Anti-HSP90 Antibody
Produktgrößen
50 ug
£326,00
OAED00193-50UG
Über dieses Produkt
- SKU:
- OAED00193
- Zusätzliche Namen:
- D6S182;EL52;epididymis luminal secretory protein 52;epididymis secretory sperm binding protein Li 65p;heat shock 84 kDa;heat shock 86 kDa;heat shock 90kD protein 1; alpha;heat shock 90kD protein 1; alpha-like 4;heat shock 90kD protein 1; beta;heat shock 90kD protein; alpha-like 4;heat shock 90kDa protein 1; alpha;heat shock protein 90 kDa;heat shock protein 90kDa alpha (cytosolic); class A member 1;heat shock protein 90kDa alpha (cytosolic); class B member 1;heat shock protein 90kDa alpha family class A member 1;heat shock protein 90kDa alpha family class B member 1;heat shock protein HSP 90-alpha;heat shock protein HSP 90-beta;HEL-S-65p;HSP 86;Hsp103;HSP84;HSP86;Hsp89;HSP89A;Hsp90;HSP90A;HSP90B;HSP90-beta;HSP90N;HSPC1;HSPC2;HSPCA;HSPCAL1;HSPCAL4;HSPCB;HSPN;LAP2;LAP-2;lipopolysaccharide-associated protein 2;LPS-associated protein 2;renal carcinoma antigen NY-REN-38.
- Klonalität:
- Polyclonal
- Weitere Details:
- 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).|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).
- Gendetails:
- heat shock protein 90 alpha family class A member 1|heat shock protein 90 alpha family class B member 1
- Host:
- Rabbit
- Immunogen:
- Synthetic peptide corresponding to aa 250-325 of human Hsp90.
- Proteindetails:
- Heat shock protein HSP 90-alpha|Heat shock protein HSP 90-beta
- Reinheit:
- Protein A affinity purified.<br/>
- Versandbedingungen:
- Blue Ice
- Lagerbedingungen:
- Long Term Storage : -20C
- Hersteller:
- Aviva Systems Biology
- Typ:
- Antibodies: Polyclonal Antibody
- Datenblatt des Herstellers:html_datasheet.php