Uracil-DNA Glycosylase (UNG) (N-Term) antibody

Antigen: Uracil-DNA Glycosylase (UNG)

Synonyms: MGC108922, DGU, UDG, UNG1, UNG2, HIGM4, UNG15, DKFZp781L1143, UNG, MGC140717, MGC56102, zgc:56102, ECK2578, JW2564, SPS, MGC82673

Binding Site: N-Term

Clonality: Polyclonal

Host: Rabbit

Reactivity: Human, Hamster

Application: Western Blotting (WB), ELISA

Certificates: ISO 9001:2008

Catalog no.: ABIN653891

Additional Information

Alternative name: UNG

Gene ID: 7374

UniProt: P13051, NP_003353.1, NP_550433.1

Immunogen: This UNG antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 1-30 amino acids from the N-terminal region of human UNG.

Isotype: Ig

Description: Other names: UNG,UNG15, UNG1, DGU

Characteristics: Purified Rabbit Polyclonal Antibody (Pab)

Specificity: This UNG antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 1-30 amino acids from the N-terminal region of human UNG.

Molecular Weight: 34645 DA

Comments:

Background: This gene encodes one of several uracil-DNA glycosylases. One important function of uracil-DNA glycosylases is to prevent mutagenesis by eliminating uracil from DNA molecules by cleaving the N-glycosylic bond and initiating the base-excision repair (BER) pathway. Uracil bases occur from cytosine deamination or misincorporation of dUMP residues. Alternative promoter usage and splicing of this gene leads to two different isoforms: the mitochondrial UNG1 and the nuclear UNG2.

Application Details

Application Notes: The suggested dilution is: ELISA ~~ 1:1,000 Western blotting~~ 1:50~100

Concentration: 0.25 mg/ml

Purification: Purified

Buffer: Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.

Storage: Maintain refrigerated at 2-8 deg C for up to 6 months. For long term storage store at -20 deg C in small aliquots to prevent freeze-thaw cycles

Research Area: Signaling, Phospho-specific antibodies, Cell Signaling, Protein Modifications, Chromatin, Metabolism, Cell Structure

Restrictions: For Research Use only

Images

UNG Antibody (N-term) (ABIN653891) western blot analysis in MCF-7 cell line lysates (35ug/lane).This demonstrates the UNG antibody detected the UNG protein (arrow).

UNG Antibody (N-term) (ABIN653891) western blot analysis in CHO cell line lysates (35ug/lane).This demonstrates the UNG antibody detected the UNG protein (arrow).

UNG Antibody (N-term) (ABIN653891) flow cytometric analysis of MCF-7 cells (right histogram) compared to a negative control cell (left histogram).FITC-conjugated goat-anti-rabbit secondary antibodies were used for the analysis.

Publications

Product: Slupphaug, Olsen, Helland et al.: "Cell cycle regulation and in vitro hybrid arrest analysis of the major human uracil-DNA glycosylase." in: Nucleic acids research, Vol. 19, Issue 19, pp. 5131-7, 1991 (PubMed).

Olsen, Aasland, Wittwer et al.: "Molecular cloning of human uracil-DNA glycosylase, a highly conserved DNA repair enzyme." in: The EMBO journal, Vol. 8, Issue 10, pp. 3121-5, 1990 (PubMed).

Mol, Arvai, Slupphaug et al.: "Crystal structure and mutational analysis of human uracil-DNA glycosylase: structural basis for specificity and catalysis." in: Cell, Vol. 80, Issue 6, pp. 869-78, 1995 (PubMed).

Slupphaug, Markussen, Olsen et al.: "Nuclear and mitochondrial forms of human uracil-DNA glycosylase are encoded by the same gene." in: Nucleic acids research, Vol. 21, Issue 11, pp. 2579-84, 1993 (PubMed).

Nilsen, Otterlei, Haug et al.: "Nuclear and mitochondrial uracil-DNA glycosylases are generated by alternative splicing and transcription from different positions in the UNG gene." in: Nucleic acids research, Vol. 25, Issue 4, pp. 750-5, 1997 (PubMed).

Haug, Skorpen, Aas et al.: "Regulation of expression of nuclear and mitochondrial forms of human uracil-DNA glycosylase." in: Nucleic acids research, Vol. 26, Issue 6, pp. 1449-57, 1998 (PubMed).

Otterlei, Haug, Nagelhus et al.: "Nuclear and mitochondrial splice forms of human uracil-DNA glycosylase contain a complex nuclear localisation signal and a strong classical mitochondrial localisation signal, respectively." in: Nucleic acids research, Vol. 26, Issue 20, pp. 4611-7, 1998 (PubMed).

Beausoleil, Jedrychowski, Schwartz et al.: "Large-scale characterization of HeLa cell nuclear phosphoproteins." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 101, Issue 33, pp. 12130-5, 2004 (PubMed).

Ameratunga, Woon: "Customised molecular diagnosis of primary immune deficiency disorders in New Zealand: an efficient strategy for a small developed country." in: The New Zealand medical journal, Vol. 122, Issue 1304, pp. 46-53, 2009 (PubMed).