HSP90AA1 anticorps (C-Term)
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- Antigène Voir toutes HSP90AA1 Anticorps
- HSP90AA1 (Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 1 (HSP90AA1))
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Épitope
- C-Term
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Reactivité
- Humain, Souris, Rat
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Hôte
- Lapin
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Clonalité
- Polyclonal
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Conjugué
- Cet anticorp HSP90AA1 est non-conjugé
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Application
- Western Blotting (WB), ELISA, Immunohistochemistry (IHC), Immunofluorescence (IF), Immunocytochemistry (ICC)
- Specificité
- Hsp90 alpha Antibody detects endogenous levels of total Hsp90 alpha.
- Homologie
- Pig,Bovine,Horse,Rabbit,Dog,Chicken
- Purification
- The antiserum was purified by peptide affinity chromatography using SulfoLinkTM Coupling Resin (Thermo Fisher Scientific).
- Immunogène
- 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 Anticorps primaire
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- Indications d'application
- 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.
- Agent conservateur
- Sodium azide
- Précaution d'utilisation
- This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
- Stock
- -20 °C
- Stockage commentaire
- Store at -20 °C. Stable for 12 months from date of receipt.
- Date de péremption
- 12 months
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- Antigène
- HSP90AA1 (Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 1 (HSP90AA1))
- Autre désignation
- HSP90AA1 (HSP90AA1 Produits)
- Synonymes
- anticorps EL52, anticorps HSP86, anticorps HSP89A, anticorps HSP90A, anticorps HSP90N, anticorps HSPC1, anticorps HSPCA, anticorps HSPCAL1, anticorps HSPCAL4, anticorps HSPN, anticorps Hsp89, anticorps Hsp90, anticorps LAP2, anticorps Hsp86, anticorps Hspca, anticorps htpG, anticorps 86kDa, anticorps 89kDa, anticorps AL024080, anticorps AL024147, anticorps Hsp86-1, anticorps hsp4, anticorps HSP90, anticorps HSP90AA1, anticorps fb17b01, anticorps hsp90, anticorps hsp90a, anticorps hsp90a.1, anticorps hsp90alpha, anticorps wu:fb17b01, anticorps zgc:86652, anticorps Hsp90alpha, anticorps heat shock protein 90 alpha family class A member 1, anticorps heat shock protein 90, alpha (cytosolic), class A member 1, anticorps Heat Shock Protein 90, cytosolic, anticorps heat shock protein 90A, anticorps molecular chaperone, anticorps heat shock protein 90, alpha (cytosolic), class A member 1, tandem duplicate 1, anticorps heat shock protein HSP 90-alpha, anticorps heat shock protein 90kDa alpha (cytosolic), class A member 1, anticorps HSP90AA1, anticorps Hsp90aa1, anticorps HSP90A, anticorps hsp90A, anticorps hsp90aa1.1, anticorps LOC108698781
- Sujet
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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
- Poids moléculaire
- 90kDa
- ID gène
- 3320
- UniProt
- P07900
- Pathways
- M Phase, Regulation of Cell Size, Signaling Events mediated by VEGFR1 and VEGFR2, VEGFR1 Specific Signals
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