- Tel: 858.663.9055
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Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
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GRP78 Antibody recognizes the 78 kDa glucose-regulated protein, an endoplasmic reticulum molecular chaperone encoded by the HSPA5 gene. GRP78 is also widely known as BiP because it was originally identified as an immunoglobulin heavy chain binding protein. It belongs to the HSP70 family and contains an amino-terminal ATPase domain, a substrate-binding domain and a carboxy-terminal KDEL retention sequence that supports localization within the endoplasmic reticulum. GRP78 binds newly synthesized and incompletely folded proteins, prevents inappropriate aggregation and assists proteins in reaching conformations suitable for transport through the secretory pathway.
GRP78 is a central regulator of endoplasmic reticulum protein quality control and the unfolded protein response. Under normal conditions, GRP78 associates with the luminal domains of the stress sensors PERK, IRE1 and ATF6, helping maintain them in inactive states. When unfolded or misfolded proteins accumulate, GRP78 is recruited away from these sensors to assist with protein folding. The released sensors then activate signaling pathways that reduce new protein synthesis, increase production of chaperones and promote clearance of damaged proteins. A GRP78 Antibody can therefore help researchers monitor an important indicator and functional regulator of endoplasmic reticulum stress.
In addition to assisting protein folding, GRP78 contributes to endoplasmic reticulum-associated degradation by directing terminally misfolded proteins toward disposal pathways. It also participates in calcium homeostasis, secretory protein assembly and cellular adaptation to glucose deprivation, hypoxia, oxidative stress and other conditions that disrupt endoplasmic reticulum function. Persistent or severe stress can shift the unfolded protein response from a protective program toward apoptosis, making GRP78 relevant to studies of the balance between cell survival and death. Changes in GRP78 abundance are commonly examined alongside markers such as CHOP, ATF4, phosphorylated PERK, phosphorylated eIF2 alpha, spliced XBP1 and cleaved ATF6.
Elevated GRP78 expression has been reported in cancers and other disease models characterized by high secretory demand, nutrient limitation or proteotoxic stress. Increased chaperone capacity can help tumor cells survive unfavorable microenvironments and may influence treatment resistance. Although GRP78 is predominantly located in the endoplasmic reticulum, selected stressed or malignant cells have also been reported to display GRP78 at the cell surface, where it may participate in signaling interactions. Researchers may use GRP78 Antibody products in western blot, immunohistochemistry, immunofluorescence, flow cytometry or other validated applications to examine protein abundance and localization. NSJ Bioreagents supplies GRP78 Antibody options for studying protein folding, endoplasmic reticulum homeostasis, unfolded protein response signaling, cancer biology and cellular stress adaptation.
Explore our Cell Biology Antibodies page for additional reagents targeting protein folding, endoplasmic reticulum stress and cellular quality-control pathways.
Optimal dilution of the GRP78 Antibody / Endoplasmic Reticulum Chaperone Antibody should be determined by the researcher.
Amino acids ETMEKAVEEKIEWLESHQDADIEDFKAKKKELE of human GRP78/BiP were used as the immunogen for the GRP78 antibody.
After reconstitution, the GRP78 antibody can be stored for up to one month at 4oC. For long-term, aliquot and store at -20oC. Avoid repeated freezing and thawing.
BiP Antibody, HSPA5 Antibody, Glucose-Regulated Protein 78 Antibody, 78 kDa Glucose-Regulated Protein Antibody, Endoplasmic Reticulum Chaperone BiP Antibody, Immunoglobulin Heavy Chain Binding Protein Antibody, Heat Shock Protein Family A Member 5 Antibody
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