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The protein encoded by PARN is a 3'-exoribonuclease, with similarity to the RNase D family of 3'-exonucleases. Additionally we are shipping PARN Antibodies (65) and PARN Kits (9) and many more products for this protein.
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we found a polyadenylation-dependent 3' end maturation pathway for the human telomerase RNA that relies on the nuclear poly(A)-binding protein PABPN1 (show PABPN1 Proteins) and the poly(A)-specific RNase PARN.
PARN increased telomerase RNA component levels by deadenylating telomerase RNA component, thereby limiting its degradation by EXOSC10 (show EXOSC10 Proteins).
Large monoallelic mutations of PARN can cause developmental/mental illness. Biallelic PARN mutations cause severe bone marrow failure and central hypomyelination.
results highlight the clinical significance of PARN and NOC (show CCRN4L Proteins) on the survival in SCC (show CYP11A1 Proteins) diagnosed patients.
Mutations in the PARN gene cause dyskeratosis congenital.
The results indicate that the cellular level of miR (show MLXIP Proteins)-122 is determined by the balance between the opposing effects of GLD-2 (show PAPD4 Proteins) and PARN/CUGBP1 (show CELF1 Proteins) on the metabolism of its 3'-terminus.
3 families with dyskeratosis congenita had key domain mutations in PARN shortening telomeres, reducing deadenylation, and downregulating TERC, DKC1 (show DKC1 Proteins), RTEL1, and TERF1 (show TERF1 Proteins).
PARN and RTEL1 mutation carriers had shortened leukocyte telomere lengths.
poly(A)-specific ribonuclease (PARN) was upregulated in gastric tumor tissues and gastric cancer cell lines MKN28 and AGS (show JAG1 Proteins).
poly(A) polymerase (show PAPOLA Proteins) Gld2 (show PAPD4 Proteins), deadenylase PARN, and translation inhibitory factor neuroguidin (Ngd (show NGDN Proteins)) are components of a dendritic CPEB (show CPEB1 Proteins)-associated polyadenylation apparatus
these data indicate that PARN modulates decay of a defined set of mRNAs in mammalian cells and implicate this deadenylase in coordinating control of genes required for cell movement.
Solution structures of the cap-binding domain of mouse PARN with and without the m(7)GpppG cap analog reveal a novel cap-binding mode.
A modeled PARN, which shows that the RRM domain from one subunit and the R3H domain from the other subunit enclose the active site.
The protein encoded by this gene is a 3'-exoribonuclease, with similarity to the RNase D family of 3'-exonucleases. It prefers poly(A) as the substrate, hence, efficiently degrades poly(A) tails of mRNAs. Exonucleolytic degradation of the poly(A) tail is often the first step in the decay of eukaryotic mRNAs. This protein is also involved in silencing of certain maternal mRNAs during oocyte maturation and early embryonic development, as well as in nonsense-mediated decay (NMD) of mRNAs that contain premature stop codons. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
, deadenylation nuclease
, poly(A)-specific ribonuclease (deadenylation nuclease)
, poly(A)-specific ribonuclease PARN
, polyadenylate-specific ribonuclease