Rabbit Polyclonal UNG antibody. Suitable for WB and reacts with Human samples. Immunogen corresponding to Synthetic Peptide within Human UNG aa 250 to C-terminus.
pH: 7 - 8
Preservative: 0.09% Sodium azide
Constituents: Tris citrate/phosphate
WB | |
---|---|
Human | Tested |
Species | Dilution info | Notes |
---|---|---|
Species Human | Dilution info 1/2000.00000 - 1/10000.00000 | Notes - |
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Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
DGU, UNG1, UNG15, UNG, Uracil-DNA glycosylase, UDG
Rabbit Polyclonal UNG antibody. Suitable for WB and reacts with Human samples. Immunogen corresponding to Synthetic Peptide within Human UNG aa 250 to C-terminus.
pH: 7 - 8
Preservative: 0.09% Sodium azide
Constituents: Tris citrate/phosphate
ab245630 was affinity purified using an epitope specific to UNG immobilized on solid support.
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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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This species and application combination has not been tested, but we predict it will work based on strong homology. However, this combination is not covered by our product promise.
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All lanes: Western blot - Anti-UNG antibody (ab245630) at 0.1 µg/mL
Lane 1: HeLa (human epithelial cell line from cervix adenocarcinoma) whole cell lysate at 50 µg
Lane 2: HeLa whole cell lysate at 15 µg
Lane 3: HeLa whole cell lysate at 5 µg
Lane 4: HEK-293T (human epithelial cell line from embryonic kidney transformed with large T antigen) whole cell lysate at 50 µg
Developed using the ECL technique.
Predicted band size: 35 kDa
Exposure time: 3min
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