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Merck
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Documenti fondamentali

HPA018166

Sigma-Aldrich

Anti-RRP1 antibody produced in rabbit

Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution, Ab2

Sinonimo/i:

Anti-Novel nuclear protein 1, Anti-Nucleolar protein Nop52, Anti-Protein NNP-1, Anti-RRP1-like protein, Anti-Ribosomal RNA processing protein 1 homolog A

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About This Item

Codice UNSPSC:
12352203
Numero Human Protein Atlas:
NACRES:
NA.43

Origine biologica

rabbit

Livello qualitativo

Coniugato

unconjugated

Forma dell’anticorpo

affinity isolated antibody

Tipo di anticorpo

primary antibodies

Clone

polyclonal

Nome Commerciale

Prestige Antibodies® Powered by Atlas Antibodies

Stato

buffered aqueous glycerol solution

Reattività contro le specie

human

tecniche

immunoblotting: 0.04-0.4 μg/mL
immunofluorescence: 0.25-2 μg/mL
immunohistochemistry: 1:200-1:500

Sequenza immunogenica

NLKFIDPFCRIAARTKDSLVLNNITRGIFETIVEQAPLAIEDLLNELDTQDEEVASDSDESSEGGERGDALSQKRSEKPPA

N° accesso UniProt

Condizioni di spedizione

wet ice

Temperatura di conservazione

−20°C

modifica post-traduzionali bersaglio

unmodified

Informazioni sul gene

human ... RRP1(8568)

Descrizione generale

The gene RRP1 (ribosomal RNA processing protein-1 homolog A) has been mapped to human chromosome 21q22.3. The protein is a human homologue of the yeast ribosomal RNA processing protein RRP1. The protein has been localized to the nucleoli and at the periphery of the chromosomes.

Immunogeno

Ribosomal RNA processing protein 1 homolog A recombinant protein epitope signature tag (PrEST)

Applicazioni

All Prestige Antibodies Powered by Atlas Antibodies are developed and validated by the Human Protein Atlas (HPA) project and as a result, are supported by the most extensive characterization in the industry.

The Human Protein Atlas project can be subdivided into three efforts: Human Tissue Atlas, Cancer Atlas, and Human Cell Atlas. The antibodies that have been generated in support of the Tissue and Cancer Atlas projects have been tested by immunohistochemistry against hundreds of normal and disease tissues and through the recent efforts of the Human Cell Atlas project, many have been characterized by immunofluorescence to map the human proteome not only at the tissue level but now at the subcellular level. These images and the collection of this vast data set can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. We also provide Prestige Antibodies® protocols and other useful information.

Azioni biochim/fisiol

In nucleoli, ribosomal RNA processing protein-1 homolog A (RRP1) is excluded from the rRNA transcription sites, which accumulates in the granular external domain and mainly co-localizes with nucleolar proteins such as B23 which are involved in late processing step. The perinuclear bodies sequentially recruit fibrillarin, nucleoli and RRP1 together with B23 during formation of the nucleolus at the end of mitosis. p32, fibrillarin and RRP1 play key roles in the separation of pre-90S particle into pre-40S and pre-60S particles. RRP1 is also involved in the cleavage at site 2 in internal transcribed space1 of pre-rRNAs at early stages of human ribosome biogenesis. Together the above two events are essential to produce the small and large ribosomal subunits in human cells.

Caratteristiche e vantaggi

Prestige Antibodies® are highly characterized and extensively validated antibodies with the added benefit of all available characterization data for each target being accessible via the Human Protein Atlas portal linked just below the product name at the top of this page. The uniqueness and low cross-reactivity of the Prestige Antibodies® to other proteins are due to a thorough selection of antigen regions, affinity purification, and stringent selection. Prestige antigen controls are available for every corresponding Prestige Antibody and can be found in the linkage section.

Every Prestige Antibody is tested in the following ways:
  • IHC tissue array of 44 normal human tissues and 20 of the most common cancer type tissues.
  • Protein array of 364 human recombinant protein fragments.

Linkage

Corresponding Antigen APREST73884

Stato fisico

Solution in phosphate-buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide

Note legali

Prestige Antibodies is a registered trademark of Merck KGaA, Darmstadt, Germany

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Codice della classe di stoccaggio

10 - Combustible liquids

Classe di pericolosità dell'acqua (WGK)

WGK 1

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


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T M Savino et al.
The Journal of cell biology, 153(5), 1097-1110 (2001-05-31)
To understand how nuclear machineries are targeted to accurate locations during nuclear assembly, we investigated the pathway of the ribosomal RNA (rRNA) processing machinery towards ribosomal genes (nucleolar organizer regions [NORs]) at exit of mitosis. To follow in living cells
Edward W Horsey et al.
RNA (New York, N.Y.), 10(5), 813-827 (2004-04-22)
The Saccharomyces cerevisiae gene RRP1 encodes an essential, evolutionarily conserved protein necessary for biogenesis of 60S ribosomal subunits. Processing of 27S pre-ribosomal RNA to mature 25S rRNA is blocked and 60S subunits are deficient in the temperature-sensitive rrp1-1 mutant. We
Uta Behrends et al.
International journal of cancer, 100(6), 669-677 (2002-09-05)
Autologous serological screening of a cDNA expression library (SEREX) derived from childhood neuroblastoma led to the identification of 10 different antigens, including 6 novel gene products. The novel antigen 018INX was derived from a small open reading frame in a
Harunori Yoshikawa et al.
Molecular & cellular proteomics : MCP, 10(8), M110-M110 (2011-05-04)
Ribosome biogenesis starts with transcription of the large ribosomal RNA precursor (47S pre-rRNA), which soon combines with numerous factors to form the 90S pre-ribosome in the nucleolus. Although the subsequent separation of the pre-90S particle into pre-40S and pre-60S particles
T M Savino et al.
Journal of cell science, 112 ( Pt 12), 1889-1900 (1999-05-26)
We report the molecular characterization of a novel nucleolar protein, Nop52, and its subcellular distribution during the cell cycle and nucleologenesis. This protein was originally identified with human autoantibodies which were subsequently used to clone its corresponding cDNA. Transfection experiments

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