Grp78/Bip (HSPA5) Antibody – Rabbit Polyclonal

GRP78: a member of the HSP family of molecular chaperones required for endoplasmic reticulum integrity and stress-induced autophagy. Plays a central role in regulating the unfolded protein response (UPR), and is an obligatory component of autophagy in mammalian cells. May play an important role in cellular adaptation and oncogenic survival. One of the client proteins of GRP78 is protein double-stranded RNA-activated protein-like endoplasmic reticulum kinase (PERK). Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER.

Protein type: Heat shock protein; Chaperone

Cellular Component: cell surface; endoplasmic reticulum; endoplasmic reticulum lumen; endoplasmic reticulum membrane; ER-Golgi intermediate compartment; focal adhesion; integral to endoplasmic reticulum membrane; melanosome; membrane; midbody; mitochondrion; myelin sheath; nucleus; plasma membrane; signalosome; smooth endoplasmic reticulum

Molecular Function: ATP binding; ATPase activity; enzyme binding; glycoprotein binding; misfolded protein binding; protein binding; protein domain specific binding; ribosome binding; ubiquitin protein ligase binding; unfolded protein binding

Biological Process: cellular response to glucose starvation; cerebellar Purkinje cell layer development; cerebellum structural organization; ER overload response; negative regulation of apoptosis; negative regulation of transforming growth factor beta receptor signaling pathway; positive regulation of cell migration; positive regulation of protein ubiquitination; proteolysis involved in cellular protein catabolic process; substantia nigra development; unfolded protein response, activation of signaling protein activity