BiP Antibodies

Target Information

BiP is an HSPA5-encoded member of the Hsp70 chaperone family that resides primarily in the endoplasmic reticulum (ER) lumen via an N-terminal signal peptide that mediates ER import and a C-terminal ER-retention motif (KDEL); under stress it can also relocalize to additional compartments, including the cell surface. Structurally, BiP is a ~78 kDa ATP-dependent chaperone organized into a conserved N-terminal nucleotide-binding (ATPase) domain and a C-terminal substrate-binding domain with a lid region, enabling cycles of ATP binding and hydrolysis to regulate client engagement and release. Functionally, BiP is a central ER proteostasis factor that binds nascent and misfolded polypeptides to promote folding and assembly, helps maintain ER integrity, and supports disposal of aberrant proteins through ER-associated degradation; it also acts as a key regulator of the unfolded protein response by binding the luminal domains of ER stress sensors (including IRE1, PERK, and ATF6) under basal conditions and being titrated away by accumulating unfolded proteins to permit signaling that restores ER homeostasis or, if stress is unresolved, contributes to downstream cell fate decisions such as autophagy and apoptosis.

Synonyms

BIP; BIP1; BIP2; BIP3; BiP-L; luminal binding protein; MJC20.12; MJC20_12; T26D3.10; T26D3_10