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Endonuclease III homolog 1 (EC 3.2.2.-) (EC 4.2.99.18) (Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase 1) (DNA glycosylase/AP lyase 1) (Endonuclease III-like glycosylase 1) (Redoxyendonuclease 1)

 NTH1_YEAST              Reviewed;         399 AA.
P31378; D6VPK3;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 1.
10-OCT-2018, entry version 160.
RecName: Full=Endonuclease III homolog 1 {ECO:0000255|HAMAP-Rule:MF_03183};
EC=3.2.2.- {ECO:0000255|HAMAP-Rule:MF_03183};
EC=4.2.99.18 {ECO:0000255|HAMAP-Rule:MF_03183};
AltName: Full=Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase 1 {ECO:0000255|HAMAP-Rule:MF_03183};
Short=DNA glycosylase/AP lyase 1 {ECO:0000255|HAMAP-Rule:MF_03183};
AltName: Full=Endonuclease III-like glycosylase 1;
AltName: Full=Redoxyendonuclease 1;
Flags: Precursor;
Name=NTG1 {ECO:0000255|HAMAP-Rule:MF_03183}; Synonyms=OGG2, SCR1;
OrderedLocusNames=YAL015C; ORFNames=FUN33;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=8458570;
Ouellette B.F.F., Clark M.W., Keng T., Storms R.K., Zhong W.-W.,
Zeng B., Fortin N., Delaney S., Barton A.B., Kaback D.B., Bussey H.;
"Sequencing of chromosome I from Saccharomyces cerevisiae: analysis of
a 32 kb region between the LTE1 and SPO7 genes.";
Genome 36:32-42(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=8144453; DOI=10.1128/jb.176.7.1872-1880.1994;
Barton A.B., Kaback D.B.;
"Molecular cloning of chromosome I DNA from Saccharomyces cerevisiae:
analysis of the genes in the FUN38-MAK16-SPO7 region.";
J. Bacteriol. 176:1872-1880(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
Storms R.K.;
"The nucleotide sequence of chromosome I from Saccharomyces
cerevisiae.";
Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
FUNCTION.
PubMed=8805338; DOI=10.1016/S0960-9822(02)00641-3;
Nash H.M., Bruner S.D., Scharer O.D., Kawate T., Addona T.A.,
Spooner E., Lane W.S., Verdine G.L.;
"Cloning of a yeast 8-oxoguanine DNA glycosylase reveals the existence
of a base-excision DNA-repair protein superfamily.";
Curr. Biol. 6:968-980(1996).
[6]
FUNCTION, AND INDUCTION BY DNA DAMAGE.
PubMed=8855249; DOI=10.1073/pnas.93.20.10735;
Eide L., Bjoras M., Pirovano M., Alseth I., Berdal K.G., Seeberg E.;
"Base excision of oxidative purine and pyrimidine DNA damage in
Saccharomyces cerevisiae by a DNA glycosylase with sequence similarity
to endonuclease III from Escherichia coli.";
Proc. Natl. Acad. Sci. U.S.A. 93:10735-10740(1996).
[7]
FUNCTION.
PubMed=9020769; DOI=10.1021/bi9625511;
Augeri L., Lee Y.M., Barton A.B., Doetsch P.W.;
"Purification, characterization, gene cloning, and expression of
Saccharomyces cerevisiae redoxyendonuclease, a homolog of Escherichia
coli endonuclease III.";
Biochemistry 36:721-729(1997).
[8]
FUNCTION, SUBSTRATES, INDUCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=9558341; DOI=10.1021/bi973042h;
You H.J., Swanson R.L., Doetsch P.W.;
"Saccharomyces cerevisiae possesses two functional homologues of
Escherichia coli endonuclease III.";
Biochemistry 37:6033-6040(1998).
[9]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=9545197; DOI=10.1016/S0960-9822(98)70158-7;
Bruner S.D., Nash H.M., Lane W.S., Verdine G.L.;
"Repair of oxidatively damaged guanine in Saccharomyces cerevisiae by
an alternative pathway.";
Curr. Biol. 8:393-403(1998).
