Recombinant Human U8 snoRNA-decapping enzyme (NUDT16)

Product Details

Abbreviation
NUDT16
Purity
>85% (SDS-PAGE)
Target Names
NUDT16
Uniprot NO.
Species
Homo sapiens (Human)
Source
Yeast
Expression Region
1-195
Target Protein Sequence
MAGARRLELG EALALGSGWR HACHALLYAP DPGMLFGRIP LRYAILMQMR FDGRLGFPGG FVDTQDRSLE DGLNRELREE LGEAAAAFRV ERTDYRSSHV GSGPRVVAHF YAKRLTLEEL LAVEAGATRA KDHGLEVLGL VRVPLYTLRD GVGGLPTFLE NSFIGSAREQ LLEALQDLGL LQSGSISGLK IPAHH
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.
Protein Length
full length protein
Tag Info
N-terminal His-tagged/Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Storage
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.
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.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Customer Reviews and Q&A

 Customer Reviews

Target Background

Function(From Uniprot)
RNA-binding and decapping enzyme that catalyzes the cleavage of the cap structure of snoRNAs and mRNAs in a metal-dependent manner. Part of the U8 snoRNP complex that is required for the accumulation of mature 5.8S and 28S rRNA. Has diphosphatase activity and removes m7G and/or m227G caps from U8 snoRNA and leaves a 5'monophosphate on the RNA. Catalyzes also the cleavage of the cap structure on mRNAs. Does not hydrolyze cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG). Also hydrolysis m7G- and m227G U3-capped RNAs but with less efficiencies. Has broad substrate specificity with manganese or cobalt as cofactor and can act on various RNA species. Binds to the U8 snoRNA; metal is not required for RNA-binding. May play a role in the regulation of snoRNAs and mRNAs degradation. Acts also as a phosphatase; hydrolyzes the non-canonical purine nucleotides inosine diphosphate (IDP) and deoxyinosine diphosphate (dITP) as well as guanosine diphosphate (GDP), deoxyguanosine diphosphate (dGDP), xanthine diphosphate (XDP), inosine triphosphate (ITP) and deoxyinosine triphosphate (ITP) to their respective monophosphate derivatives and does not distinguish between the deoxy- and ribose forms. The order of activity with different substrates is IDP > dIDP >> GDP = dGDP > XDP = ITP = dITP. Binds strongly to GTP, ITP and XTP. Participates in the hydrolysis of dIDP/IDP and probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions. Exhibits decapping activity towards NAD-capped RNAs and FAD-capped RNAs. Exhibits decapping activity towards dpCoA-capped RNAs in vitro.
Gene References into Functions
  1. hNudt16 hydrolysis of dinucleotide cap analogs and short capped oligonucleotides displayed a broader spectrum specificity than is currently known. PMID:29483298
  2. data suggest the existence in T-ALL of a disrupted RNA decapping pathway, mediated by the DNA methylation-associated loss of NUDT16, which contributes to the natural history of the disease by stabilizing transforming factors, such as is the case of the leukemogenic protein C-MYC PMID:28344317
  3. This study details structural and regulatory mechanisms explaining how substrates are selected for hydrolysis by human NUDT16. PMID:26121039
  4. The RNA decapping enzyme NUDT16 selectively degrades 5'-TOP mRNAs during Rift Valley fever virus infection and this decay is triggered in response to mTOR attenuation via the translational repressor 4EBP1/2 axis. PMID:26038567
  5. hNUDT16 can also actively cleave the mGDP cap from mRNAs in the presence of Mg(2)(+) or Mn(2)(+). PMID:21337011
  6. Like Dcp2, Nudt16 also regulates the stability of a subset of mRNAs including a member of the motin family of proteins involved in angiogenesis. PMID:21070968
  7. NUDT16 is a (deoxy)inosine diphosphatase that may function mainly in the nucleus to protect cells from deleterious effects of (d)ITP. PMID:20385596
  8. X29/H29K may be the nuclear counterparts of the cytoplasmic decapping machinery, localized in specialized bodies involved in RNA decay PMID:17567574
  9. Recombinant NUDT16, a decapping enzyme, has been crystallized. NUDT16 plays a pivotal role in U8 snoRNA stability. PMID:18607096

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Subcellular Location
Nucleus. Nucleus, nucleoplasm. Nucleus, nucleolus. Cytoplasm.
Protein Families
Nudix hydrolase family, NUDT16 subfamily
Tissue Specificity
Expressed strongly in lung, kidney, adrenal gland, testis, heart and brain.
Database Links

HGNC: 26442

UNIGENE: Hs.282050

KEGG: hsa:131870

STRING: 9606.ENSP00000422375

OMIM: 617381

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