Anti-GRP78 / BiP

0.5mg/ml if reconstituted with 0.2ml sterile DI water. 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. Protein function: Probably plays a role in facilitating the assembly of multimeric protein complexes inside the endoplasmic reticulum. Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10, probably to facilitate the release of DNAJC10 from its substrate. [The UniProt Consortium]