Grp75 Mouse Monoclonal Antibody [A6-A5-B1] (M1603-1)

UNIPROT #

P38646

PROTEIN NAME

Grp75

SYNONYMS

75 kDa glucose regulated protein antibody;75 kDa glucose-regulated protein antibody;CSA antibody;Glucose Regulated Protein antibody;Grp 75 antibody;GRP-75 antibody;GRP75 antibody;GRP75_HUMAN antibody;Heat shock 70 kDa protein 9 antibody;Heat shock 70kD protein 9 antibody;heat shock 70kDa protein 9 antibody;Heat shock 70kDa protein 9B antibody;Heat shock protein 74 kDa A antibody;Heat shock protein A antibody;Heat shock protein cognate 74 antibody;Hsc74 antibody;Hsp74 antibody;Hsp74a antibody;HSPA9 antibody;Hspa9a antibody;HSPA9B antibody;MGC4500 antibody;mitochondrial antibody;Mortalin 2 antibody;Mortalin antibody;Mortalin perinuclear antibody;Mortalin2 antibody;MOT 2 antibody;MOT antibody;MOT2 antibody;Mthsp70 antibody;p66 mortalin antibody;P66 MOT antibody;PBP74 antibody;Peptide binding protein 74 antibody;Peptide-binding protein 74 antibody;Stress 70 protein mitochondrial antibody;Stress 70 protein mitochondrial precursor antibody;Stress-70 protein antibody

SEQUENCE SIMILARITIES

Belongs to the heat shock protein 70 family.

SUBCELLULAR LOCATION

Mitochondrion, Nucleus

FUNCTION

The HSP 70 family is composed of four highly conserved proteins: HSP 70, HSC 70, GRP 75 and GRP 78. These proteins 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. All members of the family, except HSP 70, are constitutively expressed in primate cells. HSP 70 expression is strongly induced in response to heat stress. HSP 70 and HSC 70 play key roles in the cytosolic endoplasmic reticulum and mitochondrial import machinery and are found in both the cytosol and nucleus of mammalian cells. Both HSP 70 and HSC 70 are involved in the chaperoning of nascent polypeptide chains and in protecting cells against the accumulation of improperly folded proteins. GRP 78 is localized in the endoplasmic reticulum, where it receives imported secretory proteins and is involved in the folding and translocation of nascent peptide chains. GRP 75 expression is restricted to the mitochondrial matrix and aids in the translocation and folding of nascent polypeptide chains of both nuclear and mitochondrial origin. GRP 75 and GRP 78 are unresponsive to heat stress and are induced by glucose deprivation. It has been postulated that members of the HSP 70 family act as force-generating motors, relying on the hydrolysis of ATP for their activity