Anti-GRP78 / BIP Antibody [A5-C9-G6]

HUABIO

Anti-GRP78 / BIP Antibody [A5-C9-G6]

7

Western Blot

WB,IF-Cell,IHC-P,FC

Research Use Only

Monoclonal

A5-C9-G6

2 mg/ml

Unconjugated

HSPA5

heat shock protein family A (Hsp70) member 5

BIP, GRP78, HEL-S-89n, endoplasmic reticulum chaperone BiP, 78 kDa glucose-regulated protein, HSP70 family protein 5, binding-immunoglobulin protein, endoplasmic reticulum lumenal Ca(2+)-binding protein grp78, epididymis secretory sperm binding protein Li 89n, glucose-regulated protein, 78kDa, heat shock 70kDa protein 5 (glucose-regulated protein, 78kDa), heat shock protein 70 family protein 5, heat shock protein family A member 5, immunoglobulin heavy chain-binding protein

Mouse

IgG1

Endoplasmic reticulum chaperone BiP

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.

Human, Mouse

Human,Mouse

-20°C,2°C to 8°C

41116161