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GRP78 (human, recombinant)

Item No. 22730

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Synonyms
  • BiP
  • Glucose-Regulated Protein 78
  • HspA5
Purity
≥85% estimated by SDS-PAGE
Source
Active N-terminal His-tagged human GRP78 protein expressed in E. coli
Amino Acids
2-654 (full length)
MW
74.6 kDa
Formulation (Request formulation change)
50 mM HEPES, pH 8.0, 150 mM sodium chloride, 1 mM DTT, and 10% glycerol
UniProt Accession №
P11021
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    50 µg

    $267

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    Product Description

    Glucose-regulated protein 78 kDa (GRP78), also known as heat shock 70 kDa protein 5 (HspA5) and immunoglobulin heavy chain-binding protein (BiP), is a glucose-regulated protein that is constitutively expressed in the lumen of the endoplasmic reticulum (ER).1,2,3 It is composed of two functional domains, an N-terminal nucleotide-binding domain that contains an ATP catalytic site and a C-terminal substrate binding domain that binds hydrophobic polypeptides.4 GRP78 functions as a molecular chaperone, assisting in the translocation of polypeptides from the cytosol into the ER, folding of nascent polypeptides, as well as refolding and preventing aggregation of misfolded proteins. It also plays a role in the ER-assisted degradation (ERAD) and unfolded protein response (UPR) pathways.5,6 GRP78 chaperone activity is driven by an ATPase cycle that is regulated by ER-localized DnaJ-like protein co-factors and nuclear exchange factors.7,8 Expression of GRP78 is upregulated in response to ER stress caused by viral and bacterial infections as well as various cancers.9 ER stress can also promote extracellular secretion of GRP78 leading to its anti-inflammatory functions in immunity.10

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Vogel, J.P., Misra, L.M., and Rose, M.D. Loss of BiP/GRP78 function blocks translocation of secretory proteins in yeast. J. Cell. Biol. 110(6), 1885-1895 (1990).

    2. Simons, J.F., Ferro-Novick, S., Rose, M.D., et al. BiP/Kar2p serves as a molecular chaperone during carboxypeptidase Y folding in yeast. J. Cell. Biol. 130(1), 41-49 (1995).

    3. Mayer, M.P., and Bukau, B. Hsp70 chaperones: Cellular functions and molecular mechanism. Cell Mol. Life Sci. 62(6), 670-684 (2005).

    4. Yang, J., Nune, M., Zong, Y., et al. Close and allosteric opening of the polypeptide-binding site in a human Hsp70 chaperone BiP. Structure 23(12), 2191-2203 (2015).

    5. Plemper, R.K., Böhmler, S., Bordallo, J., et al. Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation. Nature 388(6645), 891-895 (1997).

    6. Okamura, K., Kimata, Y., Higashio, H., et al. Dissociation of Kar2p/BiP from an ER sensory molecule, Ire1p, triggers the unfolded protein response in yeast. Biochem. Biophys. Res. Commun. 279(2), 445-450 (2000).

    7. Szabo, A., Langer, T., Schröder, H., et al. The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE. Proc. Natl. Acad. Sci. USA 91(22), 10345-10349 (1994).

    8. Behnke, J., Feige, M.J., and Hendershot, L.M. BiP and its nucleotide exchange factors Grp170 and Sil1: Mechanisms of action and biological functions. J. Mol. Biol. 42(7), 1589-1608 (2015).

    9. Booth, L., Roberts, J.L., Cash, D.R., et al. GRP78/BiP/HSPA5/Dna K is a universal therapeutic target for human disease. J. Cell. Physiol. 230(7), 1661-1676 (2015).

    10. Shields, A.M., Panayi, G.S., and Corrigall, V.M. Resolution-associated molecular patterns (RAMP): RAMParts defending immunological homeostasis. Clin. Exp. Immunol. 165(3), 292-300 (2011).