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AB103059

Recombinant Human NUDT16 protein

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(2 Publications)

Recombinant Human NUDT16 protein is a Human Full Length protein, in the 1 to 195 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE, Mass Spec.

View Alternative Names

U8 snoRNA-decapping enzyme, IDP phosphatase, Inosine diphosphate phosphatase, Nucleoside diphosphate-linked moiety X motif 16, Nudix hydrolase 16, U8 snoRNA-binding protein H29K, m7GpppN-mRNA hydrolase, IDPase, Nudix motif 16, NUDT16

1 Images
SDS-PAGE - Recombinant Human NUDT16 protein (AB103059)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human NUDT16 protein (AB103059)

15% SDS-PAGE (3 μg)

Key facts

Purity

>95% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE, Mass Spec

applications

Biologically active

No

Accession

Q96DE0

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 10% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.316% Tris HCl, 0.0154% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "Mass Spec": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMAGARRLELGEALALGSGWRHACHALLYAPDPGMLFGRIPLRYAILMQMRFDGRLGFPGGFVDTQDRSLEDGLNRELREELGEAAAAFRVERTDYRSSHVGSGPRVVAHFYAKRLTLEELLAVEAGATRAKDHGLEVLGLVRVPLYTLRDGVGGLPTFLENSFIGSAREQLLEALQDLGLLQSGSISGLKIPAHH","proteinLength":"Full Length","predictedMolecularWeight":"23.4 kDa","actualMolecularWeight":null,"aminoAcidEnd":195,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q96DE0","tags":[{"tag":"His","terminus":"N-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

NUDT16 also known as diphosphatase is an enzyme that belongs to the nudix hydrolase family. It has a molecular mass of approximately 19 kDa. This enzyme cleaves diphosphate groups from nucleoside diphosphate derivatives. NUDT16 is highly expressed in several tissues including liver and testis. Its activity is important for maintaining cellular nucleotide pool balance by removing non-canonical nucleotides that can potentially be harmful if incorporated into DNA or RNA.
Biological function summary

NUDT16 functions to regulate nucleotide metabolism. It catalyzes the hydrolysis of nucleoside diphosphates like diadenosine tetraphosphate into monophosphates. NUDT16 often operates with other proteins in multi-enzyme complexes where it plays a role in modulating the concentrations of nucleoside diphosphates within cells. This activity coordinates the synthesis and degradation of nucleotides influencing cellular energy status and coenzyme levels.

Pathways

With regards to pathways NUDT16 integrates into nucleotide catabolism and salvage pathways. These pathways facilitate the conversion and recycling of nucleotides ensuring a steady supply for nucleic acid synthesis. NUDT16 interacts within these pathways alongside other key enzymes such as IMP dehydrogenase and GMP synthetase highlighting its role in controlling guanine nucleotide levels. This involvement provides a direct link to DNA replication and repair mechanisms which depend on the accurate control of nucleotide pools.

NUDT16 has connections to cancer and autoimmune diseases. Abnormal activity or expression of NUDT16 may contribute to the accumulation of atypical nucleotides potentially leading to mutations and genomic instability that characterize several cancer types. In autoimmune contexts altered NUDT16 function can impact immune cell activation and response. It exhibits an intriguing relationship with proteins like SAMHD1 a known regulator of nucleotide pools involved in immune responses and cancer.
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Specifications

Form

Liquid

Additional notes

ab103059 was purified using conventional chromatography techniques.

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General info

Function

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 (PubMed : 20385596, PubMed : 26121039). The order of activity with different substrates is IDP > dIDP >> GDP = dGDP > XDP = ITP = dITP (PubMed : 20385596). 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 (PubMed : 20385596). Exhibits decapping activity towards NAD-capped RNAs and FAD-capped RNAs (PubMed : 32432673). Exhibits decapping activity towards dpCoA-capped RNAs in vitro (By similarity).

Sequence similarities

Belongs to the Nudix hydrolase family. NUDT16 subfamily.

Subcellular localisation

Nucleus

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Product protocols

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Target data

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 (PubMed : 20385596, PubMed : 26121039). The order of activity with different substrates is IDP > dIDP >> GDP = dGDP > XDP = ITP = dITP (PubMed : 20385596). 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 (PubMed : 20385596). Exhibits decapping activity towards NAD-capped RNAs and FAD-capped RNAs (PubMed : 32432673). Exhibits decapping activity towards dpCoA-capped RNAs in vitro (By similarity).
See full target information NUDT16
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Publications (2)

Recent publications for all applications. Explore the full list and refine your search

Nucleic acids research 52:801-815 PubMed38000390

2023

DELTEX E3 ligases ubiquitylate ADP-ribosyl modification on nucleic acids.

Applications

Unspecified application

Species

Unspecified reactive species

Kang Zhu,Marcin J Suskiewicz,Chatrin Chatrin,Øyvind Strømland,Bryan W Dorsey,Vincent Aucagne,Dragana Ahel,Ivan Ahel

Science advances 8:eadd4253 PubMed36197986

2022

DELTEX E3 ligases ubiquitylate ADP-ribosyl modification on protein substrates.

Applications

Unspecified application

Species

Unspecified reactive species

Kang Zhu,Marcin J Suskiewicz,Andrea Hloušek-Kasun,Hervé Meudal,Andreja Mikoč,Vincent Aucagne,Dragana Ahel,Ivan Ahel
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