UNG KO cell lysate available now. Free of charge wild type control included. Knockout achieved by using CRISPR/Cas9, 2 bp deletion in exon1 and Insertion of the selection cassette in exon1.
DGU, DKFZp781L1143, HIGM 4, OTTHUMP00000240527, OTTHUMP00000240528, OTTHUMP00000240529, UDG, UNG 1, UNG 15, UNG2, UNG_HUMAN, Uracil DNA glycosylase 1, Uracil DNA glycosylase 2, Uracil-DNA glycosylase
UNG KO cell lysate available now. Free of charge wild type control included. Knockout achieved by using CRISPR/Cas9, 2 bp deletion in exon1 and Insertion of the selection cassette in exon1.
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Lysate preparation: Our lysates are made using RIPA buffer to which we add a protease inhibitor cocktail and phosphatase inhibitor cocktail (ratio: 300:100:10). This means that the protein of interest is denatured. If you require a native form of the protein please use the live cell version. Please refer to our lysis protocol for further details on how our lysates are prepared.
User storage instructions: Lyophilizate may be stored at 4°C. After reconstitution, store at -20°C for short-term storage or -80°C for long-term storage.
This product is subject to limited use licenses from The Broad Institute, ERS Genomics Limited and Sigma-Aldrich Co. LLC, and is developed with patented technology. For full details of the licenses and patents please refer to our limited use license and patent pages.
UNG which stands for Uracil-DNA glycosylase is an enzyme that functions mechanically to remove uracil from DNA. This preventive action is necessary because uracil can result from the deamination of cytosine or due to misincorporation during DNA replication. UNG exhibits a mass of approximately 33 kDa and shows expression in various tissues underlining its importance across different cellular environments. UNG is ubiquitously expressed but displays higher activity in proliferating cells making it integral during cell division.
URACIL-DNA glycosylase engages in base excision repair (BER) an important DNA repair process. This enzyme initiates the repair by excising uracil bases creating an abasic site subsequently processed by other repair proteins. UNG actively functions within single-enzymatic action but also associates with various DNA repair complexes highlighting its multifaceted role in genome maintenance. It guards against mutations by maintaining DNA integrity reducing the risk errors pose to genetic stability.
UNG plays a role in DNA repair and cell cycle pathways contributing essential actions to genomic stability and cell proliferation. Specifically it integrates into the base excision repair pathway working alongside other proteins like APEX1 and DNA polymerase beta to ensure proper repair of damaged DNA. These related proteins cooperate to fix abasic sites that arise after UNG's glycosylase activity ensuring that genetic information remains accurate and undamaged as cells replicate.
Mutations in UNG can present increased susceptibility to immunodeficiency and cancer. One such disorder includes hyper-IgM syndrome a condition where BER defects lead to an impaired immune response. Proteins like CD40 and CD40L intersect with UNG-related pathways impacting germinal center reactions and immunoglobulin isotype switching. The enzyme's dysfunction potentially contributes to the accumulation of genetic errors fostering oncogenesis in several cancers by allowing abnormal cells to escape normal regulatory mechanisms.
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Allele-2: Insertion of the selection cassette in exon1
Allele-1: 2 bp deletion in exon1
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