[10]
FUNCTION, SUBSTRATES, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=9826748; DOI=10.1093/nar/26.23.5270;
Senturker S., Auffret van der Kemp P., You H.J., Doetsch P.W.,
Dizdaroglu M., Boiteux S.;
"Substrate specificities of the ntg1 and ntg2 proteins of
Saccharomyces cerevisiae for oxidized DNA bases are not identical.";
Nucleic Acids Res. 26:5270-5276(1998).
[11]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=10471279; DOI=10.1021/bi991121i;
You H.J., Swanson R.L., Harrington C., Corbett A.H.,
Jinks-Robertson S., Sentuerker S., Wallace S.S., Boiteux S.,
Dizdaroglu M., Doetsch P.W.;
"Saccharomyces cerevisiae Ntg1p and Ntg2p: broad specificity N-
glycosylases for the repair of oxidative DNA damage in the nucleus and
mitochondria.";
Biochemistry 38:11298-11306(1999).
[12]
FUNCTION IN OXIDATIVE DNA DAMAGE REPAIR, SUBCELLULAR LOCATION,
DISRUPTION PHENOTYPE, AND INDUCTION.
PubMed=10207101; DOI=10.1128/MCB.19.5.3779;
Alseth I., Eide L., Pirovano M., Rognes T., Seeberg E., Bjoras M.;
"The Saccharomyces cerevisiae homologues of endonuclease III from
Escherichia coli, Ntg1 and Ntg2, are both required for efficient
repair of spontaneous and induced oxidative DNA damage in yeast.";
Mol. Cell. Biol. 19:3779-3787(1999).
[13]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=14500818; DOI=10.1093/nar/gkg749;
Meadows K.L., Song B., Doetsch P.W.;
"Characterization of AP lyase activities of Saccharomyces cerevisiae
Ntg1p and Ntg2p: implications for biological function.";
Nucleic Acids Res. 31:5560-5567(2003).
[14]
FUNCTION IN DNA ALKYLATION DAMAGE REPAIR.
PubMed=14697759; DOI=10.1016/j.dnarep.2003.09.005;
Hanna M., Chow B.L., Morey N.J., Jinks-Robertson S., Doetsch P.W.,
Xiao W.;
"Involvement of two endonuclease III homologs in the base excision
repair pathway for the processing of DNA alkylation damage in
Saccharomyces cerevisiae.";
DNA Repair 3:51-59(2004).
[15]
DISRUPTION PHENOTYPE.
PubMed=15923634; DOI=10.1128/MCB.25.12.5196-5204.2005;
Doudican N.A., Song B., Shadel G.S., Doetsch P.W.;
"Oxidative DNA damage causes mitochondrial genomic instability in
Saccharomyces cerevisiae.";
Mol. Cell. Biol. 25:5196-5204(2005).
[16]
DISRUPTION PHENOTYPE.
PubMed=16730479; DOI=10.1016/j.dnarep.2006.04.002;
Phadnis N., Mehta R., Meednu N., Sia E.A.;
"Ntg1p, the base excision repair protein, generates mutagenic
intermediates in yeast mitochondrial DNA.";
DNA Repair 5:829-839(2006).
[17]
FUNCTION IN OXIDATIVE DNA DAMAGE REPAIR, AND SUBSTRATES.
PubMed=18983898; DOI=10.1016/j.bbagen.2008.10.001;
Gasparutto D., Muller E., Boiteux S., Cadet J.;
"Excision of the oxidatively formed 5-hydroxyhydantoin and 5-hydroxy-
5-methylhydantoin pyrimidine lesions by Escherichia coli and
Saccharomyces cerevisiae DNA N-glycosylases.";
Biochim. Biophys. Acta 1790:16-24(2009).
[18]
SUBCELLULAR LOCATION, SUMOYLATION, AND MUTAGENESIS OF LYS-364.
