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HSPA1A is a member of the Hsp70 protein family. The 70 kilodalton heat shock proteins (Hsp70s) are a family of ubiquitously expressed heat shock proteins. The Hsp70 family stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. Extracellularly, HSP can serve a cytokine function to initiate both innate and adaptive immunity through activation of APC. HSP serves also a chaperone function and facilitates the presentation of antigen peptide to T cells. Molecular chaperones of the Hsp70 family have diverse functions in cells. They assist the folding of newly synthesized and stress-denatured proteins, as well as the import of proteins into organelles, and the dissociation of aggregated proteins. The well-conserved Hsp70 chaperones are ATP dependent: binding and hydrolysis of ATP regulate their interactions with unfolded polypeptide substrates, and ATPase cycling is necessary for their function.
The recombinant mouse HSP70 consists of 651 amino acids and predicts a molecular mass of 71.5 kDa. It migrates as an approximately 64.3 kDa band in SDS-PAGE under reducing conditions.
A DNA sequence encoding the mouse HSP70 (NP_034609.2) (Ala2-Asp641) was expressed with a polyhistidine tag at the N-terminus.
Lyophilized from sterile PBS, pH 7.4.
| Solubility (25°C) | Reconstitute the lyophilized powder in ddH2O or PBS at 100 μg/mL |
| Storage | Stable for up to twelve months from date of receipt at -20℃ to -80℃ |
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