Our Anti-Fibrillarin primary antibody from PhosphoSolutions is mouse monoclonal. It detects human, mouse, and rat Fibrillarin and is Protein G purified. It is great for use in WB, IHC, ICC.
High magnification confocal image of HeLa cells showing strong, prominent labeling of the nucleoli in the nucleus with Anti-Fibrillarin (cat. 560-FIB, 1:100, green), colabeled with Anti-Vimentin (cat. 2105-VIM, red, 1:1000) showing the cytoplasmic intermediated filaments, and nuclear staining was done with DAPI (blue).
Bovine, Chicken, Drosophila, Human, Mouse, Pig, Rat
Nop1p was originally identified as a nucleolar protein of bakers yeast, Saccharomyces cerevisiae. The Nop1p protein is 327 amino acids in size (34.5kDa), is essential for yeast viability, and is localized in the nucleoli (1). The systematic name for S. cerevisiae Nop1 is YDL014W, and it is now known to be part of the small subunit processome complex, involved in the processing of pre-18S ribosomal RNA. Nop1p is the yeast homologue of a protein found in all eukaryotes and archaea generally called fibrillarin (2). Fibrillarin/Nop1p is extraordinarily conserved, so that the yeast and human proteins are 67% identical, and the human protein can functionally replace the yeast protein. Patients with the autoimmune disease scleroderma often have strong circulating autoantibodies to a ~34 kDa protein which was subsequently found to be fibrillarin. Recent studies show that knock-out of the fibrillarin gene in mice results in embryonic lethality, although mice with only one functional fibrillarin/Nop1p gene were viable (3). This antibody is becoming widely used as a convenient marker for nucleoli in a wide variety of species (e.g. 4-6).
Protein G Purified
Monoclonal
38F3
IgG1
ICC, IHC, WB
Mouse
NOP1
34 kDa
Yeast nuclear preparation
Bovine, Chicken, Drosophila, Human, Mouse, Pig, Rat
Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C.
Liquid
Protein G purified culture supernatant.
PBS + 50% glycerol and 5 mm NaN3
WB: 1:1000
IHC: 1:100-1:500
ICC: 1:100-1:500
Unconjugated
Specific for endogenous levels of the ~34 kDa Fibrillarin /Nop1p protein.
Western blots performed on each lot.
For research use only. Not intended for therapeutic or diagnostic use. Use of all products is subject to our terms and conditions, which can be viewed on our website.
After date of receipt, stable for at least 1 year at -20°C.
Paeschke, K., Simonsson, T., Postberg, J., Rhodes, D. and Lipps, H.J., 2005. Telomere end-binding proteins control the formation of G-quadruplex DNA structures in vivo. Nature Structural & Molecular Biology, 12(10), p.847. PMID: 16142245
Vermaak, D., Henikoff, S. and Malik, H.S., 2005. Positive selection drives the evolution of rhino, a member of the heterochromatin protein 1 family in Drosophila. PLoS Genetics, 1(1), 96-108. PMID: 16103923
Tyagi, S. and Alsmadi, O., 2004. Imaging native β-actin mRNA in motile fibroblasts. Biophysical Journal, 87(6), pp.4153-4162. PMID: 15377515
Newton, K., Petfalski, E., Tollervey, D. and Cáceres, J.F., 2003. Fibrillarin is essential for early development and required for accumulation of an intron-encoded small nucleolar RNA in the mouse. Molecular and Cellular Biology, 23(23), pp.8519-8527. PMID: 14612397
Aris, J.P. and Blobel, G., 1988. Identification and characterization of a yeast nucleolar protein that is similar to a rat liver nucleolar protein. The Journal of Cell Biology, 107(1), pp.17-31. PMID: 3292539
Ochs, R.L., Lischwe, M.A., Spohn, W.H. and Busch, H., 1985. Fibrillarin: a new protein of the nucleolus identified by autoimmune sera. Biology of the Cell, 54(2), pp.123-133. PMID: 2933102
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