HSP90AA1 Recombinant Protein
Product Sizes
10ug
£218.00
OPCD04005-10UG
50ug
£387.00
OPCD04005-50UG
200ug
£673.00
OPCD04005-200UG
About this Product
- SKU:
- OPCD04005
- Additional Names:
- EL52;epididymis luminal secretory protein 52;epididymis secretory sperm binding protein Li 65p;heat shock 86 kDa;heat shock 90kD protein 1; alpha;heat shock 90kD protein 1; alpha-like 4;heat shock 90kD protein; alpha-like 4;heat shock 90kDa protein 1; alpha;heat shock protein 90kDa alpha (cytosolic); class A member 1;heat shock protein 90kDa alpha family class A member 1;heat shock protein HSP 90-alpha;HEL-S-65p;HSP 86;Hsp103;HSP86;Hsp89;HSP89A;Hsp90;HSP90A;HSP90N;HSPC1;HSPCA;HSPCAL1;HSPCAL4;HSPN;LAP2;LAP-2;lipopolysaccharide-associated protein 2;LPS-associated protein 2;renal carcinoma antigen NY-REN-38.
- Conjugate:
- Unconjugated
- Concentration:
- 200 ug/mL (prior to lyoph)
- Extra 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).
- Gene Details:
- heat shock protein 90 alpha family class A member 1
- Host:
- E. coli
- Molecular Weight:
- 72kDa
- Protein Details:
- Heat shock protein HSP 90-alpha
- Purity:
- > 95%
- Shipping Conditions:
- Blue Ice
- Source:
- E.coli
- Storage Conditions:
- 2Â[o]C to 8Â[o]C|-80Â[o]C
- Supplier:
- Aviva Systems Biology
- Type:
- Proteins, Peptides, Small Molecules & Other Biomolecules: Recombinant Proteins
- Manufacturer's Data Sheet:html_datasheet.php
