Heat shock protein HSP 90-alpha (HSP90AA1) Recombinant Protein | HSP90AA1 recombinant protein

Recombinant Cricetulus griseus Heat shock protein HSP 90-alpha (HSP90AA1), partial

• Gene Names: Hsp90aa1; HSPCA; Hsp90a
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Heat shock protein HSP 90-alpha (HSP90AA1); Recombinant Cricetulus griseus Heat shock protein HSP 90-alpha (HSP90AA1); partial; HSP90AA1 recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Length: 733

• Species: Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
• Preparation and Storage: Store at -20 degrees C. For long-term storage, store at -20 degrees C or -80 degrees C. Store working aliquots at 4 degrees C for up to one week. Repeated freezing and thawing is not recommended.

NCBI and Uniprot Product Information

• NCBI GI #: 350540064
• NCBI GeneID: 100689397
• NCBI Accession #: NP_001233750.1
• NCBI GenBank Nucleotide #: NM_001246821.1
• UniProt Accession #: P46633
• Molecular Weight: 84,849 Da
• NCBI Official Full Name: heat shock protein HSP 90-alpha
• NCBI Official Symbol: Hsp90aa1
• NCBI Official Synonym Symbols: HSPCA; Hsp90a
• NCBI Protein Information: heat shock protein HSP 90-alpha
• UniProt Protein Name: Heat shock protein HSP 90-alpha
• Protein Family: Heat shock protein
• UniProt Gene Name: HSP90AA1
• UniProt Synonym Gene Names: HSP90A; HSPCA

Uniprot Description

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. 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. 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. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes. Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation.