Comparison

HSP90AA1 Recombinant Protein

Item no. OPCD04005
Manufacturer AVIVA Systems Biology
Amount 10 ug
Category
Type Proteins Recombinant
Applications WB, SDS-PAGE
Specific against Human (Homo sapiens)
Host E.coli
Conjugate/Tag Unconjugated; HIS
Purity > 95%
ECLASS 10.1 32160409
ECLASS 11.0 32160409
UNSPSC 12352202
Alias 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.
Available
Manufacturer - Type
Protein
Manufacturer - Applications
Positive control|Sodium sodecyl sulfate - polyacrylamide gel electrophoresis|Western blot
Manufacturer - Category
Root Catalog/Products/Recombinant Proteins
Manufacturer - Conjugate / Tag
N-terminal His Tag
Molecular Weight
72kDa
Gene symbol
HSP90AA1
Gene Fullname
heat shock protein 90 alpha family class A member 1
Protein size
Recombinant
Product format
Freeze-dried Powder. PBS, pH7.4, containing 0.01% SKL, 5% Trehalose.
Reconstitution and storage
2°C to 8°C|-80°C
Description of target
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).
Nucleotide accession_num
NM_001017963.2
Protein accession_num
NP_001017963.2
Protein name
Heat shock protein HSP 90-alpha
Formulation
20mM Tris, 150mM NaCl, pH8.0, containing 1mM EDTA, 1mM DTT, 0.01% SKL, 5% Trehalose and Proclin300.
Concentration
200 ug/mL (prior to lyoph)

Note: The presented information and documents (Manual, Product Datasheet, Safety Datasheet and Certificate of Analysis) correspond to our latest update and should serve for orientational purpose only. We do not guarantee the topicality. We would kindly ask you to make a request for specific requirements, if necessary.

All products are intended for research use only (RUO). Not for human, veterinary or therapeutic use.

Amount: 10 ug
Available: In stock
available

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