KLH conjugated synthetic peptide derived from human GRP78
Conjugation:
Unconjugated
Alternative Names:
78 kDa glucose-regulated protein,binding-immunoglobulin protein,BIP,endoplasmic reticulum chaperone BiP,endoplasmic reticulum lumenal Ca(2+)-binding protein grp78,epididymis secretory sperm binding protein Li 89n,glucose-regulated protein, 78kDa,GRP78,heat shock 70kDa protein 5 (glucose-regulated protein, 78kDa),heat shock protein 70 family protein 5,heat shock protein family A member 5,HEL-S-89n,HSP70 family protein 5,immunoglobulin heavy chain-binding protein.
Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (PubMed:2294010, PubMed:23769672, PubMed:23990668, PubMed:28332555). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR) (PubMed:1550958, PubMed:19538957). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to disrupt the dimerization of ERN1/IRE1, thereby inactivating ERN1/IRE1 (By similarity). Accumulation of misfolded protein in the endoplasmic reticulum causes release of HSPA5/BiP from ERN1/IRE1, allowing homodimerization and subsequent activation of ERN1/IRE1 (By similarity).