PubMed=19029246; DOI=10.1128/MCB.01357-08;
Griffiths L.M., Swartzlander D., Meadows K.L., Wilkinson K.D.,
Corbett A.H., Doetsch P.W.;
"Dynamic compartmentalization of base excision repair proteins in
response to nuclear and mitochondrial oxidative stress.";
Mol. Cell. Biol. 29:794-807(2009).
[19]
FUNCTION IN MTDNA REPLICATION.
PubMed=19074198; DOI=10.1093/nar/gkn993;
Hori A., Yoshida M., Shibata T., Ling F.;
"Reactive oxygen species regulate DNA copy number in isolated yeast
mitochondria by triggering recombination-mediated replication.";
Nucleic Acids Res. 37:749-761(2009).
[20]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
3-LYS--LYS-6; 15-LYS-ARG-16; 33-LYS-ARG-34 AND LYS-243.
PubMed=20194111; DOI=10.1093/nar/gkq108;
Swartzlander D.B., Griffiths L.M., Lee J., Degtyareva N.P.,
Doetsch P.W., Corbett A.H.;
"Regulation of base excision repair: Ntg1 nuclear and mitochondrial
dynamic localization in response to genotoxic stress.";
Nucleic Acids Res. 38:3963-3974(2010).
-!- FUNCTION: Bifunctional DNA N-glycosylase with associated
apurinic/apyrimidinic (AP) lyase function that catalyzes the first
step in base excision repair (BER), the primary repair pathway for
the repair of oxidative DNA damage. The DNA N-glycosylase activity
releases the damaged DNA base from DNA by cleaving the N-
glycosidic bond, leaving an AP site. The AP-lyase activity cleaves
the phosphodiester bond 3' to the AP site by a beta-elimination.
Primarily recognizes and repairs oxidative base damage of
pyrimidines, but also purine-derived lesions, alkylation damage
and cytosine photoproducts generated by UV irradiation as well as
abasic sites. Has also 8-oxoguanine DNA glycosylase activity. The
AP lyase can incise AP sites opposite all four bases. May also
play a role in the regulation of mtDNA copy number by introducing
a double-stranded break (DSB) at the mtDNA replication origin
ori5, initiating the rolling-circle mtDNA replication.
{ECO:0000255|HAMAP-Rule:MF_03183, ECO:0000269|PubMed:10207101,
ECO:0000269|PubMed:10471279, ECO:0000269|PubMed:14500818,
ECO:0000269|PubMed:14697759, ECO:0000269|PubMed:18983898,
ECO:0000269|PubMed:19074198, ECO:0000269|PubMed:20194111,
ECO:0000269|PubMed:8805338, ECO:0000269|PubMed:8855249,
ECO:0000269|PubMed:9020769, ECO:0000269|PubMed:9545197,
ECO:0000269|PubMed:9558341, ECO:0000269|PubMed:9826748}.
