GRP78 / BIP Mouse Monoclonal Antibody [A5-C9-G6] (M1701-1)

UNIPROT #

P11021

PROTEIN NAME

GRP78 / BIP

SYNONYMS

78 kDa glucose regulated protein antibody;78 kDa glucose-regulated protein antibody;AL022860 antibody;AU019543 antibody;BIP antibody;D2Wsu141e antibody;D2Wsu17e antibody;Endoplasmic reticulum lumenal Ca(2+)-binding protein grp78 antibody;Endoplasmic reticulum lumenal Ca2+ binding protein grp78 antibody;Epididymis secretory sperm binding protein Li 89n antibody;FLJ26106 antibody;Glucose Regulated Protein 78kDa antibody;GRP 78 antibody;GRP-78 antibody;GRP78 antibody;GRP78_HUMAN antibody;Heat shock 70 kDa protein 5 antibody;Heat Shock 70kDa Protein 5 antibody;Heat shock protein family A (Hsp70) member 5 antibody;HEL S 89n antibody;Hsce70 antibody;HSPA 5 antibody;HSPA5 antibody;Immunoglobulin Heavy Chain Binding Protein antibody;Immunoglobulin heavy chain-binding protein antibody;mBiP antibody;MIF2 antibody;Sez7 antibody

SEQUENCE SIMILARITIES

Belongs to the heat shock protein 70 family.

POST-TRANSLATIONAL MODIFICATION

AMPylated by FICD. In unstressed cells, AMPylation at Thr-518 by FICD inactivates the chaperome activity: AMPylated form is locked in a relatively inert state and only weakly stimulated by J domain-containing proteins (By similarity). In response to endoplasmic reticulum stress, de-AMPylation by the same protein, FICD, restores the chaperone activity (By similarity).

SUBCELLULAR LOCATION

Endoplasmic reticulum lumen. Melanosome. Cytoplasm.

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.