Recombinant Human DNA-3-methyladenine glycosylase | MyBioSource MBS954215 product information

product summary

company name :

MyBioSource

product type :

protein

product name :

Recombinant Human DNA-3-methyladenine glycosylase

catalog :

MBS954215

quantity :

0.05 mg (E-Coli)

price :

190 USD

more info or order :

MyBioSource product webpage

product information

catalog number :

MBS954215

products type :

Recombinant Protein

products full name :

Recombinant Human DNA-3-methyladenine glycosylase

products short name :

DNA-3-methyladenine glycosylase

products name syn :

3-alkyladenine DNA glycosylase; 3-methyladenine DNA glycosidase; ADPGN-methylpurine-DNA glycosylase

other names :

DNA-3-methyladenine glycosylase isoform b; DNA-3-methyladenine glycosylase; DNA-3-methyladenine glycosylase; N-methylpurine DNA glycosylase; 3-alkyladenine DNA glycosylase; 3-methyladenine DNA glycosidase; ADPG; N-methylpurine-DNA glycosylase

products gene name :

MPG

other gene names :

MPG; MPG; AAG; MDG; ADPG; APNG; Mid1; anpg; PIG11; PIG16; CRA36.1; AAG; ANPG; MID1

uniprot entry name :

3MG_HUMAN

host :

E Coli or Yeast or Baculovirus or Mammalian Cell

sequence positions :

13-298

sequence length :

293

sequence :

MPARSGAQFCRRMGQKKQRPARAGQPHSSSDAAQAPAEQ
PHSSSDAAQAPCPRERCLGPPTTPGPYRSIYFSSPKGHL
TRLGLEFFDQPAVPLARAFLGQVLVRRLPNGTELRGRIV
ETEAYLGPEDEAAHSRGGRQTPRNRGMFMKPGTLYVYII
YGMYFCMNISSQGDGACVLLRALEPLEGLETMRQLRSTL
RKGTASRVLKDRELCSGPSKLCQALAINKSFDQRDLAQD
EAVWLERGPLEPSEPAVVAAA

purity :

Greater than 90% as determined by SDS-PAGE.

form :

Liquid containing glycerol; lyophilization may be available upon request.

storage stability :

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

products categories :

Epigenetics and Nuclear Signaling

products description :

Hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine, and 7-methylguanine from the damaged DNA polymer formed by alkylation lesions.

products references :

Cloning and characterization of a 3-methyladenine DNA glycosylase cDNA from human cells whose gene maps to chromosome 16.Samson L., Derfler B., Boosalis M., Call K.Proc. Natl. Acad. Sci. U.S.A. 88:9127-9131(1991) Structure of the human 3-methyladenine DNA glycosylase gene and localization close to the 16p telomere.Vickers M.A., Vyas P., Harris P.C., Simmons D.L., Higgs D.R.Proc. Natl. Acad. Sci. U.S.A. 90:3437-3441(1993) Identification of a human cell proliferation gene 11.Kim J.W.NIEHS SNPs programSequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16.Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.Hum. Mol. Genet. 10:339-352(2001) The sequence and analysis of duplication-rich human chromosome 16.Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.Nature 432:988-994(2004)

ncbi gi num :

62632765

ncbi acc num :

NP_001015052.1

ncbi gb acc num :

NM_001015052.2

uniprot acc num :

P29372

ncbi mol weight :

34.2kD

ncbi pathways :

Base Excision Repair Pathway (1270351); Base Excision Repair Pathway (83043); Base Excision Repair Pathway (451); Base-Excision Repair, AP Site Formation Pathway (1270352); Cleavage Of The Damaged Purine Pathway (1270355); DNA Repair Pathway (1270350); Depurination Pathway (1270353); Displacement Of DNA Glycosylase By APEX1 Pathway (1270360); Recognition And Association Of DNA Glycosylase With Site Containing An Affected Purine Pathway (1270354); Resolution Of Abasic Sites (AP Sites) Pathway (1270359)

uniprot summary :

MPG: Hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine, and 7-methylguanine from the damaged DNA polymer formed by alkylation lesions. Belongs to the DNA glycosylase MPG family. 2 isoforms of the human protein are produced by alternative splicing. Protein type: Nuclear receptor co-regulator; Hydrolase; EC 3.2.2.21. Chromosomal Location of Human Ortholog: 16p13.3. Cellular Component: nucleoplasm. Molecular Function: alkylbase DNA N-glycosylase activity; damaged DNA binding; DNA-3-methyladenine glycosylase I activity; protein binding. Biological Process: base-excision repair; base-excision repair, AP site formation; depurination; DNA dealkylation; DNA repair

size1 :

0.05 mg (E-Coli)

price1 :

190 USD

size2 :

0.2 mg (E-Coli)

price2 :

460

size3 :

0.5 mg (E-Coli)

price3 :

750

size4 :

0.05 mg (Baculovirus)

price4 :

1055

size5 :

1 mg (E-Coli)

price5 :

1180

more info or order :

MyBioSource product webpage