The 78 kDa glucose regulated protein/BiP (GRP78) belongs to the family of ~70 kDa heat shock proteins (HSP 70). GRP78 is a resident protein of the endoplasmic reticulum (ER) and may associate transiently with a variety of newly synthesized secretory and membrane proteins or permanently with mutant or defective proteins that are incorrectly folded, thus preventing their export from the ER lumen. GRP78 is a highly conserved protein that is essential for cell viability. The highly conserved sequence Lys-Asp-Glu-Leu (KDEL) is present at the C terminus of GRP78 and other resident ER proteins including glucose regulated protein 94 (GRP 94) and protein disulfide isomerase (PDI). The presence of carboxy terminal KDEL appears to be necessary for retention and appears to be sufficient to reduce the secretion of proteins from the ER. This retention is reported to be mediated by a KDEL receptor.

BIP; HSPA5; GRP-78; glucose regulated protein 78; 78 kDa glucose regulated protein; BIP; Endoplasmic reticulum lumenal Ca2+ binding protein grp78; FLJ26106; Glucose Regulated Protein 78kDa; GRP 78; Heat Shock 70kDa Protein 5; HSPA 5; HSPA-5; Immunoglobulin Heavy Chain Binding Protein; MIF2; GRP78_HUMAN.

Human,Mouse,Rat

WB

WB 1:500-2000

78kD

3309

P11021

https://www.uniprot.org/uniprotkb/P11021

Endoplasmic reticulum lumen. Melanosome. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

Recombinant human HSPA5 between 420-654 amino acids.

Mouse

Monoclonal

IgG1,k

affinity purified by Protein G

Liquid

0.01M TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.

Shipped at 4℃. Store at -20℃ for one year. Avoid repeated freeze/thaw cycles.