Anti-HSP90α (P717) Antibody |产品详情|进口试剂采购网

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Anti-HSP90α (P717) Antibody

品牌：Antibodies

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规格：50µl

货期：

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Anti-HSP90α (P717) Antibody

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Overview

Name:	Anti-HSP90α (P717) Antibody See all HSP90α primary antibodies
Description:	Rabbit polyclonal antibody to HSP90α (P717)
Specificity:	HSP90α (P717) pAb detects endogenous levels of HSP90α protein.
Applications:	WB, IHC, IF
Reactivity:	Human, Mouse, Rat
Immunogen:	Synthetic peptide, corresponding to amino acids 671-720 of Human HSP90α.
Host:	Rabbit
Clonality:	Polyclonal
Conjugate:	Unconjugated
Molecular Weight:	~ 85, 90 kDa
Purity:	The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Product Form:	1 mg/ml in Phosphate buffered saline (PBS) with 15 mM sodium azide, approx. pH 7.2.

Target

Function:	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). 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). 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).
Sequence Similarities:	Belongs to the heat shock protein 90 family.
Post-Translational Modification:	ISGylated.
Cellular Location:	Cytoplasm. Melanosome. Cell membrane. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.