Recombinant Human Poly(A)-specific ribonuclease PARN(PARN)

Code CSB-EP017456HU
Size US$1726
Image
  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

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Product Details

Purity Greater than 90% as determined by SDS-PAGE.
Target Names PARN
Uniprot No. O95453
Research Area Transcription
Alternative Names DAN; Deadenylating nuclease; Deadenylation nuclease; PARN; PARN_HUMAN; Poly A specific ribonuclease; Poly(A) specific ribonuclease; Poly(A)-specific ribonuclease PARN; Polyadenylate specific ribonuclease; Polyadenylate-specific ribonuclease
Species Homo sapiens (Human)
Source E.coli
Expression Region 1-639aa
Target Protein Sequence MEIIRSNFKSNLHKVYQAIEEADFFAIDGEFSGISDGPSVSALTNGFDTPEERYQKLKKHSMDFLLFQFGLCTFKYDYTDSKYITKSFNFYVFPKPFNRSSPDVKFVCQSSSIDFLASQGFDFNKVFRNGIPYLNQEEERQLREQYDEKRSQANGAGALSYVSPNTSKCPVTIPEDQKKFIDQVVEKIEDLLQSEENKNLDLEPCTGFQRKLIYQTLSWKYPKGIHVETLETEKKERYIVISKVDEEERKRREQQKHAKEQEELNDAVGFSRVIHAIANSGKLVIGHNMLLDVMHTVHQFYCPLPADLSEFKEMTTCVFPRLLDTKLMASTQPFKDIINNTSLAELEKRLKETPFNPPKVESAEGFPSYDTASEQLHEAGYDAYITGLCFISMANYLGSFLSPPKIHVSARSKLIEPFFNKLFLMRVMDIPYLNLEGPDLQPKRDHVLHVTFPKEWKTSDLYQLFSAFGNIQISWIDDTSAFVSLSQPEQVKIAVNTSKYAESYRIQTYAEYMGRKQEEKQIKRKWTEDSWKEADSKRLNPQCIPYTLQNHYYRNNSFTAPSTVGKRNLSPSQEEAGLEDGVSGEISDTELEQTDSCAEPLSEGRKKAKKLKRMKKELSPAGSISKNSPATLFEVPDTW
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight 77.5kDa
Protein Length Full Length
Tag Info N-terminal 6xHis-tagged
Form Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting
and FAQs
Protein FAQs
Storage Condition Store at -20°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA Please contact us to get it.

