Species | Human | ||||
Protein Construction |
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Purity | > 95% as determined by BisTris PAGE | ||||
Endotoxin Level | Less than 1EU per μg by the LAL method. | ||||
Expression System | E.coli | ||||
Theoretical Molecular Weight | 72.2 kDa | ||||
Apparent Molecular Weight | The protein has a predicted MW of 72.2 kDa same as Bis-Tris PAGE result. | ||||
Formulation | Supplied as 0.22μm filtered solution in 25mM Tris, 100mM Glycine, 10% Glycerol (pH 7.4). | ||||
Concentration | Verified by one or more methods from 0.64mg/ml A280/Bioactivity/BCA/Bradford. | ||||
Storage & Stability | This product remains stable for 6 months at -80°C or below. Avoid repeated freeze-thaw cycles. |
Target 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. |
Synonyms | HSP70-1; HSPA1A; HSP72 ; HSPA1; HSX70 |
For research use only. Not intended for human or animal clinical trials, therapeutic or diagnostic use.