The image on the left is immunohistochemistry of paraffin-embedded Human Lymphoma tissue using CSB-PA658038(MPG Antibody) at dilution 1/40, on the right is treated with fusion protein. (Original magnification: ×200)
Gel: 8%SDS-PAGE, Lysate: 40 μg, Lane 1-2: Lovo cells, PC3 cells, Primary antibody: CSB-PA658038(MPG Antibody) at dilution 1/950, Secondary antibody: Goat anti rabbit IgG at 1/8000 dilution, Exposure time: 1 minute
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
貨期:
Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
用途:
For Research Use Only. Not for use in diagnostic or therapeutic procedures.
Hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine, and 7-methylguanine from the damaged DNA polymer formed by alkylation lesions.
基因功能參考文獻:
high levels of APNG were associated with better overall survival in patients with glioblastoma PMID: 28662073
Data indicate that DNA glycosylases MYH, UNG2, MPG, NTH1, NEIL1, 2 and 3 on nascent DNA. PMID: 28575236
Data suggest that the change in tryptophan fluorescence of Y162W mutant of AAG (alkyladenine DNA glycosylase) is extremely rapid upon binding to either damaged or undamaged DNA, much faster than lesion-recognition and nucleotide flipping steps; thus, intercalation by tyrosine may be one of the earliest steps in search for/recognition of DNA damage. PMID: 28747435
Rheumatoid arthritis is associated with a polymorphism in the MPG gene (rs2858056) and increased serum level of the MPG protein. PMID: 25757089
Role of MPG protein in the DNA damage response through the base excision repair pathway PMID: 26025911
results suggest that individuals carrying R120C and R141Q MPG variants may be at risk for genomic instability and associated diseases as a consequence. PMID: 25538240
Elevated MPG activity is associated with lung cancer, possibly by creating an imbalance in the base excision repair pathway. PMID: 22266085
In the case of alkyladenine DNA glycosylase, DNA intercalation contributes to the specific binding of a damaged nucleotide, but this enhanced specificity comes at the cost of reduced speed of nucleotide flipping. PMID: 25324304
High MPG DNA repair assays for two different oxidative DNA lesions reveal associations with increased lung cancer risk. PMID: 25355292
disease-stage-specific alterations in the expression of MPG may highlight a potential role for MPG in determining EAC onset and thus potentially be of clinical relevance for early disease detection and increased patient survival. PMID: 23137018
AAG has a flexible amino terminus that tunes its affinity for nonspecific DNA, but we find that it is not required for intersegmental transfer. As AAG has only a single DNA binding site, this argues against the bridging model for intersegmental transfer PMID: 23839988
AAG removes both methanol and 1,N(6)-ethenoadenine from DNA with single-turnover rate constants that are significantly greater than the corresponding uncatalyzed rates. PMID: 23688261
Mitochondrial single-stranded binding protein (mtSSB) as a novel interacting partner of AAG. PMID: 23290262
UHRF1 interacts with N-methylpurine DNA glycosylase (MPG) in cancer cells in vitro and displays a co-localization with MPG in the nucleoplasm. PMID: 23537643
A functional footprinting approach was used to define the binding site of alkyladenine DNA glycosylase used for the repair of deaminated purines. PMID: 23074184
AAG can make damaged DNA by catalyzing formation of an N-glycosyl bond between 1,N(6)-ethenoadenine (epsilonA) and abasic DNA. We attribute the reversibility of this reaction to the tight binding and slow subsequent hydrolysis of DNA containing an epsilonA lesion. PMID: 20873830
Investigated the expression of MPG gene and protein in 128 glioma and 10 non-neoplastic brain tissues. Found MPG gene expression level in glioma tissues was significantly higher than that in non-neoplastic brain tissues (P < 0.001). PMID: 22496614
The non-enzymatic binding of AAG to 3,N(4)-ethenocytosine specifically blocks ALKBH2-catalyzed repair of 3,N(4)-ethenocytosine but not that of methylated ALKBH2 substrates. PMID: 22079122
Novel structures of AAG presented here help provide an understanding of this intriguing DNA repair protein, both in terms of understanding how AAG can recognize different types of DNA damage and in terms of how it may search the genome for DNA damage. PMID: 22148158
