HSP70/HSPA1A Protein, Human, Recombinant (E110D, His)

Catalog No. TMPY-02443U

HSP70/HSPA1A Protein, Human, Recombinant (E110D, His) is expressed in E. coli. The accession number is P0DMV8-1.

HSP70/HSPA1A Protein, Human, Recombinant (E110D, His)

Catalog No. TMPY-02443U

HSP70/HSPA1A Protein, Human, Recombinant (E110D, His) is expressed in E. coli. The accession number is P0DMV8-1.

Pack Size	Price	Availability	Quantity

Bulk & Custom

All TargetMol products are for research purposes only and cannot be used for human consumption. We do not provide products or services to individuals. Please comply with the intended use and do not use TargetMol products for any other purpose.

Questions

Resource Download

User Guide of Recombinant Proteins

Product Information

Biological Activity	Activity has not been tested. It is theoretically active, but we cannot guarantee it.
Description	HSP70/HSPA1A Protein, Human, Recombinant (E110D, His) is expressed in E. coli. The accession number is P0DMV8-1.
Species	Human
Expression System	E. coli
Tag	N-His
Accession Number	P0DMV8-1
Synonyms	HSPA1,HSP72,HSP70I,HSP70-1A,HSP70-1,HEL-S-103,heat shock 70kDa protein 1A
Construction	Ala2-Asp641(Glu110Asp)
Protein Purity	> 95% as determined by Tris-Bis PAGE; > 95% as determined by HPLC
Molecular Weight	72.2 kDa (Predicted and reducing conditions)
Endotoxin	< 1.0 EU/μg of the protein as determined by the LAL method.
Formulation	Supplied as 0.22 μm filtered solution in 25mM Tris, 100mM Glycine, 10% Glycerol (pH 7.4).
Stability & Storage	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. Solutions are shipping with dry ice.
Research Background	Chaperones of the 70 kDa heat shock protein (Hsp70) superfamily are key components of the cellular proteostasis system. Together with its co-chaperones, Hsp70 forms proteostasis subsystems that antagonize protein damage during physiological and stress conditions.