HSP90 alpha/beta antibody

Catalog No. ABIN7384453

Product Details anti-HSP90 alpha/beta Antibody

Target: HSP90 alpha/beta (Heat Shock Protein 90 alpha/beta (HSP90 alpha/beta))

Reactivity: Human, Rat, Mouse

Host: Rabbit

Clonality: Monoclonal

Conjugate: This HSP90 alpha/beta antibody is un-conjugated

Application: Western Blotting (WB), Immunofluorescence (IF), Immunohistochemistry (Paraffin-embedded Sections) (IHC (p)), Immunoprecipitation (IP)

Purification: Affinity Purified

Clone: R08-8A1

Isotype: IgG

Application Details

Application Notes: WB 1:1000-1:2000 IHC 1:50-1:200 IF 1:50-1:200

Restrictions: For Research Use only

Handling

Concentration: 300 μg/mL

Buffer: 50 mM Tris-Glycine( pH 7.4), 0.15M NaCl, 40 % Glycerol, 0.01 % Sodium azide and 0.05 % BSA

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. Avoid freeze / thaw cycles.

Target Details for HSP90 alpha/beta

Target: HSP90 alpha/beta (Heat Shock Protein 90 alpha/beta (HSP90 alpha/beta))

Alternative Name: Hsp90 alpha/beta (HSP90 alpha/beta Products)

Background: HSP84,HSPC2,HSPCB,D6S182,HSP90B,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. 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:16478993, PubMed:19696785). 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. 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. In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues. 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. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed:25973397). Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385). Promotes cell differentiation by chaperoning BIRC2 and thereby protecting from auto-ubiquitination and degradation by the proteasomal machinery (PubMed:18239673). Main chaperone that is involved in the phosphorylation/activation of the STAT1 by chaperoning both JAK2 and PRKCE under heat shock and in turn, activates its own transcription (PubMed:20353823).

Molecular Weight:

Observed_MW: 90kDa

Calculated_MW: 85/83kDa

Gene ID: 3326