PARN Antibody, Biotin conjugated

Code CSB-PA017456LD01HU
Size US$166
Order now
Have Questions? Leave a Message or Start an on-line Chat

Product Details

Full Product Name
Rabbit anti-Homo sapiens (Human) PARN Polyclonal antibody
Uniprot No.
Target Names
PARN
Alternative Names
DAN antibody; Deadenylating nuclease antibody; Deadenylation nuclease antibody; PARN antibody; PARN_HUMAN antibody; Poly A specific ribonuclease antibody; Poly(A) specific ribonuclease antibody; Poly(A)-specific ribonuclease PARN antibody; Polyadenylate specific ribonuclease antibody; Polyadenylate-specific ribonuclease antibody
Raised in
Rabbit
Species Reactivity
Human
Immunogen
Recombinant Human Poly(A)-specific ribonuclease PARN protein (1-639AA)
Immunogen Species
Homo sapiens (Human)
Conjugate
Biotin
Clonality
Polyclonal
Isotype
IgG
Purification Method
>95%, Protein G purified
Concentration
It differs from different batches. Please contact us to confirm it.
Buffer
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, PH 7.4
Form
liquid
Tested Applications
ELISA
Protocols
Troubleshooting and FAQs
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Lead Time
Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

Customer Reviews and Q&A

 Customer Reviews

There are currently no reviews for this product.

Submit a Review here

Target Background

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. Also able to recognize and trim poly(A) tails of microRNAs such as MIR21 and H/ACA box snoRNAs (small nucleolar RNAs) leading to microRNAs degradation or snoRNA increased stability.
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

Show More

Hide All

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. Note=Some nuclear fraction is nucleolar.
Protein Families
CAF1 family
Tissue Specificity
Ubiquitous.
Database Links

HGNC: 8609

OMIM: 604212

KEGG: hsa:5073

STRING: 9606.ENSP00000387911

UniGene: Hs.253197

icon of phone
Call us
301-363-4651 (Available 9 a.m. to 5 p.m. CST from Monday to Friday)
icon of address
Address
7505 Fannin St., Ste 610, Room 7 (CUBIO Innovation Center), Houston, TX 77054, USA
icon of social media
Join us with

Subscribe newsletter

Leave a message

* To protect against spam, please pass the CAPTCHA test below.
CAPTCHA verification
© 2007-2024 CUSABIO TECHNOLOGY LLC All rights reserved. 鄂ICP备15011166号-1
webinars: DT3C facilitates antibody internalization X
Place an order now

I. Product details

*
*
*
*

II. Contact details

*
*

III. Ship To

*
*
*
*
*
*
*

IV. Bill To

*
*
*
*
*
*
*
*