HSPA5 (heat shock 70kDa protein 5), also known as glucose-regulated protein, 78kD (GRP78) or BiP, is a member of the heat-shock protein-70 (HSP70) family and is involved in the folding and assembly of proteins in the endoplasmic reticulum. BiP is also an essential component of the translocation machinery, as well as playing a role in retrograde transport across the ER membrane of aberrant proteins destined for degradation by the proteasome. The HSPA5 gene is mapped on 9q33.3. Shen et al. (2002) concluded that HSPA5 retains ATF6 in the ER by inhibiting its Golgi localization signals and that dissociation of HSPA5 during ER stress allows ATF6 to be transported to the Golgi. The findings of Shen et al. (2002) demonstrated that HSPA5 is a key element in sensing the folding capacity within the ER.

Optimal dilution of the GRP78 antibody should be determined by the researcher.

Amino acids ETMEKAVEEKIEWLESHQDADIEDFKAKKKELE of human GRP78/BiP were used as the immunogen for the GRP78 antibody.

After reconstitution, the GRP78 antibody can be stored for up to one month at 4oC. For long-term, aliquot and store at -20oC. Avoid repeated freezing and thawing.