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Methyl-CpG-binding domain protein 2 (Demethylase) (DMTase) (Methyl-CpG-binding protein MBD2)

 MBD2_HUMAN              Reviewed;         411 AA.
Q9UBB5; O95242; Q9UIS8;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
22-NOV-2017, entry version 158.
RecName: Full=Methyl-CpG-binding domain protein 2;
AltName: Full=Demethylase;
Short=DMTase;
AltName: Full=Methyl-CpG-binding protein MBD2;
Name=MBD2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF
157-411 (ISOFORM 3), FUNCTION, AND SUBCELLULAR LOCATION.
TISSUE=Testis;
PubMed=9774669; DOI=10.1128/MCB.18.11.6538;
Hendrich B., Bird A.;
"Identification and characterization of a family of mammalian methyl-
CpG binding proteins.";
Mol. Cell. Biol. 18:6538-6547(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10441743; DOI=10.1007/s003359901112;
Hendrich B., Abbott C., McQueen H., Chambers D., Cross S.H., Bird A.;
"Genomic structure and chromosomal mapping of the murine and human
mbd1, mbd2, mbd3, and mbd4 genes.";
Mamm. Genome 10:906-912(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lymph;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION (ISOFORM 1), AND TISSUE SPECIFICITY.
PubMed=10050851; DOI=10.1038/17533;
Bhattacharya S.K., Ramchandani S., Cervoni N., Szyf M.;
"A mammalian protein with specific demethylase activity for mCpG
DNA.";
Nature 397:579-583(1999).
[5]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH
MECP1 AND HDAC1.
PubMed=10471499; DOI=10.1038/12659;
Ng H.-H., Zhang Y., Hendrich B., Johnson C.A., Turner B.M.,
Erdjument-Bromage H., Tempst P., Reinberg D., Bird A.;
"MBD2 is a transcriptional repressor belonging to the MeCP1 histone
deacetylase complex.";
Nat. Genet. 23:58-61(1999).
[6]
FUNCTION, HETERODIMERIZATION WITH MBD3, AND INTERACTION WITH DNMT1.
PubMed=10947852; DOI=10.1046/j.1365-2443.2000.00359.x;
Tatematsu K., Yamazaki T., Ishikawa F.;
"MBD2-MBD3 complex binds to hemi-methylated DNA and forms a complex
containing DNMT1 at the replication foci in late S phase.";
Genes Cells 5:677-688(2000).
[7]
FUNCTION (ISOFORM 1), AND INTERACTION WITH SIN3A.
PubMed=10950960; DOI=10.1074/jbc.M005929200;
Boeke J., Ammerpohl O., Kegel S., Moehren U., Renkawitz R.;
"The minimal repression domain of MBD2b overlaps with the methyl-CpG-
binding domain and binds directly to Sin3A.";
J. Biol. Chem. 275:34963-34967(2000).
[8]
INTERACTION WITH HDAC1, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=11102443; DOI=10.1074/jbc.M007372200;
Humphrey G.W., Wang Y., Russanova V.R., Hirai T., Qin J., Nakatani Y.,
Howard B.H.;
"Stable histone deacetylase complexes distinguished by the presence of
SANT domain proteins CoREST/kiaa0071 and Mta-L1.";
J. Biol. Chem. 276:6817-6824(2001).
[9]
INTERACTION WITH MIZF.
PubMed=11553631; DOI=10.1074/jbc.M107048200;
Sekimata M., Takahashi A., Murakami-Sekimata A., Homma Y.;
"Involvement of a novel zinc finger protein, MIZF, in transcriptional
repression by interacting with a methyl-CpG-binding protein, MBD2.";
J. Biol. Chem. 276:42632-42638(2001).
[10]
INTERACTION WITH P66ALPHA AND P66BETA, AND SUBCELLULAR LOCATION.
