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Verotoxin I-B subunit (Shiga-like, SLT-1b)

Cat no: V2121-60A

Verotoxin I-B subunit (Shiga-like, SLT-1b)

Shiga-like toxins, also called verotoxins, inhibit protein synthesis in eukaryotic cells. These toxins play a role in hemorrhagic colitis and hemolytic uremic syndrome. They damage endothelial cells in both kidney and brain, causing renal failure and neurological complications. The protein structure consists of two domains: the A polypeptide confers the activity, and the B polypeptide pentamer confers the receptor-specific binding. The A polypeptide has an N-glycosidase activity that cleaves an adenine from the 28S rRNA of the 60S cytoplasmic ribosome. This activity renders the 28S rRNA unable to interact with the elongation factors EF-1 and EF-2, thus inhibiting protein synthesis. The B polypeptide forms a pentamer that binds to the eukaryotic cell receptor globotriaosylceramide (Gb3). Shiga-like toxins then enter the cells by receptor-mediated endocytosis. The effects of shiga-like toxin 1 and shiga-like toxin 2 have been shown to vary with cell type because Gb3 receptors are present in certain tissues, particularly sensory neurons and renal cells. In those cell types, the receptor concentration and binding is modulated by factors such as tumor necrosis factor (TNF), interleukins, and fatty acid content of the membranes. Shiga-like toxin 1 and shiga-like toxin 2 differ in their effects on various tissues. They have both been shown to induce apoptosis in several different cell types. These toxins have many interesting effects at the cellular level. Once the shiga-like toxins have been endocytosed, they are retrogradely transported through the golgi apparatus to the rough endoplasmic reticulum where they effectively target the ribosomes. In addition to inhibiting protein synthesis, shiga- like toxins induce cytokines such as interleukin-1, interleukin-6, and interleukin-8. They have also been shown to induce expression of tumor necrosis factor (TNF), induce F-actin depolymerization, and activate a src kinase. Shiga-like toxin 1 and 2 are from E. coli. Shiga-like toxins are very toxic and should be handled with extreme caution.\n\nApplications: \nSuitable for use in ELISA and Neutralization. Other applications not tested.\n\nRecommended Dilution:\nELISA: 1:20-1:200\nOptimal dilutions to be determined by the researcher.\n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. For long-term storage and to avoid repeated freezing and thawing, add sterile 40-50% glycerol , aliquot and store at -20 degrees C. Aliquots are stable for at least 12months at -20 degrees 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.

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SPECIFICATIONS

Catalog Number

V2121-60A

Size

1ml

Applications

ELISA

Hosts

Mouse

Form

Supplied as a liquid in PBS, pH 7.2, 0.1% sodium azide. No stabilizing proteins added.

P Type

Mab

Purity

Purified by Protein A affinity chromatography (> 90%).

