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SRE0111

Sigma-Aldrich

Heat-labile Cod Uracil-DNA Glycosylase

recombinant, expressed in E. coli, Triton-free

同義詞:

UDG, UNG

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About This Item

分類程式碼代碼:
41106300
NACRES:
NA.54

重組細胞

expressed in E. coli

品質等級

成份

Triton-free

包裝

pkg of 100 U
pkg of 1000 U

運輸包裝

dry ice

儲存溫度

−20°C

一般說明

Uracil-DNA glycosylases are DNA repair enzymes that participate in the base excision repair pathway. Uracil DNA Glycosylase, also known as UNGor UDG, is an enzyme that hydrolyses the N-glycosylic bond between the deoxyribose sugar and the base in uracil-containing DNA leaving an abasic(apyrimidinic) site in DNA. Contamination of PCR samples with amplicon DNA generated by previous reactions, “carry-over contamination”, is one of the major sources of false positive results. Heat-labile Cod Uracil-DNA Glycosylase prevents carry-over contamination in PCR, qPCR, RT-qPCR, and RT-LAMP assays. The enzyme is produced in a recombinant E. coli (ung–) strain that contains a modified Cod UNGgene.

應用

Heat-labile Cod Uracil-DNA Glycosylase eliminates carry-over contamination in PCR, RT-PCR, RT-qPCR, qPCR and RT-LAMP

特點和優勢

  • Heat inactivation: The only UNG that is completely and irreversibly heat inactivated thus ensuring long-term sample integrity for subsequent post-PCR analysis such as cloning, sequencing or genotyping
  • Cod UNG is not active on uracil in RNA.
  • High sensitivity: Remove more than 108 copies of contaminating DNA without affecting the sensitivity (Cq) of the assay
  • Simple protocol: Applying Cod UNG in a RT-PCR is done by a 5 min Cod UNG preincubation step at RT prior to the amplification reaction

單位定義

One Unit is defined as the amount of enzyme that liberates 1 nmol Uracil per hour from Uracil-labelled DNA at 37 °C in 70 mm Tris-HCI pH 8.0 (@25 °C), 10 mM NaCI, 1 mM EDTA and 0.1 mg/ml BSA.

重構

In solution

其他說明

This product is for R&D use only. Not for drug, household, or other uses.

儲存類別代碼

12 - Non Combustible Liquids

水污染物質分類(WGK)

WGK 1

閃點(°F)

Not applicable

閃點(°C)

Not applicable


分析證明 (COA)

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存取文件庫

Uracil-DNA glycosylases?Structural and functional perspectives on an essential family of DNA repair enzymes
N Schormann et al.
Protein Science, 1667?1685-1667?1685 (2014)

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