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.

Boster Bio Anti-GRP78 BiP/HSPA5 Antibody catalog # PA1815. Tested in IHC, ICC, WB applications. This antibody reacts with Human, Mouse, Rat. The brand Picoband indicates this is a premium antibody that guarantees superior quality, high affinity, and strong signals with minimal background in Western blot applications. Only our best-performing antibodies are designated as Picoband, ensuring unmatched performance.

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

HSPA5

3309

P11021

Rat, Mouse, Human

No cross-reactivity with other proteins

A synthetic peptide corresponding to a sequence at the C-terminus of human GRP78 BiP, identical to the related mouse and rat sequences.

IHC, ICC, WB

Tags & Cell Markers

Immunogen affinity purified.

Adding 0.2 ml of distilled water will yield a concentration of 500 μg/ml.

Lyophilized

Add 0.2ml of distilled water will yield a concentration of 500ug/ml.

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. .

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.

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.

https://www.bosterbio.com/msds?sku=PA1815

72333 MW

70 kDa

No cross reactivity with other proteins.

78 kDa glucose-regulated protein

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

Belongs to the heat shock protein 70 family.

78 kDa glucose-regulated protein

Rabbit IgG

Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg Thimerosal, 0.05mg NaN3.