Mouse Glucose Regulated Protein 78 (GRP78) ELISA Kit-Sandwich

Endoplasmic reticulum chaperone BiP, also known as 78 kDa glucose-regulated protein (GRP78), is a critical chaperone in the endoplasmic reticulum (ER) lumen, essential for protein folding and quality control. It facilitates the proper folding of proteins and aids in the degradation of misfolded proteins through its interaction with DNAJC10/ERdj5, likely by promoting the release of DNAJC10/ERdj5 from its substrate. In mice, Hspa5 (also referred to as HSP70 or BiP) has diverse functions, including roles in the ER stress response, apoptosis, neurodegenerative diseases, cancer, and embryonic development. In Alzheimer's disease (AD) models, Hspa5 operates through the ferroptosis pathway, and its inhibition has been shown to alleviate ferroptosis. In Parkinson's disease (PD) models, overexpression of Hspa5 can delay disease progression, potentially by indirectly regulating protein aggregation. These findings underscore the multifaceted role of Hspa5 in cellular stress responses and neurodegenerative disease mechanisms.