Recombinant Human Dna-3-Methyladenine Glycosylase (MPG) Protein (His)

Name: Recombinant Human Dna-3-Methyladenine Glycosylase (MPG) Protein (His)
Brand: Beta LifeScience
SKU: BLC-10847P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Dna-3-Methyladenine Glycosylase (MPG) Protein (His) is produced by our Yeast expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P29372
Target Symbol	MPG
Synonyms	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)
Expression System	Yeast
Tag	N-6His
Target Protein Sequence	QFCRRMGQKKQRPARAGQPHSSSDAAQAPAEQPHSSSDAAQAPCPRERCLGPPTTPGPYRSIYFSSPKGHLTRLGLEFFDQPAVPLARAFLGQVLVRRLPNGTELRGRIVETEAYLGPEDEAAHSRGGRQTPRNRGMFMKPGTLYVYIIYGMYFCMNISSQGDGACVLLRALEPLEGLETMRQLRSTLRKGTASRVLKDRELCSGPSKLCQALAINKSFDQRDLAQDEAVWLERGPLEPSEPAVVAAARVGVGHAGEWARKPLRFYVRGSPWVSVVDRVAEQDTQA
Expression Range	13-298aa
Protein Length	Partial
Mol. Weight	33.5kDa
Research Area	Epigenetics And Nuclear Signaling
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine, and 7-methylguanine from the damaged DNA polymer formed by alkylation lesions.
Subcellular Location	Cytoplasm. Mitochondrion matrix, mitochondrion nucleoid. Nucleus.
Protein Families	DNA glycosylase MPG family
Database References	HGNC: 7211 OMIM: 156565 KEGG: hsa:4350 STRING: 9606.ENSP00000219431 UniGene: 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 N-methylpurine DNA glycosylase negatively regulates p53-mediated cell cycle arrest. PMID: 22801474 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

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.