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Key Documents

HPA006314

Sigma-Aldrich

Anti-PARN antibody produced in rabbit

enhanced validation

Ab1, Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution

Synonym(s):

Anti-Deadenylating nuclease antibody produced in rabbit, Anti-Deadenylation nuclease antibody produced in rabbit, Anti-Poly(A)-specific ribonuclease PARN antibody produced in rabbit, Anti-Polyadenylate-specific ribonuclease antibody produced in rabbit

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About This Item

UNSPSC Code:
12352203
Human Protein Atlas Number:
NACRES:
NA.43

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

product line

Prestige Antibodies® Powered by Atlas Antibodies

form

buffered aqueous glycerol solution

species reactivity

human, mouse, rat

enhanced validation

independent
Learn more about Antibody Enhanced Validation

technique(s)

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

immunogen sequence

DGEFSGISDGPSVSALTNGFDTPEERYQKLKKHSMDFLLFQFGLCTFKYDYTDSKYITKSFNFYVFPKPFNRSSPDVKFVCQSSSIDFLASQGFDFNKVFRNGIPYLNQEEERQLREQYDEKRSQANGAGA

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... PARN(5073)

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General description

Poly(A)-specific ribonuclease (PARN) is a 3′- exoribonuclease found in mammals. It is a member of the DEDD (death effector domain-containing protein) family of nucleases, and is a divalent metal-ion dependent enzyme. It is divided into three structural domains, with the nuclease domain harboring the active site. This protein also contains RNA-recognition motif (RRM) and the R3H domain, which function as RNA-binding domains. This gene is localized to human chromosome 16p13.

Immunogen

Poly(A)-specific ribonuclease PARN recombinant protein epitope signature tag (PrEST)

Application

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.

Biochem/physiol Actions

Poly(A)-specific ribonuclease (PARN) is one of the rare mammalian exonucleases that has a high specificity for poly(A) degradation. It interacts with both the poly(A) tail and with the 5′ end-located cap-structure. It is a highly processive enzyme as its interaction with 5′-end cap enhances its rate of degradation. This protein is up-regulated in gastric cancer, and its inactivation results in cell cycle arrest, thus, inhibiting the proliferation of gastric cancer cells.

Features and Benefits

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 APREST70834

Physical form

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

Legal Information

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

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Storage Class

10 - Combustible liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Wei-Feng Liu et al.
Biochemical and biophysical research communications, 379(2), 341-345 (2008-12-24)
Poly(A)-specific ribonuclease (PARN), a multi-domain dimeric enzyme, is a deadenylase in higher vertebrates and plants with the unique property of cap-dependent catalysis and processivity. We found that PARN is an allosteric enzyme, and potassium ions and the cap analogue were
K Buiting et al.
Cytogenetics and cell genetics, 87(1-2), 125-131 (2000-01-21)
The deadenylation nuclease or poly(A)-specific ribonuclease (PARN) is a 3' exonuclease, which degrades the poly(A)-tail of eukaryotic mRNA molecules. By DNA sequence analysis of cDNA and genomic clones, fluorescence in situ hybridization, and reverse transcriptase-PCR, we have determined that the
Niklas Henriksson et al.
The Journal of biological chemistry, 285(1), 163-170 (2009-11-11)
Poly(A)-specific ribonuclease (PARN) is a mammalian 3'-exoribonuclease that degrades poly(A) with high specificity. To reveal mechanisms by which poly(A) is recognized by the active site of PARN, we have performed a kinetic analysis using a large repertoire of trinucleotide substrates.
Guang-Jun He et al.
Biochimica et biophysica acta, 1834(6), 1089-1098 (2013-02-08)
Deadenylases specifically catalyze the degradation of eukaryotic mRNA poly(A) tail in the 3'- to 5'-end direction with the release of 5'-AMP as the product. Among the deadenylase family, poly(A)-specific ribonuclease (PARN) is unique in its domain composition, which contains three
Jocelyn N Galloway et al.
Human molecular genetics, 23(22), 5906-5915 (2014-07-06)
Determining the molecular mechanism(s) leading to Purkinje neuron loss in the neurodegenerative disorder fragile X-associated tremor/ataxia syndrome (FXTAS) is limited by the complex morphology of this cell type. Purkinje neurons are notoriously difficult to isolate and maintain in culture presenting

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