|Application ||WB, E|
|Calculated MW||29862 Da|
|Antigen Region||43-71 aa|
|Other Names||Single-strand selective monofunctional uracil DNA glycosylase, 322-, SMUG1|
|Target/Specificity||This SMUG1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 43-71 amino acids from the N-terminal region of human SMUG1.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||SMUG1 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Recognizes base lesions in the genome and initiates base excision DNA repair. Acts as a monofunctional DNA glycosylase specific for uracil (U) residues in DNA with a preference for single-stranded DNA substrates. The activity is greater toward mismatches (U/G) compared to matches (U/A). Excises uracil (U), 5- formyluracil (fU) and uracil derivatives bearing an oxidized group at C5 [5-hydroxyuracil (hoU) and 5-hydroxymethyluracil (hmU)] in ssDNA and dsDNA, but not analogous cytosine derivatives (5- hydroxycytosine and 5-formylcytosine), nor other oxidized bases. The activity is damage-specific and salt-dependent. The substrate preference is the following: ssDNA > dsDNA (G pair) = dsDNA (A pair) at low salt concentration, and dsDNA (G pair) > dsDNA (A pair) > ssDNA at high salt concentration.|
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abgent to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
SMUG1 is a glycosylase that removes uracil from single- and double-stranded DNA in nuclear chromatin, thus contributing to base excision repair.
Arora, M., et al. Leukemia 24(8):1470-1475(2010)
Thyagarajan, B., et al. Biol. Blood Marrow Transplant. 16(8):1084-1089(2010)
Briggs, F.B., et al. Am. J. Epidemiol. 172(2):217-224(2010)
Chanson, A., et al. Am. J. Clin. Nutr. 89(6):1927-1936(2009)
Knaevelsrud, I., et al. Int. J. Radiat. Biol. 85(5):413-420(2009)
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