UNG Antibody

Uracil-DNA glycosylase (UNG), also known as UDG, is a crucial enzyme involved in the base-excision repair (BER) pathway. Its primary function is to prevent mutagenesis by eliminating uracil from DNA molecules. This enzyme is essential for maintaining genomic stability and integrity.

Uracil can be erroneously incorporated into DNA through the deamination of cytosine or the misincorporation of dUMP residues. If not corrected, these uracil residues can lead to mutations during DNA replication. UNG excises uracil from DNA by cleaving the N-glycosidic bond, thereby initiating the BER pathway .

The enzyme operates through a “pinch-push-pull” mechanism, which involves five highly conserved motifs that collectively catalyze the glycosidic bond cleavage . These motifs include:

• Water-activating loop: 63-QDPYH-67
• Pro-rich loop: 165-PPPPS-169
• Uracil-binding motif: 199-GVLLLN-204
• Gly-Ser loop: 246-GS-247
• Minor groove intercalation loop: 268-HPSPLS-273

UNG is composed of a four-stranded parallel β-sheet surrounded by eight α-helices. The active site of the enzyme is highly conserved and is responsible for its high efficiency and specificity in repairing damaged DNA .

Mouse anti-human antibodies are commonly used in research to detect and study human proteins. The mouse monoclonal antibody against human UNG is an unconjugated antibody that has been validated for use in immunofluorescence (IF), immunohistochemistry (IHC), and western blotting (WB) . These antibodies are essential tools for studying the expression, localization, and function of UNG in various biological contexts.

The study of UNG and its interactions with other proteins is crucial for understanding the mechanisms of DNA repair and the prevention of mutagenesis. The mouse anti-human UNG antibody is particularly useful in research focused on cancer, as alterations in DNA repair pathways are often associated with tumorigenesis .