Abcam, ab78432, Recombinant human GRP78 BiP protein (Active)

Size: 50µg / 100µg
Recombinant human GRP78 BiP protein (Active) is a Human Full Length protein in the 1 to 654 aa range with >90% purity and suitable for SDS-PAGE, ELISA, western blot, Functional studies and more.The predicted molecular weight of ab78432 protein is 78 kDa.
Key facts
Purity:>90% SDS-PAGE,
Expression system:Escherichia coli,
Tags:His tag N-Terminus,
Applications:ELISA, SDS-PAGE, WB, FuncSSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:Yes,
Biological activity:ATPase active,
Accession:P11021,
Animal free:No,
Carrier free:No,
Species:Human,
Storage buffer:pH: 7.5Constituents: 10% Glycerol (glycerin, glycerine), 0.88% Sodium chloride, 0.79% Tris HCl

Product details:
Ensure the validity of your result using our bioactive recombinant human GRP78/BiP ab78432 as positive control in SDS-PAGE and western blot.
Analyze your GRP78/BiP ELISA data using the ab78432 protein to generate and plot a standard curve.
Check out our protein gel staining guide for SDS-PAGE
Check out our western blot protocol for more information
Check out our ELISA protocol for more information

Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage conditions--20°C, Appropriate long-term storage conditions--20°C, Storage information-Stable for 12 months at -20°C

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
GRP78 also known as BiP or HSPA5 is a protein that plays an important role in protein folding and assembly within the endoplasmic reticulum (ER). It weighs approximately 78 kDa hence the name GRP78. This chaperone protein binds to hydrophobic regions of nascent polypeptides to prevent aggregation and misfolding. GRP78 is expressed in high levels in the ER of cells where it monitors cellular stress and aids in maintaining ER homeostasis.
Biological function summary
GRP78/BiP is important in the unfolded protein response (UPR) a cellular stress response related to the ER. It is part of a complex that manages protein load inside the ER by regulating the fold of nascent proteins and interacting with other ER stress sensors like IRE1 PERK and ATF6. This function is essential for maintaining proper protein conformation in the ER especially during physiological stress ensuring that only correctly folded proteins proceed to the Golgi apparatus.
Pathways
GRP78/BiP significantly affects the UPR and apoptosis pathways. By controlling protein folding and quality in the ER GRP78 helps prevent cell death under stress conditions. It works closely with other proteins like ATF6 which activates stress response genes. In normal conditions GRP78 keeps stress transducers inactivated but during stress it dissociates allowing UPR signaling to occur.
GRP78/BiP has been implicated in cancer and neurodegenerative diseases. Overexpression of GRP78 is associated with tumor proliferation and poor prognosis in various cancers as cancer cells heavily rely on its protein-folding capacity to survive. Additionally in neurodegenerative diseases misfolded proteins can accumulate leading GRP78 to attempt counteracting these toxic aggregations highlighting its connection with proteins like tau and amyloid-beta in diseases such as Alzheimer's.