Rabbit GRP78 (Bip) Polyclonal Antibody | anti-HSPA5 antibody
GRP78 (Bip) Antibody: ATTO 488
Western Blot (WB)
(Western blot analysis of Human Glucose deprived glia cell lysates showing detection of GRP78 protein using Rabbit Anti-GRP78 Polyclonal Antibody (SPC-180). Primary Antibody: Rabbit Anti-GRP78 Polyclonal Antibody (SPC-180) at 1:1000.)
Scientific Background: GRP78 is a ubiquitously expressed, 78-kDa glucose regulated protein, and is commonly referred to as an immunoglobin chain binding protein (BiP). The BiP proteins are categorized as stress response proteins because they play an important role in the proper folding and assembly of nascent protein and in the scavenging of misfolded proteins in the endoplasmic reticulum lumen. Translation of BiP is directed by an internal ribosomal entry site (IRES) in the 5' non-translated region of the BiP mRNA. BiP IRES activity increases when cells are heat stressed (1). GRP78 is also critical for maintenance of cell homeostasis and the prevention of apoptosis (2). Luo et al. have provided findings that suggest GRP78 is essential for embryonic cell growth and pluripotent cell survival (3). In terms of diseases, GRP78 has been shown to be a reliable biomarker of hypoglycemia, to serve a neuroprotective function in neurons exposed to glutamate and oxidative stress (4), and its protein levels are reduced in the brains of Alzheimer's patients (5). Also, the induction of the GRP78 protein that results in severe glucose and oxygen deprivation could possible lead to drug resistance to anti-tumor drugs (6, 7).
NCBI and Uniprot Product Information
NCBI Description
The protein encoded by this gene is a member of the heat shock protein 70 (HSP70) family. It is localized in the lumen of the endoplasmic reticulum (ER), and is involved in the folding and assembly of proteins in the ER. As this protein interacts with many ER proteins, it may play a key role in monitoring protein transport through the cell.[provided by RefSeq, Sep 2010]
Uniprot Description
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; focal adhesion; smooth endoplasmic reticulum; cell surface; 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; chaperone binding; ubiquitin protein ligase binding; ATPase activity; unfolded protein binding; ribosome binding; calcium ion binding; misfolded protein 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; substantia nigra development; cellular protein metabolic process; platelet degranulation; unfolded protein response, activation of signaling protein activity; positive regulation of protein ubiquitination; blood coagulation; negative regulation of transforming growth factor beta receptor signaling pathway; ER overload response; negative regulation of apoptosis; positive regulation of cell migration