PubMed=12183469; DOI=10.1074/jbc.M207467200;
Brackertz M., Boeke J., Zhang R., Renkawitz R.;
"Two highly related p66 proteins comprise a new family of potent
transcriptional repressors interacting with MBD2 and MBD3.";
J. Biol. Chem. 277:40958-40966(2002).
[11]
INTERACTION WITH GPN1.
PubMed=12588985; DOI=10.1128/MCB.23.5.1656-1665.2003;
Lembo F., Pero R., Angrisano T., Vitiello C., Iuliano R., Bruni C.B.,
Chiariotti L.;
"MBDin, a novel MBD2-interacting protein, relieves MBD2 repression
potential and reactivates transcription from methylated promoters.";
Mol. Cell. Biol. 23:1656-1665(2003).
[12]
FUNCTION, AND INTERACTION WITH DHX9.
PubMed=12665568; DOI=10.1128/MCB.23.8.2645-2657.2003;
Fujita H., Fujii R., Aratani S., Amano T., Fukamizu A., Nakajima T.;
"Antithetic effects of MBD2a on gene regulation.";
Mol. Cell. Biol. 23:2645-2657(2003).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[14]
FUNCTION, AND INTERACTION WITH GATAD2A AND GATAD2B.
PubMed=16415179; DOI=10.1093/nar/gkj437;
Brackertz M., Gong Z., Leers J., Renkawitz R.;
"p66alpha and p66beta of the Mi-2/NuRD complex mediate MBD2 and
histone interaction.";
Nucleic Acids Res. 34:397-406(2006).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-407, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-407, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
FUNCTION, AND DNA-BINDING.
PubMed=24307175; DOI=10.1074/jbc.M113.512236;
Cramer J.M., Scarsdale J.N., Walavalkar N.M., Buchwald W.A.,
Ginder G.D., Williams D.C. Jr.;
"Probing the dynamic distribution of bound states for methylcytosine-
binding domains on DNA.";
J. Biol. Chem. 289:1294-1302(2014).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[23]
STRUCTURE BY NMR OF 360-393 IN COMPLEX WITH GATAD2A, SUBUNIT, AND
INTERACTION WITH GATAD2A.
PubMed=21490301; DOI=10.1073/pnas.1015341108;
Gnanapragasam M.N., Scarsdale J.N., Amaya M.L., Webb H.D., Desai M.A.,
Walavalkar N.M., Wang S.Z., Zu Zhu S., Ginder G.D., Williams D.C. Jr.;
"p66Alpha-MBD2 coiled-coil interaction and recruitment of Mi-2 are
critical for globin gene silencing by the MBD2-NuRD complex.";
Proc. Natl. Acad. Sci. U.S.A. 108:7487-7492(2011).
-!- FUNCTION: Binds CpG islands in promoters where the DNA is
methylated at position 5 of cytosine within CpG dinucleotides.
Binds hemimethylated DNA as well. Recruits histone deacetylases
and DNA methyltransferases. Acts as transcriptional repressor and
plays a role in gene silencing. Functions as a scaffold protein,
targeting GATAD2A and GATAD2B to chromatin to promote repression.
May enhance the activation of some unmethylated cAMP-responsive
promoters. {ECO:0000269|PubMed:10471499,
ECO:0000269|PubMed:10947852, ECO:0000269|PubMed:12665568,
ECO:0000269|PubMed:16415179, ECO:0000269|PubMed:24307175,
ECO:0000269|PubMed:9774669}.
-!- SUBUNIT: Heterodimer with MBD3. Component of the MeCP1 complex
that contains HDAC1 and HDAC2. Binds DNMT1, MIZF, GPN1, SIN3A,
GATAD2A/p66-alpha and GATAD2B/p66-beta. Interacts with DHX9.
{ECO:0000269|PubMed:10471499, ECO:0000269|PubMed:10947852,
ECO:0000269|PubMed:10950960, ECO:0000269|PubMed:11102443,
ECO:0000269|PubMed:11553631, ECO:0000269|PubMed:12183469,
ECO:0000269|PubMed:12588985, ECO:0000269|PubMed:12665568,
ECO:0000269|PubMed:16415179, ECO:0000269|PubMed:21490301}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12183469,
ECO:0000269|PubMed:9774669}. Note=Nuclear, in discrete foci.