-!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or
apyrimidinic site in DNA is broken by a beta-elimination reaction,
leaving a 3'-terminal unsaturated sugar and a product with a
terminal 5'-phosphate. {ECO:0000255|HAMAP-Rule:MF_03183,
ECO:0000269|PubMed:14500818, ECO:0000269|PubMed:20194111,
ECO:0000269|PubMed:9545197}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=227 nM for dihydrouracil containing duplex oligonucleotides
(N-glycosylase activity) {ECO:0000269|PubMed:14500818,
ECO:0000269|PubMed:9558341, ECO:0000269|PubMed:9826748};
KM=250 nM for 5-hydroxy-6-hydrothymine containing duplex
oligonucleotides (N-glycosylase activity)
{ECO:0000269|PubMed:14500818, ECO:0000269|PubMed:9558341,
ECO:0000269|PubMed:9826748};
KM=721 nM for 5-hydroxy-6-hydrouracil containing duplex
oligonucleotides (N-glycosylase activity)
{ECO:0000269|PubMed:14500818, ECO:0000269|PubMed:9558341,
ECO:0000269|PubMed:9826748};
KM=755 nM for 5-hydroxy-5-methylhydantoin containing duplex
oligonucleotides (N-glycosylase activity)
{ECO:0000269|PubMed:14500818, ECO:0000269|PubMed:9558341,
ECO:0000269|PubMed:9826748};
KM=997 nM for 5-hydroxyuracil containing duplex oligonucleotides
(N-glycosylase activity) {ECO:0000269|PubMed:14500818,
ECO:0000269|PubMed:9558341, ECO:0000269|PubMed:9826748};
KM=1380 nM for 5-hydroxycytosine containing duplex
oligonucleotides (N-glycosylase activity)
{ECO:0000269|PubMed:14500818, ECO:0000269|PubMed:9558341,
ECO:0000269|PubMed:9826748};
KM=3250 nM for thymine glycol containing duplex oligonucleotides
(N-glycosylase activity) {ECO:0000269|PubMed:14500818,
ECO:0000269|PubMed:9558341, ECO:0000269|PubMed:9826748};
KM=1305 nM for 2,6-diamino-4-hydroxy-5-formamidopyrimidine
(FapyAde) containing duplex oligonucleotides (N-glycosylase
activity) {ECO:0000269|PubMed:14500818,
ECO:0000269|PubMed:9558341, ECO:0000269|PubMed:9826748};
KM=2460 nM for 4,6-diamino-5-formamidopyrimidine (FapyGua)
containing duplex oligonucleotides (N-glycosylase activity)
{ECO:0000269|PubMed:14500818, ECO:0000269|PubMed:9558341,
ECO:0000269|PubMed:9826748};
KM=24.86 nM for AP/G abasic-site containing duplex
oligonucleotides (AP lyase activity)
{ECO:0000269|PubMed:14500818, ECO:0000269|PubMed:9558341,
ECO:0000269|PubMed:9826748};
KM=11.37 nM for AP/A abasic-site containing duplex
oligonucleotides (AP lyase activity)
{ECO:0000269|PubMed:14500818, ECO:0000269|PubMed:9558341,
ECO:0000269|PubMed:9826748};
KM=6.67 nM for AP/T abasic-site containing duplex
oligonucleotides (AP lyase activity)
{ECO:0000269|PubMed:14500818, ECO:0000269|PubMed:9558341,
ECO:0000269|PubMed:9826748};
KM=36.58 nM for AP/C abasic-site containing duplex
oligonucleotides (AP lyase activity)
{ECO:0000269|PubMed:14500818, ECO:0000269|PubMed:9558341,
ECO:0000269|PubMed:9826748};
Vmax=1.9 nmol/min/ng enzyme for dihydrouracil containing duplex
oligonucleotides (N-glycosylase activity)
{ECO:0000269|PubMed:14500818, ECO:0000269|PubMed:9558341,
ECO:0000269|PubMed:9826748};
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03183,
ECO:0000269|PubMed:10207101, ECO:0000269|PubMed:10471279,
ECO:0000269|PubMed:19029246, ECO:0000269|PubMed:20194111}.
Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03183,
ECO:0000269|PubMed:10207101, ECO:0000269|PubMed:10471279,
ECO:0000269|PubMed:19029246, ECO:0000269|PubMed:20194111}.
Note=Relocalizes to organelles containing elevated oxidative DNA
damage. {ECO:0000269|PubMed:19029246,
ECO:0000269|PubMed:20194111}.
-!- INDUCTION: By oxidizing agents. {ECO:0000269|PubMed:10207101,
ECO:0000269|PubMed:8855249, ECO:0000269|PubMed:9558341}.
-!- PTM: Monosumoylated. Sumoylation is associated with targeting of
NTG1 to nuclei containing oxidative DNA damage.
{ECO:0000269|PubMed:19029246}.
-!- DISRUPTION PHENOTYPE: Greatly increases spontaneous and hydrogen
peroxide-induced mutation frequency. Causes mitochondrial genome
instability. Suppresses mitochondrial point mutation rates,
frameshifts and recombination rates, probably because NTG1 can
generate mutagenic intermediates in yeast mitochondrial DNA.
