Anti-GRP78/BIP/HSPA5 Antibody Picoband®, Cy3 Conjugate

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.

Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks. Essential during mitosis and meiosis for proper segregation of daughter chromosomes. May play a role in regulating the period length of ARNTL/BMAL1 transcriptional oscillation (By similarity).

1. Hendershot, L. M., Valentine, V. A., Lee, A. S., Morris, S. W., Shapiro, D. N. Localization of the gene encoding human BiP/GRP78, the endoplasmic reticulum cognate of the HSP70 family, to chromosome 9q34. Genomics 20: 281-284, 1994. 2. Law, M. L., Seeliger, M. B., Lee, A. S., Kao, F. T. Genetic mapping of the structural gene coding for a glucose-regulated protein (GRP78) of 78k-dalton to the long arm of human chromosome 9. (Abstract) Cytogenet. Cell Genet. 37: 518-519, 1984. 3. Shen, J., Chen, X., Hendershot, L., Prywes, R. ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals. Dev. Cell 3: 99-111, 2002.

At -20℃ for one year from date of receipt. After reconstitution, at 4℃ for one month. It can also be aliquotted and stored frozen at -20℃ for six months. Avoid repeated freezing and thawing.