Abcam, ab132162, Recombinant Human SMUG1 protein

Size: 10µg
Recombinant Human SMUG1 protein is a Human Full Length protein, in the 1 to 177 aa range, expressed in Wheat germ, suitable for SDS-PAGE, ELISA, WB.
Key facts
Expression system:Wheat germ,
Tags:GST tag N-Terminus,
Applications:ELISA, WB, SDS-PAGESee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:No,
Accession:Q53HV7,
Animal free:No,
Carrier free:No,
Species:Human,
Storage buffer:pH: 8Constituents: 0.79% Tris HCl, 0.31% Glutathione

Properties and Storage Information:
Shipped at conditions-Dry Ice, Appropriate short-term storage conditions--80°C, Appropriate long-term storage conditions--80°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
SMUG1 also known as Single-strand-selective Monofunctional Uracil-DNA Glycosylase 1 plays a role in DNA repair mechanisms. It is an enzyme involved in the base excision repair (BER) pathway specializing in the removal of uracil from single-stranded DNA. SMUG1 has a molecular weight of about 33 kDa. The protein is expressed in various tissues with notable presence in the brain liver and lung. Its expression levels adjust according to the tissue's need for active DNA repair.
Biological function summary
The process of DNA metabolism relies heavily on mechanisms related to the SMUG1 enzyme. As part of the DNA repair machinery it identifies and excises uracil bases from DNA which result from deamination of cytosine or misincorporation during DNA synthesis. SMUG1 does not function within a larger protein complex but interacts dynamically with other repair proteins like AP endonucleases. This activity helps maintain genomic stability by preventing mutations that could arise from uracil incorporation.
Pathways
SMUG1 contributes importantly to the base excision repair pathway an important process for DNA maintenance. This pathway addresses small non-helix-distorting base lesions such as deaminated oxidized or alkylated bases. Within this pathway SMUG1's activity aligns with other glycosylases and the APEX1 protein which processes the abasic sites left after SMUG1 removes uracil. Furthermore SMUG1's function supports the overall cellular DNA damage response signaling when repair and further processing are necessary.
Alterations in the SMUG1 protein have connections to cancer and neurodegeneration. Loss of SMUG1 activity may result in accumulation of mutations due to unprocessed uracil in the DNA contributing to tumorigenesis. In particular studies have shown links between SMUG1 and glioma where defective DNA repair mechanisms escalate mutation rates. Also in neurodegenerative disorders it contributes directly through genomic instability with connections to APEX1 showing potential overlapping repair functions critical for neuron maintenance.