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Retinol Binding Protein 4 (RBP4) ELISA Bioassay

Cat no: R1701-36

Retinol Binding Protein 4 (RBP4) ELISA Bioassay

Human RBP4 immunoassay is a 2.5 hour solid phase ELISA designed to measure human RBP4 in cell culture supernates, serum, plasma, urine, and saliva. It contains NS0-expressed recombinant human RBP4 and has been shown to accurately quantitate the recombinant factor. Results obtained using natural human RBP4 showed linear curves that were parallel to the standard curves obtained using the Quantikine kit standards. These results indicate that this kit can be used to determine relative mass values for naturally occurring human RBP4.\n\nAssay Type: Solid Phase Sandwich ELISA\nFormat: 96-well strip plate\nAssay Length: 2.5 hours\nSample Type & Volume Required Per Well:Cell Culture Supernates (20 microL), Serum (10 microL), EDTA Plasma (10 microL), Heparin Plasma (10 microL), Saliva (10 microL), Urine (10 microL)\nSensitivity: 0.628 ng/mL\nAssay Range: 1.56 - 100 ng/mL (Serum, Heparin Plasma, Saliva, Cell Culture Supernates, EDTA Plasma, Urine)\nSpecificity: Natural and recombinant human RBP4\nCross-reactivity: < 0.5% cross-reactivity observed with available related molecules. Cross-species reactivity not tested.\nInterference: No significant interference observed with available related molecules.\n\nKit Components:\nRBP4 Microplate, 1x96 wells\nRBP4 Conjugate, 1x21ml \nRBP4 Standard (lyophilized), 1x200ng \nAssay Diluent, 2x11ml\nCalibrator Diluent, 2x21ml \nWash Buffer Concentrate (25X), 1x 21ml \nColor Reagent A, (H2O2) 1x12.5ml\nColor Reagent B (TMPD), 1x12.5ml \nStop Solution (2N H2SO4) 1x6ml \n\nStorage and Stability:\nStore components at 4 degrees C. Stable for 6 months. For maximum recovery of product, centrifuge the original vial prior to removing the cap.пїЅ

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SPECIFICATIONS

Catalog Number

R1701-36

Size

1Kit

References

1. Blomhoff, R. et al. (1992) Annu. Rev. Nutr. 12:37. 2. Zanotti, G. and R. Berni (2004) Vitam. and Horm. 69:271. 3. Breustedt, D.A. et al. (2006) Biochim. Biophys. Acta 1764:161. 4. Colantuoni, V. et al. (1983) Nucleic Acids Res. 11:7769. 5. Moise, A.R. et al. (2007) Biochemistry 46:4449. 6. Okada, T. and K. Palczewski (2001) Curr. Opin. Struct. Biol. 11:420. 7. McGrane, M.M. (2007) J. Nutr. Biochem. 18:497. 8. Means, A.L. and L.J. Gudas (1995) Annu. Rev. Biochem. 64:201. 9. Cowan, S.W. et al. (1990) Proteins: Struct. Funct. Genet. 8:44. 10. Melhus, H. et al. (1992) J. Biol. Chem. 267:12036. 11. Tsutsumi, C. et al. (1992) J. Biol. Chem. 267:1805. 12. Jaconi, S. et al. (1995) J. Lipid Res. 36:1247. 13. Naylor, H.M. and M.E. Newcomer (1999) Biochemistry 38:2647. 14. van Bennekum, A.M. et al. (2001) J. Biol. Chem. 276:1107. 15. Raila, J. et al. (2005) J. Nutr. 135:2512. 16. Huang, J. and A. Vieira (2006) Int. J. Mol. Med. 17:627. 17. van Bennekum, A. et al. (1999) J. Lipid Res. 40:565. 18. Biesalski, H.K. et al. (1999) Am. J. Clin. Nutr. 69:931. 19. Yang, Q. et al. (2005) Nature 436:356. 20. Kloting, N. et al. (2007) Cell Metab. 6:79. 21. Stefan, N. et al. (2007) Diabetes Care 30:1173. 22. Raila, J. et al. (2007) Kidney Int. 72:505. 23. Von Eynatten, M. et al. (2007) Diabetologia 50:1930. 24. Munkhtulga, L. et al. (2007) Hum. Genet. 120:879. 25. Moro, C. et al. (2007) Diabetologia 50:1038. 26. Sell, H. and J. Eckel (2007) Diabetologia 50:2221.14.

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