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AB173062

Recombinant Human dUTPase protein - BSA and Azide free

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(1 Publication)

Recombinant Human dUTPase protein - BSA and Azide free is a Human Full Length protein, in the 1 to 164 aa range, expressed in Escherichia coli, with >95%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE, HPLC.

View Alternative Names

dUTPase, dUTP pyrophosphatase, DUT

Key facts

Purity

>95% SDS-PAGE

Endotoxin level

< 1 EU/µg

Expression system

Escherichia coli

Tags

Tag free

Applications

HPLC, SDS-PAGE

applications

Biologically active

No

Accession

P33316

Animal free

No

Carrier free

Yes

Species

Human

Storage buffer

pH: 7.4 Constituents: PBS

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>" }, "HPLC": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"MPCSEETPAISPSKRARPAEVGGMQLRFARLSEHATAPTRGSARAAGYDLYSAYDYTIPPMEKAVVKTDIQIALPSGCYGRVAPRSGLAAKHFIDVGAGVIDEDYRGNVGVVLFNFGKEKFEVKKGDRIAQLICERIFYPEIEEVQALDDTERGSGGFGSTGKN","proteinLength":"Full Length","predictedMolecularWeight":"26 kDa","actualMolecularWeight":null,"aminoAcidEnd":164,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P33316","tags":[]}]
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Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-20°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.

The enzyme deoxyuridine triphosphatese also known as dUTPase hydrolyzes dUTP to dUMP and inorganic pyrophosphate. It prevents the incorporation of uracil into DNA which can lead to mutations. The molecular mass of human dUTPase is about 18-20 kDa. It is widely expressed in both prokaryotic and eukaryotic cells including places like the thymus and spleen where DNA synthesis is very active. Alternative names such as DUT or dUTP pyrophosphatase are often used to refer to this enzyme.
Biological function summary

DUTPase maintains nucleotide pool balance and genome integrity. By converting dUTP to dUMP it provides substrates for thymidylate synthase to produce thymidine triphosphate (dTTP) which is essential for DNA replication and repair. dUTPase is not typically part of a larger protein complex but cooperates with other enzymes in nucleotide metabolism. Its activity protects cells from apoptosis that might occur due to extensive uracil misincorporation.

Pathways

DUTPase plays a role in nucleotide metabolism and one-carbon metabolism pathways. It regulates the pyrimidine metabolism pathway ensuring sufficient dTTP levels for DNA synthesis. dUTPase interacts indirectly with proteins like thymidylate synthase and dihydrofolate reductase through these pathways. These interactions aid in maintaining a steady supply of nucleotides important for DNA replication and repair.

Impairments in dUTPase function can relate to cancer and immunodeficiency disorders. In some cancers altered dUTPase expression affects the sensitivity to chemotherapeutic agents particularly those targeting thymidylate synthesis. In certain immunodeficiencies dUTPase malfunction leads to increased uracil incorporation compromising DNA integrity. The enzyme connects with proteins such as thymidylate synthase in these diseases due to its role in managing nucleotide pools critical for cell proliferation.
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Specifications

Form

Liquid

Additional notes

Greater than 95% as determined by SEC-HPLC and reducing SDS-PAGE.

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General info

Function

Catalyzes the cleavage of 2'-deoxyuridine 5'-triphosphate (dUTP) into 2'-deoxyuridine 5'-monophosphate (dUMP) and inorganic pyrophosphate and through its action efficiently prevents uracil misincorporation into DNA and at the same time provides dUMP, the substrate for de novo thymidylate biosynthesis (PubMed : 17880943, PubMed : 8631816, PubMed : 8805593). Inhibits peroxisome proliferator-activated receptor (PPAR) activity by binding of its N-terminal to PPAR, preventing the latter's dimerization with retinoid X receptor (By similarity). Essential for embryonic development (By similarity).

Sequence similarities

Belongs to the dUTPase family.

Post-translational modifications

Nuclear isoform 2 is phosphorylated in vivo on Ser-11, a reaction that can be catalyzed in vitro by CDC2. Phosphorylation in mature T-cells occurs in a cell cycle-dependent manner. Isoform 3 is not phosphorylated.

Subcellular localisation

Nucleus

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Product protocols

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Target data

Catalyzes the cleavage of 2'-deoxyuridine 5'-triphosphate (dUTP) into 2'-deoxyuridine 5'-monophosphate (dUMP) and inorganic pyrophosphate and through its action efficiently prevents uracil misincorporation into DNA and at the same time provides dUMP, the substrate for de novo thymidylate biosynthesis (PubMed : 17880943, PubMed : 8631816, PubMed : 8805593). Inhibits peroxisome proliferator-activated receptor (PPAR) activity by binding of its N-terminal to PPAR, preventing the latter's dimerization with retinoid X receptor (By similarity). Essential for embryonic development (By similarity).
See full target information DUT
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Publications (1)

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

Nucleic acids research 48:264-277 PubMed31647103

2019

Inactivation of folylpolyglutamate synthetase Met7 results in genome instability driven by an increased dUTP/dTTP ratio.

Applications

Unspecified application

Species

Unspecified reactive species

Tobias T Schmidt,Sushma Sharma,Gloria X Reyes,Anna Kolodziejczak,Tina Wagner,Brian Luke,Anders Hofer,Andrei Chabes,Hans Hombauer
View all publications
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Product promise

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