Mapping of nuclear localization signals by simultaneous fusion to green fluorescent protein and to beta-galactosidase.
نویسندگان
چکیده
1.Ausubel, F.M., R. Brent, R.E. Kinston, D.D. Moore, J.G. Seidman, J.A. Smith and K. Struhl. 1987. Current Protocols in Molecular Biology. Greene/Wiley Interscience, New York. 2.Chandler, C.S. and F.J. Ballard. 1986. Multiple biotin-containing proteins in 3T3-L1 cells. Biochem. J. 237:123-130. 3.Dignam, J., R. Lebovitz and R. Roeder. 1983. Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei. Nucleic Acids Res. 11:1475-1489. 4.Grino, M. and A.J. Zamora. 1998. An in situ hybridization histochemistry technique allowing simultaneous visualization by the use of confocal microscopy of three cellular mRNA species in individual neurons. J. Histochem. Cytochem. 46:753-759. 5.Haneji, T. and S.S. Koide. 1989. Transblot identification of biotin-containing proteins in rat liver. Anal. Biochem. 177:57-61. 6.Hsu, S.M. and L. Raine. 1981. Protein A, avidin, and biotin in immunohistochemistry. J. Histochem. Cytochem. 29:1349-1353. 7.Hymes, J. and B. Wolf. 1996. Biotinidase and its roles in biotin metabolism. Clin. Chim. Acta 255:1-11. 8.Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685. 9.Nedergaard, J. and B. Cannon. 1979. Overview–preparation and properties of mitochondria from different sources. Methods in Enzymology, Vol 55. Academic Press, New York. 10.Nikolau, B.J., E.S. Wurtele and P.K. Stumpf. 1985. Use of streptavidin to detect biotin-containing proteins in plants. Anal. Biochem. 149:448-453. 11.Pringle, J.H., L. Primrose, C.N. Kind, I.C. Talbot and I. Lauder. 1989. In situ hybridization demonstration of poly-adenylated RNA sequences in formalin-fixed paraffin sections using a biotinylated oligonucleotide poly d(T) probe. J. Pathol. 158:279-286. 12.Whitehead T.P., L.J. Kricka, T.J. Carter and G.H. Thorpe. 1979. Analytical luminescence: its potential in the clinical laboratory. Clin. Chem. 25:1531-1546.
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ورودعنوان ژورنال:
- BioTechniques
دوره 26 5 شماره
صفحات -
تاریخ انتشار 1999