This antibody is purified through a protein A column, followed by peptide affinity purification.
Immunogen
This HSPA1A/HSPA1B antibody is generated from a rabbit immunized with a KLH conjugated synthetic peptide between amino acids from the human region of human HSPA1A/HSPA1B.
hsp70-4 antibody, hspa1a antibody, Hsp70-3 antibody, Hsp70.3 antibody, Hsp72 antibody, hsp68 antibody, hsp70A1 antibody, HSP72 antibody, Hsp70-1 antibody, Hspa1 antibody, Hspa1b antibody, hsp70-1 antibody, hsp70-1a antibody, hsp70i antibody, hsp72 antibody, hspa1 antibody, hspa1b antibody, HSP70-1 antibody, HSP70-1A antibody, HSP70I antibody, HSPA1 antibody, HSPA1A antibody, HSPA1B antibody, HSP70-2 antibody, HSPA2 antibody, HSP70 antibody, hspA1A antibody, heat shock cognate 70-kd protein, tandem duplicate 3 antibody, heat shock 70 kDa protein 1 antibody, heat shock 70 kDa protein II antibody, heat shock protein 1A antibody, heat shock 70kD protein 1A antibody, heat shock protein family A (Hsp70) member 1A S homeolog antibody, heat shock protein family A (Hsp70) member 1A antibody, heat shock protein 70.2 antibody, heat shock 70kDa protein 1A antibody, heat shock 70 kDa protein 1B antibody, heat shock protein 70.1 antibody, hsp70.3 antibody, LOC100023597 antibody, LOC100554002 antibody, LOC100608888 antibody, Hspa1a antibody, hspa1a.S antibody, HSPA1A antibody, HSP70.2 antibody, LOC100354037 antibody, HSP70.1 antibody
Background
In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell.