Recombinant Human HSPA1A protein

>90% as determined by SDS-PAGE

Please contact with the lab for this information.

A DNA sequence encoding the human HSPA1A (Met1-Asp641) was fused with His tag

P0DMV8

E.coli

Homo sapiens (Human)

66.85 kDa

Supplied as solution form in PBS pH 7.5 or lyophilized from PBS pH 7.5.

In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise.

Use a manual defrost freezer and avoid repeated freeze thaw cycles.
Store at 2 to 8 °C for one week .
Store at -20 to -80 °C for twelve months from the date of receipt.

Reconstitute in sterile water for a stock solution.A copy of datasheet will be provided with the products, please refer to it for details.

HSPA1A is a member of the Hsp7 protein family. The 7 kilodalton heat shock proteins (Hsp7s) are a family of ubiquitously expressed heat shock proteins. HSP are abundant and conserved proteins present in all cells. Upon temperature shock or other stress stimuli, HSP are synthesized intracellularly, which may protect cells from protein denaturation or from death. 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 presentation of antigen peptide to T cells. Molecular chaperones of the Hsp7 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 Hsp7 chaperones are ATP dependent: binding and hydrolysis of ATP regulates their interactions with unfolded polypeptide substrates, and ATPase cycling is necessary for their function. All cellular functions of Hsp7 chaperones use the same mechanism of ATP-driven polypeptide binding and release.

Heat shock 70 kDa protein 1A,Heat shock 70 kDa protein 1,HSP70-1,HSP70.1.

For research use only .