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Citrullinated GRP78 (human, recombinant)

Item No. 25107

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Synonyms
  • BiP
  • Endoplasmic Reticulum Lumenal Ca2+-Binding Protein GRP78
  • Glucose-Related Protein 78
  • Heat Shock Protein 5 (70 kDa)
  • Hsp5 (70 kDa)
  • Immunoglobulin Heavy Chain-Binding Protein
Purity
≥90% estimated by SDS-PAGE
Source
N-Terminal histidine-tagged human GRP78 purified from E. coli, citrullinated by PAD2
Amino Acids
2-654
MW
74.6 kDa
Storage Buffer
PBS, pH 7.4, with 10% glycerol
UniProt Accession №
P11021
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    100 µg

    $600

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    Product Description

    Glucose-regulated protein 78 kDa (GRP78) is a molecular chaperone that is ubiquitously expressed in the endoplasmic reticulum of mammalian cells.1,2,3 GRP78 can be citrullinated at its 27 arginine residues by protein deiminases (PADs).4 The accumulation of citrullinated proteins in vivo leads to the production of anti-citrullinated protein antibodies (ACPAs) which perpetuate the inflammatory process.5 In vitro, ACPAs bind to citrullinated GRP78 expressed on the cell surface of peripheral blood mononuclear cells PMBCs and U937 cells leading to the production of TNF-α.6,7 In a mouse model of collagen-induced arthritis (CIA), anti-citrullinated GRP78 antibodies are found in the serum.4 Pre-immunization with citrullinated GRP78 prior to CIA induction shortens the time to joint inflammation and increases arthritis scores compared with non-citrullinated GRP78-immunized and non-immunized control mice. In autoimmune diseases such as rheumatoid arthritis, patient-derived serum contains higher levels of anti-citrullinated GRP78 antibodies than serum derived from patients with systemic lupus erythematosus and healthy controls.4

    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. Shoda, H., Fujio, K., Shibuya, M., et al. Detection of autoantibodies to citrullinated BiP in rheumatoid arthritis patients and pro-inflammatory role of citrullinated BiP in collagen-induced arthritis. Arthritis Res. Ther. 13(6), R191 (2011).

    5. Kuhn, K.A., Kulik, L., Tomooka, B., et al. Antibodies against citrullinated proteins enhance tissue injury in experimental autoimmune arthritis. J. Clin. Invest. 116(4), 961-973 (2006).

    6. Lu, M.C., Lai, N.S., Yu, H.C., et al. Anti-citrullinated protein antibodies bind surface-expressed citrullinated Grp78 on monocyte/macrophages and stimulate tumor necrosis factor α production. Arthritis Rheum. 62(5), 1213-1223 (2010).

    7. Lu, M.C., Lai, N.S., Yin, W.Y., et al. Anti-citrullinated protein antibodies activated ERK1/2 and JNK mitogen-activated protein kinases via binding to surface-expressed citrullinated GRP78 on mononuclear cells. J. Clin. Immunol. 33(3), 558-566 (2013).