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SAB4200044

Sigma-Aldrich

Anti-dUTPase antibody, Rat monoclonal

clone HUTP 3E6, purified from hybridoma cell culture

Synonym(s):

Anti-DUT, Anti-Deoxyuridine triphosphatase, Anti-Deoxyuridine triphosphate nucleotidohydrolase, Anti-dUTP pyrophosphatase, Monoclonal Anti-dUTPase antibody produced in rat

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rat

conjugate

unconjugated

antibody form

purified from hybridoma cell culture

antibody product type

primary antibodies

clone

HUTP 3E6, monoclonal

form

buffered aqueous solution

mol wt

antigen ~22 kDa

species reactivity

mouse, marmoset, human

packaging

antibody small pack of 25 μL

technique(s)

immunocytochemistry: suitable
immunoprecipitation (IP): suitable
western blot: 0.25-0.5 μg/mL using using Raji cell extracts

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... DUT(1854)

General description

Deoxyuridine triphosphate nucleotidohydrolase (dUTPase) maintains the genomic integrity of cells. This enzyme is a symmetrical trimer with 152 amino acids.
Monoclonal Anti-dUTPase (rat IgG2a isotype) is derived from the hybridoma HUTP 3E6 produced by the fusion of mouse myeloma cells (P3X63Ag8.653) and splenocytes from a rat immunized with protein. The DUT gene is mapped on the human chromosome at 15q21.1.

Specificity

Monoclonal Anti-dUTPase recognizes human, mouse and marmoset dUTPase.

Immunogen

human dUTPase protein.

Application

Monoclonal Anti-dUTPase antibody produced in rat may be used in:
  • immunoblotting
  • immunoprecipitation
  • immunocytochemistry

Biochem/physiol Actions

Deoxyuridine triphosphate nucleotidohydrolase (dUTPase) hydrolyses dUTP to dUMP and pyrophosphate and promotes nucleotide metabolism. Epstein-Barr virus (EBV) encoded dUTP plays a crucial role in pathophysiology of EBV related diseases, by regulating cellular microenvironment. It is used as a target for anticancer chemotherapy.
Elevated levels of dUTP lead to increased incorporation of uracil into DNA, which induces extensive excision repair mediated by uracil glycosylase. This repair process, resulting in the removal and reincorporation of dUTP, is self-defeating and leads to DNA fragmentation and cell death.

Physical form

Solution in 0.01M phosphate buffered saline pH 7.4, containing 15 mM sodium azide.

Storage and Stability

Store at -20 °C. For continuous use, the product may be stored at 2-8 °C for up to one month. For extended storage, freeze at -20 °C in working aliquots. Repeated freezing and thawing, or storage in “frost-free” freezers, is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilution samples should be discarded if not used within 12 hours.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class Code

10 - Combustible liquids

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

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Epstein-Barr virus encoded dUTPase containing exosomes modulate innate and adaptive immune responses in human dendritic cells and peripheral blood mononuclear cells
Ariza M, et al.
PLoS ONE, 8(7), e69827-e69827 (2013)
Kinetic mechanism of human dUTPase, an essential nucleotide pyrophosphatase enzyme
Toth J, et al.
Test, 282(46), 33572-33582 (2007)
Hideki Makishima et al.
Blood, 117(21), e198-e206 (2011-02-25)
Progression of chronic myelogenous leukemia (CML) to accelerated (AP) and blast phase (BP) is because of secondary molecular events, as well as additional cytogenetic abnormalities. On the basis of the detection of JAK2, CBL, CBLB, TET2, ASXL1, and IDH1/2 mutations
J Fleischmann et al.
International journal of cancer, 84(6), 614-617 (1999-11-24)
We report the generation of 2 monoclonal antibodies (MAbs), 2B12 and 3E6, suitable for the detection of human dUTPase in routinely processed paraffin sections by immunohistochemistry. Using these MAbs, we observed nuclear expression of dUTPase in the proliferation zones of
Kinetic properties and specificity of trimeric Plasmodium falciparum and human dUTPases
Quesada-Soriano I, et al.
Biochimie, 92(2), 178-186 (2010)

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