Glucose Regulated Protein 78

E2097Mo

Sandwich

48T,96T

0.121ng/mL

0.2-60ng/mL

Serum, plasma, cell culture supernates

Mouse

2-8ºC

1h 30m

Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (PubMed: 12411443, PubMed: 12$475.00|$350.00965). 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 (PubMed: 12411443). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR) (By similarity). 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). Plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). May function as an allosteric modulator for SEC61 Channel-forming translocon complex, likely cooperating with SEC62 to enable the productive insertion of these precursors into SEC61 Channel. Appears to specifically regulate translocation of precursors having inhibitory residues in their mature region that weaken Channel gating. May also play a role in apoptosis and cell proliferation (By similarity).

72,422

14828

78 kDa glucose-regulated protein;Binding-immunoglobulin protein;BiP;Endoplasmic reticulum chaperone BiP;GRP-78;Heat shock protein 70 family protein 5;Heat shock protein family A member 5;HSP70 family protein 5;HSPA 5;HSPA5;Immunoglobulin heavy chain-binding protein

HSPA5

Tags & Cell Markers

HSPA5