Detected at replication foci in late S phase.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=MBD2a, MBD2b;
IsoId=Q9UBB5-1; Sequence=Displayed;
Name=3;
IsoId=Q9UBB5-3; Sequence=VSP_011077, VSP_011078;
Note=Incomplete sequence.;
-!- TISSUE SPECIFICITY: Highly expressed in brain, heart, kidney,
stomach, testis and placenta. {ECO:0000269|PubMed:10050851}.
-!- CAUTION: Functional studies (PubMed:10050851, PubMed:10950960 and
PubMed:12665568) have used a C-terminal fragment of isoform 1
which has been described originally as isoform MBD2b but cannot
however be proven by supporting cDNA sequences.
{ECO:0000305|PubMed:9774669}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/MBD2ID41309ch18q21.html";
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EMBL; AF072242; AAC68871.1; -; mRNA.
EMBL; AF072246; AAC68875.1; -; mRNA.
EMBL; AF120989; AAD56596.1; -; Genomic_DNA.
EMBL; AF120988; AAD56596.1; JOINED; Genomic_DNA.
EMBL; AF120993; AAD56597.1; -; Genomic_DNA.
EMBL; AF120988; AAD56597.1; JOINED; Genomic_DNA.
EMBL; AF120989; AAD56597.1; JOINED; Genomic_DNA.
EMBL; AF120990; AAD56597.1; JOINED; Genomic_DNA.
EMBL; AF120991; AAD56597.1; JOINED; Genomic_DNA.
EMBL; AF120992; AAD56597.1; JOINED; Genomic_DNA.
EMBL; BC032638; AAH32638.1; -; mRNA.
CCDS; CCDS11953.1; -. [Q9UBB5-1]
CCDS; CCDS45871.1; -. [Q9UBB5-3]
RefSeq; NP_003918.1; NM_003927.4. [Q9UBB5-1]
RefSeq; NP_056647.1; NM_015832.4. [Q9UBB5-3]
UniGene; Hs.25674; -.
PDB; 2L2L; NMR; -; B=360-393.
PDBsum; 2L2L; -.
DisProt; DP01068; -.
ProteinModelPortal; Q9UBB5; -.
SMR; Q9UBB5; -.
BioGrid; 114445; 51.
CORUM; Q9UBB5; -.
IntAct; Q9UBB5; 18.
MINT; MINT-210249; -.
STRING; 9606.ENSP00000256429; -.
BindingDB; Q9UBB5; -.
ChEMBL; CHEMBL3707462; -.
iPTMnet; Q9UBB5; -.
PhosphoSitePlus; Q9UBB5; -.
BioMuta; MBD2; -.
DMDM; 50401198; -.
EPD; Q9UBB5; -.
MaxQB; Q9UBB5; -.
PaxDb; Q9UBB5; -.
PeptideAtlas; Q9UBB5; -.
PRIDE; Q9UBB5; -.
Ensembl; ENST00000256429; ENSP00000256429; ENSG00000134046. [Q9UBB5-1]
Ensembl; ENST00000583046; ENSP00000464554; ENSG00000134046. [Q9UBB5-3]
GeneID; 8932; -.
KEGG; hsa:8932; -.
UCSC; uc002lfg.2; human. [Q9UBB5-1]
CTD; 8932; -.
DisGeNET; 8932; -.
EuPathDB; HostDB:ENSG00000134046.11; -.
GeneCards; MBD2; -.
HGNC; HGNC:6917; MBD2.
HPA; CAB037282; -.
HPA; HPA067582; -.
HPA; HPA067615; -.
MIM; 603547; gene.
neXtProt; NX_Q9UBB5; -.
OpenTargets; ENSG00000134046; -.