{ECO:0000269|PubMed:10207101, ECO:0000269|PubMed:15923634,
ECO:0000269|PubMed:16730479}.
-!- MISCELLANEOUS: Does not possess a consensus sequence for a C-
terminal iron-sulfur center typical of all other endonuclease III
homologs. {ECO:0000305|PubMed:9558341}.
-!- SIMILARITY: Belongs to the Nth/MutY family. {ECO:0000255|HAMAP-
Rule:MF_03183}.
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EMBL; L05146; AAC04942.1; -; Genomic_DNA.
EMBL; BK006935; DAA06973.1; -; Genomic_DNA.
PIR; S36719; S36719.
RefSeq; NP_009387.1; NM_001178160.1.
ProteinModelPortal; P31378; -.
BioGrid; 31751; 104.
DIP; DIP-6614N; -.
IntAct; P31378; 24.
STRING; 4932.YAL015C; -.
MaxQB; P31378; -.
PaxDb; P31378; -.
PRIDE; P31378; -.
TopDownProteomics; P31378; -.
EnsemblFungi; YAL015C; YAL015C; YAL015C.
GeneID; 851218; -.
KEGG; sce:YAL015C; -.
EuPathDB; FungiDB:YAL015C; -.
SGD; S000000013; NTG1.
GeneTree; ENSGT00510000047513; -.
HOGENOM; HOG000252209; -.
InParanoid; P31378; -.
KO; K10773; -.
OrthoDB; EOG092C3TX5; -.
BioCyc; YEAST:G3O-28827-MONOMER; -.
Reactome; R-SCE-110329; Cleavage of the damaged pyrimidine.
Reactome; R-SCE-110357; Displacement of DNA glycosylase by APEX1.
PRO; PR:P31378; -.
Proteomes; UP000002311; Chromosome I.
GO; GO:0005739; C:mitochondrion; IDA:SGD.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IDA:SGD.
GO; GO:0008534; F:oxidized purine nucleobase lesion DNA N-glycosylase activity; IDA:SGD.
GO; GO:0000703; F:oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity; IDA:SGD.
GO; GO:0006284; P:base-excision repair; IDA:SGD.
GO; GO:0006285; P:base-excision repair, AP site formation; IDA:SGD.
GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
GO; GO:0006281; P:DNA repair; IDA:SGD.
GO; GO:0006296; P:nucleotide-excision repair, DNA incision, 5'-to lesion; IBA:GO_Central.
GO; GO:0090297; P:positive regulation of mitochondrial DNA replication; IMP:SGD.
CDD; cd00056; ENDO3c; 1.
Gene3D; 1.10.1670.10; -; 1.
HAMAP; MF_03183; Endonuclease_III_Nth; 1.
InterPro; IPR011257; DNA_glycosylase.
InterPro; IPR004036; Endonuclease-III-like_CS2.
InterPro; IPR003265; HhH-GPD_domain.
InterPro; IPR000445; HhH_motif.
InterPro; IPR023170; HTH_base_excis_C.
InterPro; IPR030841; NTH1.
Pfam; PF00633; HHH; 1.
Pfam; PF00730; HhH-GPD; 1.
SMART; SM00478; ENDO3c; 1.
SUPFAM; SSF48150; SSF48150; 1.
PROSITE; PS01155; ENDONUCLEASE_III_2; 1.
1: Evidence at protein level;
Complete proteome; DNA damage; DNA repair; Glycosidase; Hydrolase;
Isopeptide bond; Lyase; Mitochondrion; Nucleus; Reference proteome;
Transit peptide; Ubl conjugation.
TRANSIT 1 26 Mitochondrion. {ECO:0000255|HAMAP-
Rule:MF_03183}.
CHAIN 27 399 Endonuclease III homolog 1.
/FTId=PRO_0000001744.
