Fibrillarin (Nop1p) Antibody
Mouse monoclonal antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND

Application
| WB, IF |
|---|---|
| Primary Accession | P15646 |
| Reactivity | Human, Rat |
| Host | mouse |
| Clonality | monoclonal |
| Isotype | IgG1 |
| Clone Names | 38F3 |
| Calculated MW | 34 KDa |
| Gene ID | 851548 |
|---|---|
| Gene Name | NOP1 |
| Other Names | rRNA 2'-O-methyltransferase fibrillarin, 211-, Histone-glutamine methyltransferase, U3 small nucleolar RNA-associated protein NOP1, Nucleolar protein 1, U3 snoRNA-associated protein NOP1, NOP1, LOT3 |
| Target/Specificity | Yeast nuclear preparations. |
| Dilution | WB~~ 1:1000 IF~~ 1:500 |
| Format | Total IgG fraction |
| Antibody Specificity | Specific for the ~34kDa Fibrillarin /Nop1p protein. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | Fibrillarin (Nop1p) Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Shipping | Blue Ice |

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Provided below are standard protocols that you may find useful for product applications.
Background
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 archea 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 ~34kDa 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).
References
1. Ochs RL, Lischwe MA, Spohn WH, Busch H. Fibrillarin: a new protein of the nucleolus identified by autoimmune sera. Biol Cell 54:123-133 (1985).
2. Aris JP and Blobel G. Identification and characterization of a yeast nucleolar protein that is similar to a rat liver nucleolar protein. J. Cell Biol. 107:17-31 (1988).
3. Newton K, Petfalski E, Tollervey D, Caceres JF. Fibrillarin is essential for early development and required for accumulation of an intron-encoded small nucleolar RNA in the mouse. Mol Cell Biol. 23:8519-8527 (2003).
4. Tyagi S and Alsmadi O. Imaging native beta-actin mRNA in motile fibroblasts. Biophys J. 87:4153-62 (2004).
5. Paeschke1 K, Simonsson T, Postberg J, Rhodes D, Lipps H-J. Telomere end-binding proteins control the formation of G-quadruplex DNA structures in vivo Nature Structural & Molecular Biology 12, 847-854 (2005).
6. Vermaak D, Henikoff S, Malik HS. Positive selection drives the evolution of rhino, a member of the heterochromatin protein 1 family in Drosophila. PLoS Genetics 1:96-108 (2005).
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