Anti-GRP78 BiP/HSPA5 Antibody Picoband®

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.

78 kDa glucose-regulated protein; GRP-78; Endoplasmic reticulum lumenal Ca (2+) -binding protein grp78; Heat shock 70 kDa protein 5; Immunoglobulin heavy chain-binding protein; BiP; HSPA5; GRP78

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. .

Store at -20°C for one year from date of receipt. After reconstitution, at 4°C for one month. It can also be aliquotted and stored frozen at -20°C for six months. Avoid repeated freeze-thaw cycles.

Immunocytochemistry , 0.5-1μg/ml, Human, Mouse, Rat<br>Immunohistochemistry (Frozen Section), 0.5-1μg/ml, Rat, Human, Mouse<br>Immunohistochemistry (Paraffin-embedded Section), 0.5-1μg/ml, Human, Rat, Mouse, By Heat<br>Western blot, 0.1-0.5μg/ml, Human, Rat, Mouse<br>