Zebrafish Hspa5 Antibody / Grp78 / Bip, 100 ug

Heat shock 70 kDa protein 5 (Hspa5), also known as GRP78 (Glucose-Regulated Protein 78) or BiP (Binding Immunoglobulin Protein), is a highly conserved member of the HSP70 family of molecular chaperones. In zebrafish (Danio rerio), hspa5 encodes an endoplasmic reticulum (ER)-resident chaperone that plays a central role in protein quality control, particularly during ER stress and the unfolded protein response (UPR).

Hspa5 facilitates proper protein folding, prevents aggregation of misfolded proteins, and targets irreversibly misfolded proteins for degradation. It is also a key regulator of ER homeostasis, acting as a sensor for misfolded proteins and an upstream effector in activating UPR pathways, including PERK, ATF6, and IRE1.<

In zebrafish, hspa5 is expressed ubiquitously during early embryogenesis and is upregulated in response to physiological and environmental stressors such as hypoxia, oxidative stress, and toxin exposure. Its expression is especially prominent in secretory tissues and rapidly developing organs such as the liver, pancreas, and brain.

Zebrafish Hspa5 serves as a useful marker for ER stress and has been widely used in models of developmental defects, neurodegeneration, metabolic disease, and toxicology screening. Due to its evolutionary conservation and functional parallels to mammalian GRP78, zebrafish Hspa5 is a valuable target for studying cellular stress responses and disease mechanisms in vivo.