Target Data

Function 3'-exoribonuclease that has a preference for poly(A) tails of mRNAs, thereby efficiently degrading poly(A) tails. Exonucleolytic degradation of the poly(A) tail is often the first step in the decay of eukaryotic mRNAs and is also used to silence certain maternal mRNAs translationally during oocyte maturation and early embryonic development. Interacts with both the 3'-end poly(A) tail and the 5'-end cap structure during degradation, the interaction with the cap structure being required for an efficient degradation of poly(A) tails. Involved in nonsense-mediated mRNA decay, a critical process of selective degradation of mRNAs that contain premature stop codons. Also involved in degradation of inherently unstable mRNAs that contain AU-rich elements (AREs) in their 3'-UTR, possibly via its interaction with KHSRP. Probably mediates the removal of poly(A) tails of AREs mRNAs, which constitutes the first step of destabilization.
Gene References into Functions
  1. Results show that PARN deadenylase activity is regulated by the phosphorylated form of Nucleolin. PMID: 29168431
  2. Studies suggest that the effects of poly(A)-specific ribonuclease (PARN) mutations on telomere length are likely indirect and may lead to telomere shortening that less perfectly cosegregates with heterozygous mutations. PMID: 26908837
  3. Pulmonary fibrosis patients with mutations in telomerase reverse transcriptase, telomerase RNA component, regulator of telomere elongation helicase 1 and poly(A)-specific ribonuclease were identified and clinical data were analysed. Genetic mutations in telomere related genes lead to a variety of interstitial lung disease diagnoses that are universally progressive. PMID: 27540018
  4. PARN polyadenylates the 3' end of telomerase RNA component (known as TERC or hTR), which serves as the template for telomerase reverse transcriptase-mediated telomere replication. PMID: 28414520
  5. PARN is a new component of the ribosome biogenesis machinery in human cells. PMID: 28402503
  6. provide evidence that PARN can also deadenylate the U6 and RMRP RNAs without affecting their levels PMID: 28760775
  7. poly(A)-specific ribonuclease (PARN) participates in steps leading to 18S pre-rRNA maturation in human cells PMID: 27899605
  8. we found a polyadenylation-dependent 3' end maturation pathway for the human telomerase RNA that relies on the nuclear poly(A)-binding protein PABPN1 and the poly(A)-specific RNase PARN. PMID: 26628368
  9. PARN increased telomerase RNA component levels by deadenylating telomerase RNA component, thereby limiting its degradation by EXOSC10. PMID: 26950371
  10. Large monoallelic mutations of PARN can cause developmental/mental illness. Biallelic PARN mutations cause severe bone marrow failure and central hypomyelination. PMID: 26342108
  11. results highlight the clinical significance of PARN and NOC on the survival in SCC diagnosed patients. PMID: 26541675
  12. Mutations in the PARN gene cause dyskeratosis congenital. PMID: 26482878
  13. The results indicate that the cellular level of miR-122 is determined by the balance between the opposing effects of GLD-2 and PARN/CUGBP1 on the metabolism of its 3'-terminus. PMID: 26130707
  14. 3 families with dyskeratosis congenita had key domain mutations in PARN shortening telomeres, reducing deadenylation, and downregulating TERC, DKC1, RTEL1, and TERF1. PMID: 25893599
  15. PARN and RTEL1 mutation carriers had shortened leukocyte telomere lengths. PMID: 25848748
  16. poly(A)-specific ribonuclease (PARN) was upregulated in gastric tumor tissues and gastric cancer cell lines MKN28 and AGS. PMID: 25499764
  17. Both R3H and RRM domains were essential for the high affinity of long poly(A) substrate. PMID: 23388391
  18. poly(A) polymerase Gld2, deadenylase PARN, and translation inhibitory factor neuroguidin (Ngd) are components of a dendritic CPEB-associated polyadenylation apparatus PMID: 22727665
  19. The atomic force microscopy images of single PARN molecules reveal compact ellipsoidal dimers (10.9 x 7.6 x 4.6nm). PMID: 21741754
  20. PARN harbors specificity for adenosine recognition in its active site and that the nucleotides surrounding the scissile bond are critical for adenosine recognition. PMID: 19901024
  21. residues of human PARN, Asp(28), Glu(30), Asp(292), and Asp(382), are essential for catalysis but are not required for stabilization of the PARN x RNA substrate complex. PMID: 11742007
  22. Results show that tristetraprolin can promote the deadenylation of AU-rich element (ARE)-containing, polyadenylated substrates by poly(A) RNase. PMID: 12748283
  23. study of binding and coordination of divalent metal ions in the active site of PARN PMID: 15358788
  24. The crystal structure of C-terminal truncated human PARN determined in two states (free and RNA-bound forms) reveals that PARN is folded into two domains, an R3H domain and a nuclease domain PMID: 16281054
  25. CUG-BP binds specifically to both of these RNAs and stimulates poly(A) shortening by PARN. Moreover, CUG-BP interacts with PARN in extracts by coimmunoprecipitation, and this interaction can be recapitulated using recombinant proteins PMID: 16601207
  26. The entire RNA-recognition motif (RRM) domain not only contributes to the substrate binding and efficient catalysis of PARN, but also stabilizes the overall structures of the protein. PMID: 17391638
  27. REsults describe the crystal structure of the poly(A)-specific ribonuclease (PARN)-RRM domain with a bound 7-methylguanosine triphosphate nucleotide, revealing a novel binding mode for the m(7)G cap. PMID: 18694759
  28. PARN is an allosteric enzyme, and potassium ions and the cap analogue are effectors with binding sites located at the RRM domain. PMID: 19103158
  29. Xenopus oocytes contain cytoplasmic (p62) and nuclear (p74) isoforms of PARN. p62 is proteolytically derived from p74. Both isoforms are expressed throughout oogenesis and early development. PMID: 11424938
  30. The m7GpppG cap has multiple effects on PARN activity. In cis, the 5'cap stimulates deadenylation by increasing PARN processivity. In trans, low concentrations of cap stimulate PARN activity whereas high concentrations inhibit deadenylation. PMID: 11359775
  31. PARN is a poly(A)-specific member of the RNase D family of 3' exoribonucleases. It is distributed between the nucleus and the cytoplasm and is not stably associated with ribosomes. Xenopus PARN catalyzes deadenylation during oocyte maturation. PMID: 9736620
  32. Deadenylation by the mammalian and amphibian poly(A)-specific exoribonuclease, PARN, is stimulated by the presence of an m(7)-guanosine cap on substrate RNAs. PARN exhibits intrinsic cap-binding activity. PMID: 10698948
  33. PARN binds to the 5' cap on substrate mRNAs. Cap-binding is stimulated by a poly(A) tail and competed by eIF4E. Cap-PARN interactions integrate regulated mRNA stability and translation. PMID: 10882133

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Involvement in disease Dyskeratosis congenita, autosomal recessive, 6 (DKCB6); Pulmonary fibrosis, and/or bone marrow failure, telomere-related, 4 (PFBMFT4)
Subcellular Location Nucleus, Cytoplasm, Nucleus, nucleolus
Protein Families CAF1 family
Tissue Specificity Ubiquitous.
Database Links

HGNC: 8609

OMIM: 604212

KEGG: hsa:5073

STRING: 9606.ENSP00000387911

UniGene: Hs.253197

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