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Human MPG ELISA Kit für Sandwich ELISA - ABIN423243
Ma, Luo, Wu, Chen, Kou, Wang: Circulation levels of acute phase proteins in patients with Takayasu arteritis. in Journal of vascular surgery 2010
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Data indicate that DNA glycosylases MYH (zeige MUTYH ELISA Kits), UNG2 (zeige CCNO ELISA Kits), MPG, NTH1 (zeige NTHL1 ELISA Kits), NEIL1 (zeige NEIL1 ELISA Kits), 2 and 3 on nascent DNA.
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.
Rheumatoid arthritis is associated with a polymorphism in the MPG gene (rs2858056) and increased serum level of the MPG protein.
Role of MPG protein in the DNA damage response through the base excision repair pathway
results suggest that individuals carrying R120C and R141Q MPG variants may be at risk for genomic instability and associated diseases as a consequence.
Elevated MPG activity is associated with lung cancer, possibly by creating an imbalance in the base excision repair pathway.
High MPG DNA repair assays for two different oxidative DNA lesions reveal associations with increased lung cancer risk.
disease-stage-specific alterations in the expression of MPG may highlight a potential role for MPG in determining EAC (zeige CYLD ELISA Kits) onset and thus potentially be of clinical relevance for early disease detection and increased patient survival.
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
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.
The depletion of Aag did not significantly change the transcriptional inhibitory or mutagenic properties of all five examined lesions, suggesting a negligible role of Aag in the repair of these DNA adducts in mammalian cells.
This study demonstrates for the first time a non-linear dose-response for alkylation-induced colorectal carcinogenesis and reveals DNA repair by MGMT (zeige MGMT ELISA Kits), but not AAG, as a key node in determining a carcinogenic threshold.
the detrimental effects of Aag-initiated BER during I/R and sterile inflammation, and present a novel target for controlling I/R-induced injury.
Toxicity, induced by tert (zeige TERT ELISA Kits)-butyl-hydroperoxide and potassium bromate, differs in base excision repair proficient (Mpg (+/+), Nth1 (zeige NTHL1 ELISA Kits) (+/+)) and deficient (Mpg (-/-), Nth1 (zeige NTHL1 ELISA Kits) (-/-)) mouse embryonic fibroblasts following Msh2 (zeige MSH2 ELISA Kits) knockdown, was examined.
These results provide in vivo evidence that Aag-initiated BER may play a critical role in determining the side-effects of alkylating agent chemotherapies and that Parp1 (zeige PARP1 ELISA Kits) plays a crucial role in Aag-mediated tissue damage.
ALKBH2 (zeige ALKBH2 ELISA Kits) and ALKBH3 (zeige ALKBH3 ELISA Kits) provide cancer protection similar to that of the DNA glycosylase AAG and display apparent epistasis with Aag
AAG is a mammalian enzyme that can act on all three purine deamination bases, hypoxanthine, xanthine, and oxanine
the N-terminal tail in MPG plays a critical role in overcoming product inhibition, which is achieved by reducing the differences of MPG binding affinity toward hypoxanthine and apurinic/apyrimidinic sites
Aag-mediated DNA repair prevents colonic epithelial damage and reduces the severity of dextran sulfate sodium-induced colon tumorigenesis.
Aag-initiated base excision repair drives alkylation-induced retinal degeneration.
enzyme that cleaves 3-methyladenine and 7-methylguanine residues from DNA
, N-methylpurine-DNA glycosylase
, DNA-3-methyladenine glycosylase
, 3' end of the Mid1 gene, localized 68 kb upstream the humanzeta globin gene on 16p
, 3-alkyladenine DNA glycosylase
, 3-methyladenine DNA glycosidase
, CRA36.1 (3-methyl-adenine DNA glycosylase)
, N-methylpurine-DNA glycosylase, MPG
, proliferation-inducing protein 11
, proliferation-inducing protein 16
, 3-methyladenine DNA glycosylase
, N-methylpurine-DNA glycocylase