Anti-fibrillarin: mouse Mab

Product Uses
The following protocols have been tested with this antibody:

Source
Fibrillarin antibody is provided as a monoclonal antibody. The main use of the antibody is to label the nucleolus during in situ staining or when using the nuclear spread method. It can also be used for immunoprecipitation of nucleoprotein complexes as reported from the originating lab of Eng Tan and Mike Pollard (Scripps Research Institute). The antibody has been produced as mouse ascites fluid. The control protein (bovine thymus extract, Cat. # EXT03) is supplied as a lyophilized powder; this should be reconstituted in 500 μl of cold Milli-Q water to 2 mg/ml. After addition of water the protein should be left at room temperature for 5 minutes with occasional pipetting up and down to make sure that the protein has completely dissolved into solution, it can then be stored at -20°C. We recommend running 20 μg of positive control protein in Western blots.
Western blot analysis identifies a characteristic fibrillarin band at 35 kDa. Other bands are also identified such as the histone proteins because of their arginine rich regions.

Material
The fibrillarin antibody (100 μg) is supplied as a lyophilized powder. It is recommended to resuspend the powder in 200 μl of Milli-Q water which gives a concentration of 500 μg/ml in PBS. Chlorhexidine (0.005%) is included as preservative.

For product Datasheets and MSDSs please click on the PDF links below.   For additional information, click on the FAQs tab above or contact our Technical Support department at tservice@cytoskeleton.com

Product Description

MSDS

Datasheet

Cat #

Anti-fibrillarin: mouse Mab AFB01

Arabi, A., Wu, S., Ridderstrale, K., Bierhoff, H., Shiue, C., Fatyol, K., Fahlen, S., Hydbring, P., Soderberg, O., Grummt, I. et al. (2005). c-Myc associates with ribosomal DNA and activates RNA polymerase I transcription. Nat. Cell Biol. 7, 303-310.

Orihara-Ono, M., Suzuki, E., Saito, M., Yoda, Y., Aigaki, T. and Hama, C. (2005). The slender lobes gene, identified by retarded mushroom body development, is required for proper nucleolar organization in Drosophila. Dev. Biol. 281, 121-133.

Arabi, A., Rustum, C., Hallberg, E. and Wright, A. P. (2003). Accumulation of c-Myc and proteasomes at the nucleoli of cells containing elevated c-Myc protein levels. J. Cell Sci. 116, 1707-1717.

Gonda, K., Fowler, J., Katoku-Kikyo, N., Haroldson, J., Wudel, J. and Kikyo, N. (2003). Reversible disassembly of somatic nucleoli by the germ cell proteins FRGY2a and FRGY2b. Nat. Cell Biol. 5, 205-210.

Polak, P. E., Simone, F., Kaberlein, J. J., Luo, R. T. and Thirman, M. J. (2003). ELL and EAF1 are Cajal body components that are disrupted in MLL-ELL leukemia. Mol. Biol. Cell 14, 1517-1528.

Rubbi, C. P. and Milner, J. (2003). Disruption of the nucleolus mediates stabilization of p53 in response to DNA damage and other stresses. EMBO J. 22, 6068-6077.

Sugimoto, M., Kuo, M. L., Roussel, M. F. and Sherr, C. J. (2003). Nucleolar Arf tumor suppressor inhibits ribosomal RNA processing. Mol. Cell 11, 415-424.

Caballero, O. L., Resto, V., Patturajan, M., Meerzaman, D., Guo, M. Z., Engles, J., Yochem, R., Ratovitski, E., Sidransky, D. and Jen, J. (2002). Interaction and colocalization of PGP9.5 with JAB1 and p27(Kip1). Oncogene 21, 3003-3010.

Coming soon!   If you have any questions concerning this product, please contact our Technical Service department at tservice@cytoskeleton.com