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

BHP10505769
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Subcellular Location Nucleus, Cytoplasm, Melanosome, Cell membrane
Uniprot O02705, O02705
Database Links

KEGG:ssc:397028

STRING:9823.ENSSSCP00000002743

UniGene:Ssc.12191
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. 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. Interacts with HECTD1 (via N-terminus) (By similarity).
Pathway Estrogen signaling pathway; PI3K-Akt signaling pathway; Protein processing in endoplasmic reticulum; Necroptosis; Antigen processing and presentation; IL-17 signaling pathway; NOD-like receptor signaling pathway; Th17 cell differentiation
Protein Families Heat shock protein 90 family
Research Area Signal Transduction
Tissue Specificity Preferentially expressed in pituitary gland, brain, adrenal gland, and testis, in comparison to other tissues.
Weight 19.7 kDa
Stotage Note Repeated freezing and thawing is not recommended. Store working aliquots at 4℃ for up to one week.
Buffer Tris-based buffer，50% glycerol
Purity Greater than 90% as determined by SDS-PAGE.
Storage The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Storage Buffer Tris-based buffer,50% glycerol
Immunogen Species Sus Scrofa (Pig)
SKU Supplier No. Size Your price Quantity
BHP10505769 CSB-BP010802PI 100ug $1322
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BHP10505769 CSB-BP010802PI 20ug $472
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