Protein Tag: N-Gst
Uniprot: P0DMV8-1
Accession: P0DMV8-1
Background: 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. HSP are abundant and conserved proteins present in all cells. Upon temperature shock or other stress stimuli, HSP is synthesized intracellularly, which may protect cells from protein denaturation or 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 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. All cellular functions of Hsp70 chaperones use the same mechanism of ATP-driven polypeptide binding and release.
Bio Acitivity: Not validated for activity
Sequence: Ile291-Asp641
Purity: > 90% as determined by reducing SDS-PAGE.
Formulation: Lyophilized from a 0.2 μm filtered solution in PBS with 5% Trehalose and 5% Mannitol.
Reconstitution: It is recommended that sterile water be added to the vial to prepare a stock solution of 0.5 mg/mL. Concentration is measured by UV-Vis.
Endotoxin: < 10 EU/mg of the protein as determined by the LAL method.
Calculated MW: 64.5 kDa
Observed MW: 65 kDa
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