SRE0112
Heat-labile Cod Uracil-DNA Glycosylase
recombinant, expressed in E. coli, Triton-free and Glycerol-free
别名:
UDG, UNG
General description
Uracil-DNA glycosylases are DNA repair enzymes that participate in the base excision repair pathway. UracilDNA Glycosylase, also known as UNG or 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 UNG gene.
Application
Heat-labile Cod Uracil-DNA Glycosylase eliminates carry-over contamination in PCR, RT-PCR, RT-qPCR, qPCR and RT-LAMP
Biochem/physiol Actions
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.
Features and Benefits
- 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
Preparation Note
In solution
Other Notes
This product is for R&D use only. Not for drug, household, or other uses.
存储类别
12 - Non Combustible Liquids
wgk
nwg
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
新产品
此项目有
Uracil-DNA glycosylases?structural and functional perspectives on an essential family of DNA repair enzymes
Schormann N, et al.
Protein Science, 23(12), 1667-1685 (2014)
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