DOMAIN 223 247 HhH. {ECO:0000255|HAMAP-Rule:MF_03183}.
MOTIF 14 37 Bipartite nuclear localization signal.
{ECO:0000255}.
ACT_SITE 243 243 Nucleophile; for N-glycosylase activity.
{ECO:0000255|HAMAP-Rule:MF_03183}.
SITE 262 262 Important for catalytic activity.
{ECO:0000255|HAMAP-Rule:MF_03183}.
CROSSLNK 194 194 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000305}.
MUTAGEN 3 6 KISK->EISE: In NTG1(mts); reduces
mitochondrial localization by 40%.
{ECO:0000269|PubMed:20194111}.
MUTAGEN 15 16 KR->AA: In NTG1(nls1); reduces nuclear
localization by 60%.
{ECO:0000269|PubMed:20194111}.
MUTAGEN 33 34 KR->AA: In NTG1(nls2); reduces nuclear
localization by 60%.
{ECO:0000269|PubMed:20194111}.
MUTAGEN 243 243 K->Q: Abolishes cleavage of substrate
oligonucleotides.
{ECO:0000269|PubMed:20194111}.
MUTAGEN 364 364 K->R: Cannot properly relocalize in
response to oxidative stress.
{ECO:0000269|PubMed:19029246}.
SEQUENCE 399 AA; 45577 MW; A3C878A3004908F3 CRC64;
MQKISKYSSM AILRKRPLVK TETGPESELL PEKRTKIKQE EVVPQPVDID WVKSLPNKQY
FEWIVVRNGN VPNRWATPLD PSILVTPAST KVPYKFQETY ARMRVLRSKI LAPVDIIGGS
SIPVTVASKC GISKEQISPR DYRLQVLLGV MLSSQTKDEV TAMAMLNIMR YCIDELHSEE
GMTLEAVLQI NETKLDELIH SVGFHTRKAK YILSTCKILQ DQFSSDVPAT INELLGLPGV
GPKMAYLTLQ KAWGKIEGIC VDVHVDRLTK LWKWVDAQKC KTPDQTRTQL QNWLPKGLWT
EINGLLVGFG QIITKSRNLG DMLQFLPPDD PRSSLDWDLQ SQLYKEIQQN IMSYPKWVKY
LEGKRELNVE AEINVKHEEK TVEETMVKLE NDISVKVED


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AE56100RA Rat DNA- (apurinic or apyrimidinic site) lyase (APEX1) ELISA Kit 48T
CSB-EL001900RA Rat DNA-(apurinic or apyrimidinic site) lyase (APEX1) ELISA kit 96T
CSB-EP001900HU Recombinant human DNA-(apurinic or apyrimidinic site) lyase 500ug
CSB-EL001900MO Mouse DNA-(apurinic or apyrimidinic site) lyase (APEX1) ELISA kit 96T
CSB-EL001901MO Mouse DNA-(apurinic or apyrimidinic site) lyase (APEX2) ELISA kit 96T
abx108186 Polyclonal Rabbit DNA-(apurinic or apyrimidinic site) lyase Antibody (HRP) 100 μg
CSB-EL001901BO Bovine DNA-(apurinic or apyrimidinic site) lyase (APEX2) ELISA kit 96T
CSB-EL001901HU Human DNA-(apurinic or apyrimidinic site) lyase (APEX2) ELISA kit 96T
CSB-EL001900HU Human DNA-(apurinic or apyrimidinic site) lyase (APEX1) ELISA kit 96T
abx109730 Polyclonal Rabbit DNA-(apurinic or apyrimidinic site) lyase Antibody 100 μg
CSB-EL001900BO Bovine DNA-(apurinic or apyrimidinic site) lyase (APEX1) ELISA kit 96T
abx106767 Polyclonal Rabbit DNA-(apurinic or apyrimidinic site) lyase Antibody (FITC) 100 μg
CSB-EP001900HU Recombinant human DNA-(apurinic or apyrimidinic site) lyase Source: E.coli 200ug


 

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