Isotype

IgG1

References

1. Riley, L.W., Remis, R.S., Helgerson, S.D., McGee, H.B., Wells, J.G., David, B.R., Hebert, R.J., Olcott, E.S., Johnson, L.M., Hargrett, N.T., Blake, P.A., and Cohen, M.L. (1983) New Engl. J. Med. 308, 681-685. 2. Ashkenazi, S. (1993) Annu. Rev. Med. 44, 11-18. 3. Takeda, T., Dohi, S., Igarashi, T., Yamanaka, T., Yoshiya, K., Kobayashi, N. (1993) J. Infect. 27, 339-341. 4. Coia, J.E. (1998) FEMS Immunology and Med. Microbiol. 20, 1-9. 5. Endo, Y., Tsurugi, K., Yutsudo, T., Takeda, Y., Ogasawara, T., Igarashi, K. (1998) Eur. J. Biochem. 171, 45-50. 6. Lingwood, C.A. (1993) Adv. Lipid Res. 25, 189-211. 7. Sandvig, K., Van Deurs, B. (1994) FEBS Lett. 346, 99-102. 8. Lingwood, C.A. (1996) Trends Microbiol. 4, 147-153. 9. Ren, J., Utsunomiya, I., Taguchi, K., Ariga, T., Tai, T., Ihara, Y., Miyatake, T. (1999) Brain Res. 825, 183-188. 10. Williams, J.M., Boyd, B., Nutikka, A., Lingwood, C.A., Barnett Foster, D.E., Milford, D.V., Taylor, C.M. (1999) Tox. Lett. 105, 47-57. 11. Van De Kar, N.C., Monnens, L.A.,Van Hinsbergh, V.W. (1993) Behring Inst. Mitt. 92, 202-209. 12. Ramegowda, B., Tesh, V.L. (1996) Inf. and Imm. 64, 1173-1180. 13. Pellizzari, A., Pang, H., Lingwood, C.A. (1992) Biochem. 31, 1363-1370. 14. Boyd, B., Magnusson, G., Zhiuyan, Z., Lingwood, C.A. (1994) Eur. J. Biochem. 223, 873-878. 15. Kiarash, A., Boyd, B., Lingwood, C.A. (1994) J. Bio. Chem. 269, 11138-11146. 16. Hurley, B.P., Jacewicz, M., Thorpe, C.M., Linciocome, L.L., King, A.J., Keusch, G.T., Acheson, D.W. (1999) Inf. and Imm. 67, 6670-6677. 17. Van Setten, P.A., Van Hinsbergh, V.W., Van Den Heuvel, L.P., Van Der Velden, T.J., Van De Kar, N.C., Krebbers, R.J., Karmali, M.A., Monnens, L.A. (1997) J. Am. Soc. Nephrology 8, 1877-1888. 18. Arab, S., Rutka, J., Lingwood, C.A. (1999) Oncology Res. 11, 33-39. 19. Inward, C.D., Williams, J., Chant, I., Crocker, J., Milford, D.V., Rose, P.E., Taylor, C.M. (1995) J. Infection 30, 213- 218. 20. Uchida, H., Kiyokawa, N., Taguchi, T., Horie, H., Fujimoto, J., Takeda, T. (1999) J. Infect. Dis. 180, 1902-1911. 21. Yoshida, T., Fukada, M., Koide, N., Ikeda, H., Sugiyama, T., Kato, Y., Ishikawa, N., Yokochi, T. (1999) J. Infect. Dis. 180, 2048-2052. 22. Arab, S., Murakami, M., Dirks, P., Boyd, B., Hubbard, S.L., Lingwood, C.A., Rutka, J.T. (1998) J. Neuro-Oncology 40, 137-150. 23. Roberts, L.M., Lord, J.M., (1992) Curr. Opin. Biotechnol. 3, 422-429. 24. Van Setten, P.A., Monnens, L.A., Verstraten, R.G., Van Den Heuvel, L.P., Van Hinsbergh, V.W., (1996) Blood 88, 174- 183. 25. Tesh, V.L., Ramegowda, B., Samuel, J.E. (1994) Inf. and Imm.62, 5085-5094. 26. Thorpe, C.M., Hurley, B.P., Lincicome, L.L., Jacewicz, M.S., Keusch, G.T., Acheson, D.W. (1999) Inf. and Imm. 67, 5985-5993. 27. Harel, Y., Silva, M., Giroir, B., Weinberg, A., Cleary, T.B., Beutler, B. (1993) J. Clin. Invest. 92, 2110-2116. 28. Bourdet-Sicard, R., R diger, M., Jokusch, B.M., Gounon, P., Sansonetti, P.J., Nhieu, G.T. (1999) EMBO Journal 18 5853-5862. 29. Katagiri, Y.U., Mori, T., Nakajima, H., Katagiri, C., Taguchi, T., Takeda, T., Kiyokawa, N., Fujimoto, J. (1999) J. Biol. Chem. 274, 35278-35282. 30. Takeda, Y., Kurazono, H., Yamasaki, S. (1993) Microbiol. Immunol. 37, 591-599. 31. Melton-Celsa, A.R., O'Brien, A.D. (1997) Guidebook to Protein Toxins and Their Use in Cell Biology. (Eds. Rappuoli, R. and Montecucco, C.) Sambrook and Tooze, Oxford Univ. Press.

Additional Info

Specific for Verotoxin I-B subunit (SLT-1b). Neutralizes Verotoxin

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