HSC70/HSP73 Recombinant Protein

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: Chaperone; Heat shock protein

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

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

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