Recombinant Human DNA-3-methyladenine glycosylase(MPG),partial

Code CSB-YP014749HU
Size US$1298
Image
  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

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Product Details

Purity Greater than 90% as determined by SDS-PAGE.
Target Names MPG
Uniprot No. P29372
Research Area Epigenetics and Nuclear Signaling
Alternative Names 3 alkyladenine DNA glycosylase; 3-alkyladenine DNA glycosylase; 3-methyladenine DNA glycosidase; 3MG_HUMAN; AAG; ADPG; Alkyladenine DNA glycosylase; anpg; APNG; CRA36.1; DNA 3 methyladenine glycosylase; DNA-3-methyladenine glycosylase; MDG; Mid1; Mpg; N methylpurine DNA glycosirase; N methylpurine DNA glycosylase; N-methylpurine-DNA glycosylase; PIG11; PIG16; Proliferation inducing protein 11; Proliferation inducing protein 16
Species Homo sapiens (Human)
Source Yeast
Expression Region 13-298aa
Target Protein Sequence QFCRRMGQKKQRPARAGQPHSSSDAAQAPAEQPHSSSDAAQAPCPRERCLGPPTTPGPYRSIYFSSPKGHLTRLGLEFFDQPAVPLARAFLGQVLVRRLPNGTELRGRIVETEAYLGPEDEAAHSRGGRQTPRNRGMFMKPGTLYVYIIYGMYFCMNISSQGDGACVLLRALEPLEGLETMRQLRSTLRKGTASRVLKDRELCSGPSKLCQALAINKSFDQRDLAQDEAVWLERGPLEPSEPAVVAAARVGVGHAGEWARKPLRFYVRGSPWVSVVDRVAEQDTQA
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight 33.5kDa
Protein Length Partial
Tag Info N-terminal 6xHis-tagged
Form Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting
and FAQs
Protein FAQs
Storage Condition Store at -20°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA Please contact us to get it.

Target Data

Function Hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine, and 7-methylguanine from the damaged DNA polymer formed by alkylation lesions.
Gene References into Functions
  1. high levels of APNG were associated with better overall survival in patients with glioblastoma PMID: 28662073
  2. Data indicate that DNA glycosylases MYH, UNG2, MPG, NTH1, NEIL1, 2 and 3 on nascent DNA. PMID: 28575236
  3. 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
  4. Rheumatoid arthritis is associated with a polymorphism in the MPG gene (rs2858056) and increased serum level of the MPG protein. PMID: 25757089
  5. Role of MPG protein in the DNA damage response through the base excision repair pathway PMID: 26025911
  6. 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
  7. Elevated MPG activity is associated with lung cancer, possibly by creating an imbalance in the base excision repair pathway. PMID: 22266085
  8. 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
  9. High MPG DNA repair assays for two different oxidative DNA lesions reveal associations with increased lung cancer risk. PMID: 25355292
  10. 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
  11. 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
  12. 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
  13. Mitochondrial single-stranded binding protein (mtSSB) as a novel interacting partner of AAG. PMID: 23290262
  14. 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
  15. A functional footprinting approach was used to define the binding site of alkyladenine DNA glycosylase used for the repair of deaminated purines. PMID: 23074184
  16. N-methylpurine DNA glycosylase negatively regulates p53-mediated cell cycle arrest. PMID: 22801474
  17. 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
  18. 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
  19. 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
  20. 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
  21. 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
  22. 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
  23. Structural basis for the inhibition of human alkyladenine DNA glycosylase (AAG) by 3,N4-ethenocytosine-containing DNA. PMID: 21349833
  24. Substitution of active site tyrosines with tryptophan alters the free energy for nucleotide flipping by human alkyladenine DNA glycosylase PMID: 21244040
  25. rs710079 and rs2858056 polymorphisms and the GCGC haplotype in the MPG gene are associated with the risk of rheumatoid arthritis progression. PMID: 21063071
  26. AAG uses hopping to effectively search both strands of a DNA duplex in a single binding encounter. PMID: 20201599
  27. 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
  28. 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
  29. 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
  30. 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
  31. evidence that the excised base rather than AP-site could be rate-limiting for DNA-glycosylase reactions PMID: 19616486
  32. 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
  33. 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
  34. Methylated DNA-binding domain 1 cooperates with this enzyme for transcriptional repression and DNA repair. PMID: 14555760
  35. alkyladenine DNA-glycosylase activates neutral lesions by protonation of the nucleobase leaving group PMID: 14567703
  36. analysis of substrate specificity of human 3-methyladenine-DNA glycosylase PMID: 14688248
  37. plays a role in maintaining integrity of the genome by recruiting DNA repair proteins to actively transcribing DNA [3-methyladenine DNA glycosylase] PMID: 14761960
  38. AAG is a mammalian enzyme that can act on all three purine deamination bases, hypoxanthine, xanthine, and oxanine PMID: 15247209
  39. 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
  40. this newly purified full-length hMPG is appreciably stable at high temperature, such as 50 degrees C. PMID: 18191412
  41. 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
  42. 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
  43. Results suggest the possible significance of repair of the frequent lesions in single-stranded DNA transiently generated during replication and transcription. PMID: 19219989
  44. RNS-induced posttranslational modification of AAG is one mechanism of base excision repair dysregulation PMID: 19864471

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Subcellular Location Cytoplasm, Mitochondrion matrix, mitochondrion nucleoid, Nucleus
Protein Families DNA glycosylase MPG family
Database Links

HGNC: 7211

OMIM: 156565

KEGG: hsa:4350

STRING: 9606.ENSP00000219431

UniGene: Hs.459596

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