Uracil-DNA Glycosylase (UNG) (AA 281-298), (AA 290-307) antibody

Details for Product No. ABIN123481
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Antigen
Synonyms DGU, HIGM4, HIGM5, UDG, UNG1, UNG15, UNG2, ung, zgc:56102, PSPTO4236, BA5648, ECK2578, JW2564, An02g14790, AO090001000732, DDBDRAFT_0204444, DDBDRAFT_0214910, DDB_0204444, DDB_0214910
Epitope
AA 281-298, AA 290-307
(12), (11), (7), (5), (4), (2), (2), (1), (1), (1), (1), (1), (1)
Reactivity
Dog (Canine), Chimpanzee, Chicken, Human, Mouse (Murine), Rabbit, Rat (Rattus), Xenopus laevis, Zebrafish (Danio rerio)
(81), (42), (40)
Host
Rabbit
(56), (26)
Clonality
Polyclonal
Application
Western Blotting (WB), Immunohistochemistry (Paraffin-embedded Sections) (IHC (p))
(76), (50), (25), (14), (4), (3), (2), (2), (2), (2), (1)
Pubmed 5 references available
Catalog no. ABIN123481
Quantity 0.1 mg
Price
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Immunogen A synthetic peptide sequence CRHFSKTNELLQKSGKKP corresponding to amino acids 281-298 of human UNG1 (NP 003353.1) and amino acids 290-307 of human UNG2 (NP 550433.1).
Purification Protein G Chromatography
Background The human UNG gene encodes both nuclear (UNG2) and mitochondrial (UNG1) forms of uracil- DNA glycosylase. These forms are generated by alternative splicing and the use of two differentially regulated promoters, PA and PB (2, 3) The cDNAs for UNG1 and UNG2 are of similar size (2061 and 2058 bp, respectively) and as a result the corresponding mRNAs are not resolved as two species in gel electrophoresis (5). Nuclear UNG2 differs from mitochondrial UNG1 in 44 amino acids of the N-terminal sequence that is not necessary for catalytic activity. A major role of the UNG gene products is to repair mutagenic U:G mispairs caused by cytosine deamination. For example, UNG2 removes misincorporated dUMP residues. The level and expression pattern of UNG1 and UNG2 differs between cell and tissue type (5). Additionally, the expression of UNG is cell cycle regulated (Nagelhus et al. 1995). The expression and activity of UNG has been found in general to be higher in proliferating as compared to nonproliferating tissues and cells (reviewed in Kruman et al. 2004). UNG1 is a 304 amino acid protein. UNG2 is a 313 amino acid protein.
UniProt P13051
Application Notes Western blot (2 ug/ml). HeLa cell lysate can be used as positive control. Other applications not tested. Optimal dilutions are dependent on conditions and should be determined by the user. Further Comments: The specificity of this antibody has been validated by antisense UNG oligonucleotide (Kruman et al. 2004).
Restrictions For Research Use only
Format Liquid
Concentration 0.5 mg/mL
Buffer PBS containing 0.05% BSA and 0.05% Sodium Azide
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Storage Comment Stable at 2-8°C for up to one month or at -20°C for longer. Avoid repeated freezing and thawing. Shelf Life: one year from despatch.
Expiry Date 12 months
Supplier Images
anti-Uracil-DNA Glycosylase (UNG) (AA 281-298), (AA 290-307) antibody Detection of UNG in HeLa cell lysate with anti-UNG pcAb at 2 ug/ml dilution.
General 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).

Bharati, Krokan, Kristiansen et al.: "Human mitochondrial uracil-DNA glycosylase preform (UNG1) is processed to two forms one of which is resistant to inhibition by AP sites." in: Nucleic acids research, Vol. 26, Issue 21, pp. 4953-9, 1998 (PubMed).

Nilsen, Rosewell, Robins et al.: "Uracil-DNA glycosylase (UNG)-deficient mice reveal a primary role of the enzyme during DNA replication." in: Molecular cell, Vol. 5, Issue 6, pp. 1059-65, 2000 (PubMed).

Krokan, Otterlei, Nilsen et al.: "Properties and functions of human uracil-DNA glycosylase from the UNG gene." in: Progress in nucleic acid research and molecular biology, Vol. 68, pp. 365-86, 2001 (PubMed).

Hosts (56), (26)
Reactivities (81), (42), (40)
Applications (76), (50), (25), (14), (4), (3), (2), (2), (2), (2), (1)
Epitopes (12), (11), (7), (5), (4), (2), (2), (1), (1), (1), (1), (1), (1)
Request Want additional data for this product?

The Independent Validation Initiative strives to provide you with high quality data. Find out more

Add to Basket

Order hotline:

  • +1 404 474 4654
  • +1 888 205 9894 (TF)
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