Evaluation of APNG protein levels in several clinical datasets demonstrated that in patients, high nuclear APNG expression correlated with poorer overall survival compared with patients lacking APNG expression. PMID: 22156195
The use of a concerted mechanism supports previous speculations that AAG uses a nonspecific strategy to excise both neutral 1,N(6)-ethenoadenine and cationic N(3)-methyladenine lesions. PMID: 21877721
Structural basis for the inhibition of human alkyladenine DNA glycosylase (AAG) by 3,N4-ethenocytosine-containing DNA. PMID: 21349833
Substitution of active site tyrosines with tryptophan alters the free energy for nucleotide flipping by human alkyladenine DNA glycosylase PMID: 21244040
rs710079 and rs2858056 polymorphisms and the GCGC haplotype in the MPG gene are associated with the risk of rheumatoid arthritis progression. PMID: 21063071
AAG uses hopping to effectively search both strands of a DNA duplex in a single binding encounter. PMID: 20201599
The human alkyl-N-purine-DNA glycosylase (ANPG or MPG) excises both 1,N(6)-ethenoadenine and 1,N(2)-ethenoguanine adducts, exocyclic DNA adducts generated by lipid peroxidation, when present in DNA. PMID: 12016206
The human alkyl-N-purine-DNA glycosylase (ANPG or MPG) excises with high efficiency hypoxanthine residues, deamination product of adenine, when present in DNA. ANPG is by far the most efficient hypoxanthine-DNA glycosylase of all the enzymes tested. PMID: 8016081
The human alkyl-N-purine-DNA glycosylase (ANPG or MPG) binds tightly to ethenocytosine adduct when present in DNA. Unlike the ethenopurines, ANPG does not excise ethenocytosine but prevents its repair by forming an abortive protein-DNA complex. PMID: 14761949
AAG and its mutants bind DNA containing one and two base-pair loops with significant affinity, thus shielding them from mismatch repair; the strength of such binding correlates with their ability to induce the mutator phenotype. PMID: 20347426
evidence that the excised base rather than AP-site could be rate-limiting for DNA-glycosylase reactions PMID: 19616486
Effects of hydrogen bonding within a damaged base pair on the activity of wild type and DNA-intercalating mutants of the human alkyladenine DNA glycosylase. PMID: 12077143
MPG mRNA expression was slightly higher in astrocytic tumors than in adjacent tissue, suggesting a role in astrocytic tumors & the possibility that the altered MPG expression & intracellular localization could be associated with astrocytic tumorigenesis. PMID: 12820404
Methylated DNA-binding domain 1 cooperates with this enzyme for transcriptional repression and DNA repair. PMID: 14555760
alkyladenine DNA-glycosylase activates neutral lesions by protonation of the nucleobase leaving group PMID: 14567703
analysis of substrate specificity of human 3-methyladenine-DNA glycosylase PMID: 14688248
plays a role in maintaining integrity of the genome by recruiting DNA repair proteins to actively transcribing DNA [3-methyladenine DNA glycosylase] PMID: 14761960
AAG is a mammalian enzyme that can act on all three purine deamination bases, hypoxanthine, xanthine, and oxanine PMID: 15247209
C147G and C342G missense mutations and a 5'-UTR 1-27 insT were found in familial colorectal cancer DNA suggesting a limited role for this gene in the devlopment of CRC. PMID: 17029639
this newly purified full-length hMPG is appreciably stable at high temperature, such as 50 degrees C. PMID: 18191412
The mutability of the AAG substrate binding pocket, and the essentiality of individual binding pocket amino acids for survival of methylation damage, was assessed. PMID: 18706524
Although the amino terminus of the protein is dispensable for glycosylase activity at a single site, we find that deletion of the 80 amino-terminal amino acids significantly decreases the processivity of AAG. PMID: 18839966
Results suggest the possible significance of repair of the frequent lesions in single-stranded DNA transiently generated during replication and transcription. PMID: 19219989
RNS-induced posttranslational modification of AAG is one mechanism of base excision repair dysregulation PMID: 19864471