UDG Antibody (B-7): sc-390255

UDG Antibody (B-7) is a mouse monoclonal IgG2a kappa light chain antibody that detects UDG protein of mouse, rat, and human origin by western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), and enzyme-linked immunosorbent assay (ELISA). UDG monoclonal antibody (B-7) is available in both non-conjugated and various conjugated forms, including agarose, horseradish peroxidase (HRP), phycoerythrin (PE), fluorescein isothiocyanate (FITC), and multiple Alexa Fluor® conjugates. Uracil-DNA glycosylase (UDG) plays a critical role in maintaining genomic integrity by excising uracil from DNA, which can arise from misincorporation during DNA replication or from cytosine deamination. This enzymatic activity is essential for preventing mutations that could lead to various diseases, including cancer. UDG operates through a unique mechanism where UDG undergoes a conformational change from an "open" state to a "closed" state upon binding to DNA, which facilitates the cleavage of the glycosidic bond between uracil and deoxyribose. This conformational shift creates a catalytic center that enhances UDG′s ability to flip the uridine nucleotide into the active site for efficient excision. UDG exists in two isoforms, UDG1 and UDG1A, with UDG1 localized to the mitochondria and UDG1A, which features a distinct 44-residue amino-terminal extension, localized to the nucleus, highlighting UDG′s diverse functional roles within different cellular compartments.

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UDG Antibody (B-7) References:

1. Protein mimicry of DNA from crystal structures of the uracil-DNA glycosylase inhibitor protein and its complex with Escherichia coli uracil-DNA glycosylase.  |  Putnam, CD., et al. 1999. J Mol Biol. 287: 331-46. PMID: 10080896
2. Quality control by DNA repair.  |  Lindahl, T. and Wood, RD. 1999. Science. 286: 1897-905. PMID: 10583946
3. Uracil-DNA glycosylase-DNA substrate and product structures: conformational strain promotes catalytic efficiency by coupled stereoelectronic effects.  |  Parikh, SS., et al. 2000. Proc Natl Acad Sci U S A. 97: 5083-8. PMID: 10805771
4. Expression of uracil DNA glycosylase (UDG) does not affect cellular sensitivity to thymidylate synthase (TS) inhibition.  |  Welsh, SJ., et al. 2003. Eur J Cancer. 39: 378-87. PMID: 12565992
5. Chromosomal assignment of human uracil-DNA glycosylase to chromosome 12.  |  Aasland, R., et al. 1990. Genomics. 7: 139-41. PMID: 2335354
6. Uracil DNA glycosylase (UDG) activities in Bradyrhizobium diazoefficiens: characterization of a new class of UDG with broad substrate specificity.  |  Chembazhi, UV., et al. 2017. Nucleic Acids Res. 45: 5863-5876. PMID: 28369586
7. Sensitive detection of uracil-DNA glycosylase (UDG) activity based on terminal deoxynucleotidyl transferase-assisted formation of fluorescent copper nanoclusters (CuNCs).  |  Liu, G., et al. 2019. Talanta. 195: 320-326. PMID: 30625549
8. A highly sensitive method for simultaneous detection of hAAG and UDG activity based on multifunctional dsDNA probes mediated exponential rolling circle amplification.  |  Fan, L., et al. 2021. Talanta. 232: 122429. PMID: 34074415
9. Properties of a recombinant human uracil-DNA glycosylase from the UNG gene and evidence that UNG encodes the major uracil-DNA glycosylase.  |  Slupphaug, G., et al. 1995. Biochemistry. 34: 128-38. PMID: 7819187
10. A nucleotide-flipping mechanism from the structure of human uracil-DNA glycosylase bound to DNA.  |  Slupphaug, G., et al. 1996. Nature. 384: 87-92. PMID: 8900285
11. Base excision repair enzyme family portrait: integrating the structure and chemistry of an entire DNA repair pathway.  |  Parikh, SS., et al. 1997. Structure. 5: 1543-50. PMID: 9438868
12. Base excision repair initiation revealed by crystal structures and binding kinetics of human uracil-DNA glycosylase with DNA.  |  Parikh, SS., et al. 1998. EMBO J. 17: 5214-26. PMID: 9724657

Monoclonal antibodies for mammalian and non-mammalian protein targets represent essentially all targets covered by polyclonal antibodies. Over 8,300 of our antibodies are offered as ImmunoCruz^® conjugates which eliminates the need for a secondary antibody.

Santa Cruz Biotechnology antibodies have over 360,000 research citations. Anti-UDG Antibody (B-7) has 1 citations in a variety of scientific publications.

Primary antibodies like Anti-UDG Antibody (B-7) for mammalian target proteins are recommended for the detection of a range of mammalian species, primarily of mouse, rat and human species. Many mammalian antibodies are also ideal for veterinary research and reactive with ovine, porcine, caprine, feline, canine, bovine and equine protein targets. Santa Cruz Biotechnology primary monoclonal antibodies are suitable for laboratory research applications and are not intended for diagnostic or therapeutic use.

UDG Antibody (B-7) Specifications

Alternate Product Name: UDG

Product Clone Name: B-7

Classification: Primary Antibody

Clonality: Monoclonal Antibody

Antibody Isotype: IgG_2a kappa light chain

Amino Acids: 67-313

Epitope Target: UDG

Epitope Species: human

Product Reactivity/Detection: UDG isoforms 1 and 2

Species Reactivity/Detection: mouse, rat, human

Additional Mammalian Reactivity: N/A

Additional Non-Mammalian Reactivity: N/A

Applications: WB, IP, IF, ELISA

Vialing Information: Each vial contains 200 µg IgG_2a kappa light chain in 1.0 ml of PBS with < 0.1% sodium azide and 0.1% gelatin

Research Citations: 1 citations in various scientific publications

Available Conjugates/Forms for UDG Antibody (B-7): AC: Agarose, AF488: Alexa Fluor^® 488, AF546: Alexa Fluor^® 546, AF594: Alexa Fluor^® 594, AF647: Alexa Fluor^® 647, AF680: Alexa Fluor^® 680, AF790: Alexa Fluor^® 790, FITC: Fluoroscein, HRP: Horseradish Peroxidase, PE: Phycoerythrin