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

Chromosomal Location of Human Ortholog: 9q33.3

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

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

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