HSP90AA1 antibody (C-Term)
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- Target See all HSP90AA1 Antibodies
- HSP90AA1 (Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 1 (HSP90AA1))
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Binding Specificity
- C-Term
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Reactivity
- Human, Mouse, Rat
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Host
- Rabbit
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Clonality
- Polyclonal
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Conjugate
- This HSP90AA1 antibody is un-conjugated
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Application
- Western Blotting (WB), Immunohistochemistry (IHC), ELISA, Immunofluorescence (IF), Immunocytochemistry (ICC)
- Specificity
- Hsp90 alpha Antibody detects endogenous levels of total Hsp90 alpha.
- Predicted Reactivity
- Pig,Bovine,Horse,Rabbit,Dog,Chicken
- Purification
- The antiserum was purified by peptide affinity chromatography using SulfoLinkTM Coupling Resin (Thermo Fisher Scientific).
- Immunogen
- A synthesized peptide derived from human Hsp90 alpha, corresponding to a region within C-terminal amino acids.
- Isotype
- IgG
- Top Product
- Discover our top product HSP90AA1 Primary Antibody
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- Application Notes
- WB 1:500-1:2000, IHC 1:50-1:200, IF/ICC 1:100-1:500, ELISA(peptide) 1:20000-1:40000
- Restrictions
- For Research Use only
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- Format
- Liquid
- Concentration
- 1 mg/mL
- Buffer
- Rabbit IgG in phosphate buffered saline , pH 7.4, 150 mM NaCl, 0.02 % sodium azide and 50 % glycerol.
- Preservative
- Sodium azide
- Precaution of Use
- This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
- Storage
- -20 °C
- Storage Comment
- Store at -20 °C. Stable for 12 months from date of receipt.
- Expiry Date
- 12 months
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Hsp90β promotes aggressive vasculogenic mimicry via epithelial-mesenchymal transition in hepatocellular carcinoma." in: Oncogene, (2018) (PubMed).
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Hsp90β promotes aggressive vasculogenic mimicry via epithelial-mesenchymal transition in hepatocellular carcinoma." in: Oncogene, (2018) (PubMed).
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- Target
- HSP90AA1 (Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 1 (HSP90AA1))
- Alternative Name
- HSP90AA1 (HSP90AA1 Products)
- Synonyms
- EL52 antibody, HSP86 antibody, HSP89A antibody, HSP90A antibody, HSP90N antibody, HSPC1 antibody, HSPCA antibody, HSPCAL1 antibody, HSPCAL4 antibody, HSPN antibody, Hsp89 antibody, Hsp90 antibody, LAP2 antibody, Hsp86 antibody, Hspca antibody, htpG antibody, 86kDa antibody, 89kDa antibody, AL024080 antibody, AL024147 antibody, Hsp86-1 antibody, hsp4 antibody, HSP90 antibody, HSP90AA1 antibody, fb17b01 antibody, hsp90 antibody, hsp90a antibody, hsp90a.1 antibody, hsp90alpha antibody, wu:fb17b01 antibody, zgc:86652 antibody, Hsp90alpha antibody, heat shock protein 90 alpha family class A member 1 antibody, heat shock protein 90, alpha (cytosolic), class A member 1 antibody, Heat Shock Protein 90, cytosolic antibody, heat shock protein 90A antibody, molecular chaperone antibody, heat shock protein 90, alpha (cytosolic), class A member 1, tandem duplicate 1 antibody, heat shock protein HSP 90-alpha antibody, heat shock protein 90kDa alpha (cytosolic), class A member 1 antibody, HSP90AA1 antibody, Hsp90aa1 antibody, HSP90A antibody, hsp90A antibody, hsp90aa1.1 antibody, LOC108698781 antibody
- Background
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Description: 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).
Gene: HSP90AA1
- Molecular Weight
- 83 kDa
- Gene ID
- 3320
- UniProt
- P07900
- Pathways
- M Phase, Regulation of Cell Size, Signaling Events mediated by VEGFR1 and VEGFR2, VEGFR1 Specific Signals
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