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HSP90 alpha Protein, Mouse, Recombinant (His)

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HSP90 alpha Protein, Mouse, Recombinant (His)

Catalog No. TMPY-06846

HSP90 alpha Protein, Mouse, Recombinant (His) is expressed in Baculovirus insect cells with His tag. The predicted molecular weight is 87.19 kDa and the accession number is NP_032328.2.

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Pack Size	Price	Availability	Quantity
100 μg	$700	7-10 days
1 mg	$4,560	7-10 days

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Biological Description

Biological Information	Testing in progress
Description	HSP90 alpha Protein, Mouse, Recombinant (His) is expressed in Baculovirus insect cells with His tag. The predicted molecular weight is 87.19 kDa and the accession number is NP_032328.2.
Species	Mouse
Expression System	Baculovirus Insect Cells
Tag	N-His
Accession Number	NP_032328.2
Synonyms	AL024080,Hspca,hsp4,Hsp86-1,heat shock protein 90kDa α (cytosolic), class A member 1,86kDa,Hsp90,AL024147,heat shock protein 90kDa alpha (cytosolic), class A member 1,89kDa,Hsp89,Hsp90 α
Construction	The Mouse HSP90AA1 (NP_032328.2) (Met1-Asp733) was expressed, with a polyhistidine tag at the N-terminus.
Protein Purity	≥ 95 % as determined by SDS-PAGE.
Molecular Weight	87.19 kDa (predicted)
Endotoxin	< 1.0 EU/μg of the protein as determined by the LAL method.
Formulation	Lyophilized from a solution filtered through a 0.22 μm filter, containing 20 mM PB, 300 mM NaCl, 10% glycerol, 1 mM TCEP, 0.5 mM PMSF, pH 7.0.Typically, a mixture containing 5% to 8% trehalose, mannitol, and 0.01% Tween 80 is incorporated as a protective agent before lyophilization.
Reconstitution	A Certificate of Analysis (CoA) containing reconstitution instructions is included with the products. Please refer to the CoA for detailed information.
Stability & Storage	It is recommended to store recombinant proteins at -20°C to -80°C for future use. Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.
Shipping	In general, Lyophilized powders are shipping with blue ice.
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.