HSP90AA1 Antikörper (C-Term)

Produktnummer ABIN6254913

Produktdetails anti-HSP90AA1 Antikörper

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

Bindungsspezifität: C-Term

Reaktivität: Human, Maus, Ratte

Wirt: Kaninchen

Klonalität: Polyklonal

Konjugat: Dieser HSP90AA1 Antikörper ist unkonjugiert

Applikation: Western Blotting (WB), Immunohistochemistry (IHC), ELISA, Immunofluorescence (IF), Immunocytochemistry (ICC)

Spezifität: Hsp90 alpha Antibody detects endogenous levels of total Hsp90 alpha.

Homologie: Pig,Bovine,Horse,Rabbit,Dog,Chicken

Aufreinigung: The antiserum was purified by peptide affinity chromatography using SulfoLink^TM Coupling Resin (Thermo Fisher Scientific).

Immunogen: A synthesized peptide derived from human Hsp90 alpha, corresponding to a region within C-terminal amino acids.

Isotyp: IgG

Anwendungsinformationen

Applikationshinweise: WB 1:500-1:2000, IHC 1:50-1:200, IF/ICC 1:100-1:500, ELISA(peptide) 1:20000-1:40000

Beschränkungen: Nur für Forschungszwecke einsetzbar

Handhabung

Format: Liquid

Konzentration: 1 mg/mL

Buffer: Rabbit IgG in phosphate buffered saline , pH 7.4, 150 mM NaCl, 0.02 % sodium azide and 50 % glycerol.

Konservierungsmittel: Sodium azide

Vorsichtsmaßnahmen: This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.

Lagerung: -20 °C

Informationen zur Lagerung: Store at -20 °C. Stable for 12 months from date of receipt.

Haltbarkeit: 12 months

Details zu HSP90AA1

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

Andere Bezeichnung: HSP90AA1 (HSP90AA1 Produkte)

Synonyme: EL52 antikoerper, HSP86 antikoerper, HSP89A antikoerper, HSP90A antikoerper, HSP90N antikoerper, HSPC1 antikoerper, HSPCA antikoerper, HSPCAL1 antikoerper, HSPCAL4 antikoerper, HSPN antikoerper, Hsp89 antikoerper, Hsp90 antikoerper, LAP2 antikoerper, Hsp86 antikoerper, Hspca antikoerper, htpG antikoerper, 86kDa antikoerper, 89kDa antikoerper, AL024080 antikoerper, AL024147 antikoerper, Hsp86-1 antikoerper, hsp4 antikoerper, HSP90 antikoerper, HSP90AA1 antikoerper, fb17b01 antikoerper, hsp90 antikoerper, hsp90a antikoerper, hsp90a.1 antikoerper, hsp90alpha antikoerper, wu:fb17b01 antikoerper, zgc:86652 antikoerper, Hsp90alpha antikoerper, heat shock protein 90 alpha family class A member 1 antikoerper, heat shock protein 90, alpha (cytosolic), class A member 1 antikoerper, Heat Shock Protein 90, cytosolic antikoerper, heat shock protein 90A antikoerper, molecular chaperone antikoerper, heat shock protein 90, alpha (cytosolic), class A member 1, tandem duplicate 1 antikoerper, heat shock protein HSP 90-alpha antikoerper, heat shock protein 90kDa alpha (cytosolic), class A member 1 antikoerper, HSP90AA1 antikoerper, Hsp90aa1 antikoerper, HSP90A antikoerper, hsp90A antikoerper, hsp90aa1.1 antikoerper, LOC108698781 antikoerper

Hintergrund:

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

Molekulargewicht: 90kDa

Gen-ID: 3320

UniProt: P07900

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