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Anti-Fibrillarin Antibody, clone 38F3

clone 38F3, from mouse

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Histone-glutamine methyltransferase, U3 small nucleolar RNA-associated protein NOP1, Nucleolar protein 1, U3 snoRNA-associated protein NOP1

biological source


Quality Level

antibody form

purified immunoglobulin

antibody product type

primary antibodies


38F3, monoclonal

species reactivity

human, rat, yeast, mouse, Drosophila


immunocytochemistry: suitable
western blot: suitable



NCBI accession no.

UniProt accession no.

shipped in


target post-translational modification


Gene Information

human ... FBL(2091)

General description

rRNA 2′-O-methyltransferase fibrillarin (UniProt: P15646; also known as Histone-glutamine methyltransferase, U3 small nucleolar RNA-associated protein NOP1, Nucleolar protein 1, U3 snoRNA-associated protein NOP1) is encoded by the NOP1 (also known as LOT3, YDL014W, D2870) gene (Gene ID: 851548) in yeast. Fibrillarin is a nucleolar protein that is highly conserved throughout evolution. Human fibrillarin is 67% identical to its yeast homolog Nop1p. Fibrillarin is a protein component of C/D box small nucleolar ribonucleoproteins (snoRNPs) that direct 2 -O-methylation of rRNA and is also involved in other aspects of rRNA processing. Unlike snRNAs, which have a cytoplasmic phase of maturation, snoRNAs are restricted to the nucleus. Fibrillarin is essential for yeast viability and fibrillarin knockout is shown to be lethal in S. cerevisiae; however, expression of human or Xenopus fibrillarin overcome this lethality. The first 80 amino acids from the N terminal region of fibrillarin contain multiple RGG, or arginine-glycine-glycine (GAR). The remaining ~240 amino acids consist of the so called fibrillarin domain. NOP1 depleted strains of yeast are greatly impaired in the production of cytoplasmic ribosomes, and they have a reduced level of rRNA. Patients with scleroderma are reported to have strong circulating autoantibodies to fibrillarin. (Ref.: Tollervey, D et al. (1991). EMBO J. 10(3):573-83; Newton, K et al. (2003). Mol. Cell. Biol. 23(23): 8519-8527).


Clone 38F3 specifically detects Fibrillarin/Nop1p in multiple mammalian species and in yeast.


Yeast nuclear extract


Anti-Fibrillarin, clone 38F3, Cat. No. MABE1154, is a highly specific mouse monoclonal antibody that targets Fibrillarin/Nop1p and has been tested in Immunocytochemistry and Western Blotting.
Immunocytochemistry Analysis: A representative lot detected Fibrillarin in human SH-SY5Y cells (Courtesy of Dr Gerry Shaw).

Immunocytochemistry Analysis: A representative lot detected Fibrillarin in Immunocytochemistry applications (Newton, K., et. al. (2003). Mol. Cell. Biol. 23(23):8519-27).
Research Category
Epigenetics & Nuclear Function


Evaluated by Western Blotting in HeLa cell lysates.

Western Blotting Analysis: 0.5 µg/mL of this antibody detected Fibrillarin in 10 µg of HeLa cell lysates.

Target description

~34 kDa observed; 34.46 kDa calculated. Uncharacterized bands may be observed in some lysate(s).

Physical form

Affinity Purified
Format: Purified
Purified mouse monoclonal antibody IgG1 in buffer containing PBS with 0.03% sodium azide with 50% glycerol.

Storage and Stability

Stable for 1 year at -20°C from date of receipt.

Handling Recommendations: Upon receipt and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance.

Other Notes

Concentration: Please refer to lot specific datasheet.


Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Storage Class

10 - Combustible liquids



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Emma Lacroix et al.
Journal of cell science, 134(22) (2021-10-28)
In response to environmental stress, human cells have been shown to form reversible amyloid aggregates within the nucleus, termed amyloid bodies (A-bodies). These protective physiological structures share many of the biophysical characteristics associated with the pathological amyloids found in Alzheimer's

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