandis, et al. ; Br. J. Cancer 87, 339 (2002), Application(s): EIA , Abstract;
Hsp25 and -90 immunoreactivity in the normal rat eye: M. Tytell, et al. ; Invest. Ophthalmol. Vis. Sci. 42, 3031 (2001), Application(s): WB , Abstract;CpG-A stimulates Hsp72 secretion from plasmacytoid dendritic cells, facilitating cross-presentation: T. Tanaka, et al.; Immunol. Lett. 167, 34 (2015), Application(s): ELISAusing human or murine DCs , Abstract;
The Effects of Acute Waterborne Exposure to Sublethal Concentrations of Molybdenum on the Stress Response in Rainbow Trout, Oncorhynchus mykiss: C.D. Ricketts, et al.; PLoS One 10, e0115334 (2015), Application(s): Western Blotting, Abstract; Full Text
Antigen microarrays identify unique serum autoantibody signatures inclinical and pathologic subtypes of multiple sclerosis: H. Weiner, et al. ; PNAS 105, 18889 (2008), Application(s): Antigen Microarray , Abstract;
CAIR-1/BAG-3 abrogates heat shock protein-70 chaperone complex-mediated protein degradation: accumulation of poly-ubiquitinated Hsp90 client proteins: E.C. Kohn, et al. ; J. Biol. Chem. 278, 28490 (2003), Application(s): WB , Abstract;
Development of a purine-scaffold novel class of Hsp90 binders that inhibit the proliferation of cancer cells and induce the degradation of Her2 tyrosine kinase: N. Rosen, et al. ; Bioorg. Med. Chem. 10, 3555 (2002), Abstract;
Hsp90 makes the human HBV Pol competent for in vitro priming rather than maintaining the human HBV Pol/pregenomic RNA complex: G. Jung, et al. ; Arch. Biochem. Biophys. 401, 99 (2002), Application(s): WB , Abstract;
Identification of heat shock protein90 and other proteins as tumour antigens by serological screening of an ovarian carcinoma expression library: E.P. Diamandis, et al. ; Br. J. Cancer 87, 339 (2002), Application(s): EIA , Abstract;
Hsp25 and -90 immunoreactivity in the normal rat eye: M. Tytell, et al. ; Invest. Ophthalmol. Vis. Sci. 42, 3031 (2001), Application(s): WB , Abstract;
Gene SymbolHSP90AA1|HSP90AB1
Gene Full Nameheat shock protein 90 alpha family class A member 1|heat shock protein 90 alpha family class B member 1
Alias SymbolsD6S182;EL52;epididymis luminal secretory protein 52;epididymis secretory sperm binding protein Li 65p;heat shock 84 kDa;heat shock 86 kDa;heat shock 90kD protein 1, alpha;heat shock 90kD protein 1, alpha-like 4;heat shock 90kD protein 1, beta;heat shock 90kD protein, alpha-like 4;heat shock 90kDa protein 1, alpha;heat shock protein 90 kDa;heat shock protein 90kDa alpha (cytosolic), class A member 1;heat shock protein 90kDa alpha (cytosolic), class B member 1;heat shock protein 90kDa alpha family class A member 1;heat shock protein 90kDa alpha family class B member 1;heat shock protein HSP 90-alpha;heat shock protein HSP 90-beta;HEL-S-65p;HSP 86;Hsp103;HSP84;HSP86;Hsp89;HSP89A;Hsp90;HSP90A;HSP90B;HSP90-beta;HSP90N;HSPC1;HSPC2;HSPCA;HSPCAL1;HSPCAL4;HSPCB;HSPN;LAP2;LAP-2;lipopolysaccharide-associated protein 2;LPS-associated protein 2;renal carcinoma antigen NY-REN-38.
NCBI Gene Id3320|3326
Protein NameHeat shock protein HSP 90-alpha|Heat shock protein HSP 90-beta
Description of TargetMolecular 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). 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). 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).|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. 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:16478993, PubMed:19696785). 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. 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 regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues. 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. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed:25973397). Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385). Promotes cell differentiation by chaperoning BIRC2 and thereby protecting from auto-ubiquitination and degradation by the proteasomal machinery (PubMed:18239673). Main chaperone that is involved in the phosphorylation/activation of the STAT1 by chaperoning both JAK2 and PRKCE under heat shock and in turn, activates its own transcription (PubMed:20353823).
Uniprot IDP07900|P08238
Protein Accession #NP_001284491.1
Nucleotide Accession #NM_001297562.1
Protein Size (# AA)Native
Molecular Weight90 kDa
Write Your Own Review
You're reviewing:HSP90AA1 Recombinant Protein (Human) (OPED00071)
Your Rating
We found other products you might like!