HSP90 alpha Protein, Human, Recombinant (His)

Heat shock protein 90 (90 kDa heat-shock protein, HSP90) is a molecular chaperone involved in the trafficking of proteins in the cell. It is a remarkably versatile protein involved in the stress response and normal homoeostatic control mechanisms. HSP90 interacts with 'client proteins', including protein kinases, transcription factors, and others, and either facilitates their stabilization and activation or directs them for proteasomal degradation. By this means, HSP90 displays a multifaceted ability to influence signal transduction, chromatin remodeling and epigenetic regulation, development, and morphological evolution. HSP90 operates as a dimer in a conformational cycle driven by ATP binding and hydrolysis at the N-terminus. Disruption of HSP90 leads to client protein degradation and often cell death. Under stressful conditions, HSP90 stabilizes its client proteins and protects the cell against cellular stressors such as in cancer cells. Especially, several oncoproteins act as HSP90 client proteins and tumor cells require higher HSP90 activity than normal cells to maintain their malignancy. For this reason, Hsp90 has emerged as a promising target for anti-cancer drug development.

Pack Size	Availability	Price/USD	Quantity
100 μg	5 days	$ 700.00
1 mg	5 days	$ 4,560.00

Description

Species	Human
Expression System	Baculovirus-Insect Cells
Tag	His
Accession Number	NP_005339.3
Synonyms	EL52, HSP89A, heat shock protein 90kDa alpha (cytosolic), class A member 1, HSPN, HSPCAL4, HSPCA, HSP90N, heat shock protein 90kDa α (cytosolic), class A member 1, HSPCAL1, Hsp90 α, HSPC1, LAP2, Hsp89, LAP-2, HSP86, Hsp90, HSP90A
Construction	A DNA sequence encoding the Human HSP90AA1 (NP_005339.3) (Met1-Asp732) was expressed, with a polyhistidine tag at the N-terminus.
Protein Purity	≥ 90 % as determined by SDS-PAGE.
Molecular Weight	Approxiamtely 87.06 kDa

Endotoxin	< 1.0 EU per μg protein as determined by the LAL method.
Formulation	Lyophilized from sterile 20mM Pb, 300mM Nacl, 10% glycerol, 0. 5mM PMSF, pH 7.0. Please contact us for any concerns or special requirements. Normally 5 % - 8 % trehalose, mannitol and 0. 01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hard copy of CoA.
Reconstitution	A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information.
Stability & Storage	Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Shipping	In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Research Background	Heat shock protein 90 (90 kDa heat-shock protein, HSP90) is a molecular chaperone involved in the trafficking of proteins in the cell. It is a remarkably versatile protein involved in the stress response and normal homoeostatic control mechanisms. HSP90 interacts with 'client proteins', including protein kinases, transcription factors, and others, and either facilitates their stabilization and activation or directs them for proteasomal degradation. By this means, HSP90 displays a multifaceted ability to influence signal transduction, chromatin remodeling and epigenetic regulation, development, and morphological evolution. HSP90 operates as a dimer in a conformational cycle driven by ATP binding and hydrolysis at the N-terminus. Disruption of HSP90 leads to client protein degradation and often cell death. Under stressful conditions, HSP90 stabilizes its client proteins and protects the cell against cellular stressors such as in cancer cells. Especially, several oncoproteins act as HSP90 client proteins and tumor cells require higher HSP90 activity than normal cells to maintain their malignancy. For this reason, Hsp90 has emerged as a promising target for anti-cancer drug development.