The HSP 70 family comprises four highly conserved proteins, HSP 70, HSC 70, GRP 75 and GRP 78, which serve a variety of roles. They act as molecular chaperones facilitating the assembly of multi-protein complexes, participate in the translocation of polypeptides across cell membranes and to the nucleus, and aid in the proper folding of nascent polypeptide chains. HSC 70, GRP 75 and GRP 78 are constitutively expressed in primate cells. HSP 70 expression is strongly induced in response to heat stress. HSP 70 and HSC 70, which are found in both the cytosol and nucleus of mammalian cells, play key roles in the cytosolic endoplasmic reticulum and mitochondrial import machinery. They are involved in chaperoning nascent polypeptide chains and in protecting cells against the accumulation of improperly folded proteins.
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
