HSP90AA1 Antibody

Datasheet
Code CSB-RA011087A1HU
Size US$350
Uniprot No. P07900
Image
  • IHC image of CSB-RA011087A1HU diluted at 1:87.5 and staining in paraffin-embedded human endometrial cancer performed on a Leica BondTM system. After dewaxing and hydration, antigen retrieval was mediated by high pressure in a citrate buffer (pH 6.0). Section was blocked with 10% normal goat serum 30min at RT. Then primary antibody (1% BSA) was incubated at 4°C overnight. The primary is detected by a biotinylated secondary antibody and visualized using an HRP conjugated SP system.

  • IHC image of CSB-RA011087A1HU diluted at 1:87.5 and staining in paraffin-embedded human testis tissue performed on a Leica BondTM system. After dewaxing and hydration, antigen retrieval was mediated by high pressure in a citrate buffer (pH 6.0). Section was blocked with 10% normal goat serum 30min at RT. Then primary antibody (1% BSA) was incubated at 4°C overnight. The primary is detected by a biotinylated secondary antibody and visualized using an HRP conjugated SP system.

  • Immunofluorescence staining of Hela cells with CSB-RA011087A1HU at 1:29, counter-stained with DAPI. The cells were fixed in 4% formaldehyde, permeabilized using 0.2% Triton X-100 and blocked in 10% normal Goat Serum. The cells were then incubated with the antibody overnight at 4°C. The secondary antibody was Alexa Fluor 488-congugated AffiniPure Goat Anti-Rabbit IgG (H+L).

Protocols ELISA Protocol
Immunohistochemistry (IHC) Protocol
Immunofluorescence (IF) Protocol
Immunogen A synthesized peptide derived from human HSP90AA1
Species Reactivity Human
Tested Applications ELISA, IHC, IF; Recommended dilution: IHC:1:50-1:200, IF:1:20-1:200
Relevance 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). 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).
Form Liquid
Conjugate Non-conjugated
Storage Buffer Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
Purification Method Affinity-chromatography
Isotype Rabbit IgG
Clonality Monoclonal
Alias 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
Immunogen Species Human
Research Area Signal Transduction
Gene Names HSP90AA1
Storage Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
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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
Subcellular Location Nucleus, Cytoplasm, Melanosome, Cell membrane
Protein Families Heat shock protein 90 family
Database Links

HGNC: 5253

OMIM: 140571

KEGG: hsa:3320

STRING: 9606.ENSP00000335153

UniGene: Hs.525600

Pathway Estrogen signaling pathway
PI3K-Akt signaling pathway
Necroptosis
Protein processing in endoplasmic reticulum
Antigen processing and presentation
IL-17 signaling pathway
NOD-like receptor signaling pathway
Th17 cell differentiation

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