Technical Data
Glucose Regulated Protein 78 (Grp78, BiP)
Grp78, a 78kD glucose-regulated protein, also known as BiP or immunoglobulin heavy chain binding protein, is a stress-response protein which is induced by agents or conditions that adversely affect endoplasmic reticulum (ER) function (2). This protein is essential for the proper glycosylation, folding and assembly of many membrane bound and secreted proteins (3). Grp78 is critical for maintenance of cell homeostasis and the prevention of apoptosis (4). Grp78 protein levels have been shown to be a reliable biomarker of hypoglycermia (5) as well as serving a neuroprotective function in neurons exposed to glutamate and oxidative stress (2). Grp78 levels are reduced in the brains of Alzheimer’s Disease patients and decreased expression of Grp78 is found associated with missense mutations in the human presenilin-1 (PS1) gene (6). The induction of the Grp78 protein has been associated with the development of drug-resistance to anti-tumor drugs (7).

Suitable for use in Western Blot. Other applications have not been tested.

Recommended Dilution:
Western Blot (ECL): 1:1000
Optimal dilutions to be determined by the researcher.

Positive Controls:
G3057-22: Recombinant Hamster Grp78 Protein.

Storage and Stability:
May be stored at 4°C for short-term only. For long-term storage, aliquot and store at -20°C. Aliquots are stable for at least 12 months at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
PabIgGAffinity Purified
50ug4°C (-20°C Glycerol)Blue IceRatRabbit
Synthetic peptide corresponding to aa 645-654 of rat Grp78 (KLH).
Purified by Protein A affinity chromatography.
Supplied as a liquid in PBS, 0.09% sodium azide, 50% glycerol
Recognizes rat Grp78 at ~78kD Species Crossreactivity: mouse, bovine, hamster, monkey, rabbit, Xenopus, and fungus (Cryphonectria parasitica).
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Ting, J. and Lee, A.S. (1988) DNA 7: 275-286. 2. Yu, Z., et al., (1999) Exp. Neurol. 155: 302-314. 3. Mote, P.L., et al., (1998) Mech. Ageing Dev. 104: 149-158. 4. Yang, G.H., et al., (2000) Toxicol. Appl. Pharmacol. 162: 207-217. 5. Barnes, J.A., et al., (1999) Cell Stress & Chap. 4: 250-258. 6. Katayama, T., et al., (1999) Nat. Cell Biol. 1: 479-485. 7. Koomagi. R., et al., (1999) Anticancer Res. 19: 4333-4336. 8. Muresan, Z. and Arvan, P., (1997) J. Biol. Chem. 272: 26,095-26,102. 9. Laitusis, A.L., et al., (1999) J. Biol. Chem. 274: 486-493. 10. Hobman, T.C., et al., (1998) Molec. Biol. of the Cell 9: 1265-1278. 11. Doan, A., et al., (1996) Neuron 17(5): 1023-1030. 12. Gimelbrant, A.A., et al., (1999) J. Neurochem. 72(6): 2301-2311. 13. Ravary, A., et al., (2001) Eur. J. Neurosci. 13(7): 1349-1362. 14. Litovchick, L., et al., (2002) J. Biol. Chem. 277(37): 34,413-34,423. 15. Dinser, R., et al., (2002) J. Clin. Invest. 110(4): 505-513. 16. Ko, M.K. and Kay, E.P., (2002) Mol. Vis. 8: 1-9. 17. Kaufmann, T., et al., (2003) J. Cell Biol. 160(1): 53-64. 18. Tailleux, L., et al., (2003) J. Immunol. 170(4): 1939-1948. 19. Yamaguchi, H., et al., (2003) Cancer Res. 63(7): 1483-1489. 20. Tobisawa, S., et al., (2003) Biochem. Biophys. Res. Commun. 303(2): 496-503.