Recombinant HSP90AA1 anticorps

N° du produit ABIN7127552

Cet anticorps Lapin Monoclonal détecte spécifiquement HSP90AA1 dans WB, IHC, ELISA, IF et IP. Il présente une réactivité envers Humain.

Aperçu rapide pour Recombinant HSP90AA1 anticorps (ABIN7127552)

Antigène: HSP90AA1 (Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 1 (HSP90AA1))

Type d'anticorp: Recombinant Antibody

Reactivité: Humain

Hôte: Lapin

Clonalité: Monoclonal

Conjugué: Cet anticorp HSP90AA1 est non-conjugé

Application: Western Blotting (WB), Immunohistochemistry (IHC), ELISA, Immunofluorescence (IF), Immunoprecipitation (IP)

Clone: 4B5

Détail du produit anti-HSP90AA1 anticorps

Fonction: HSP90AA1 Recombinant Monoclonal Antibody

Réactivité croisée: Rat

Purification: Affinity-chromatography

Immunogène: A synthesized peptide derived from human HSP90AA1

Isotype: IgG

Information d'application

Indications d'application: WB:1:500-1:5000, IHC:1:50-1:200, IF:1:20-1:200, IP:1:200-1:1000

Restrictions: For Research Use only

Stockage

Format: Liquid

Buffer: 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,-80 °C

Stockage commentaire: Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.

Détails sur HSP90AA1

Antigène: HSP90AA1 (Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 1 (HSP90AA1))

Autre désignation: HSP90AA1

Sujet:

Background: 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).

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

UniProt: P07900

Pathways: M Phase, Regulation of Cell Size, Signaling Events mediated by VEGFR1 and VEGFR2, VEGFR1 Specific Signals