PharmGKB; PA30660; -.
eggNOG; ENOG410INB9; Eukaryota.
eggNOG; ENOG410ZPAZ; LUCA.
GeneTree; ENSGT00410000025376; -.
HOGENOM; HOG000013073; -.
HOVERGEN; HBG052417; -.
InParanoid; Q9UBB5; -.
KO; K11590; -.
OMA; PAIWLNT; -.
OrthoDB; EOG091G0I05; -.
PhylomeDB; Q9UBB5; -.
TreeFam; TF325032; -.
Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
Reactome; R-HSA-73728; RNA Polymerase I Promoter Opening.
SIGNOR; Q9UBB5; -.
ChiTaRS; MBD2; human.
GeneWiki; Methyl-CpG-binding_domain_protein_2; -.
GenomeRNAi; 8932; -.
PRO; PR:Q9UBB5; -.
Proteomes; UP000005640; Chromosome 18.
Bgee; ENSG00000134046; -.
CleanEx; HS_MBD2; -.
ExpressionAtlas; Q9UBB5; baseline and differential.
Genevisible; Q9UBB5; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0000792; C:heterochromatin; IEA:Ensembl.
GO; GO:0000118; C:histone deacetylase complex; IEA:Ensembl.
GO; GO:0000790; C:nuclear chromatin; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0070742; F:C2H2 zinc finger domain binding; IPI:UniProtKB.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0008327; F:methyl-CpG binding; IDA:UniProtKB.
GO; GO:0003729; F:mRNA binding; IEA:Ensembl.
GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
GO; GO:0003696; F:satellite DNA binding; TAS:ProtInc.
GO; GO:0035197; F:siRNA binding; IEA:Ensembl.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0043044; P:ATP-dependent chromatin remodeling; IDA:UniProtKB.
GO; GO:0043623; P:cellular protein complex assembly; IEA:Ensembl.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
GO; GO:0000183; P:chromatin silencing at rDNA; TAS:Reactome.
GO; GO:0048568; P:embryonic organ development; IEA:Ensembl.
GO; GO:0007507; P:heart development; IEA:Ensembl.
GO; GO:0042711; P:maternal behavior; IEA:Ensembl.
GO; GO:0006346; P:methylation-dependent chromatin silencing; IGI:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IBA:GO_Central.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; NAS:UniProtKB.
GO; GO:0035563; P:positive regulation of chromatin binding; IEA:Ensembl.
GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IEA:Ensembl.
GO; GO:0042127; P:regulation of cell proliferation; IEA:Ensembl.
GO; GO:0044030; P:regulation of DNA methylation; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR016177; DNA-bd_dom_sf.
InterPro; IPR032343; MBD2/MBD3_p55-bd.
InterPro; IPR025884; MeCpG-bd_2/3_C_dom.
InterPro; IPR001739; Methyl_CpG_DNA-bd.
Pfam; PF01429; MBD; 1.
Pfam; PF14048; MBD_C; 1.
Pfam; PF16564; MBDa; 1.
SMART; SM00391; MBD; 1.
SUPFAM; SSF54171; SSF54171; 1.
PROSITE; PS50982; MBD; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; DNA-binding;
Nucleus; Phosphoprotein; Reference proteome; Transcription;
Transcription regulation.
CHAIN 1 411 Methyl-CpG-binding domain protein 2.
/FTId=PRO_0000096260.
DOMAIN 145 213 MBD. {ECO:0000255|PROSITE-
ProRule:PRU00338}.
REGION 1 149 Necessary for interaction with DHX9.
{ECO:0000269|PubMed:12665568}.
COMPBIAS 6 140 Gly-rich.
COMPBIAS 50 96 Arg-rich.
MOD_RES 181 181 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 407 407 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
VAR_SEQ 235 302 GKPDLNTTLPIRQTASIFKQPVTKVTNHPSNKVKSDPQRMN
EQPRQLFWEKRLQGLSASDVTEQIIKT -> LRWNTHRPAP
WHALSRLCLLIRCLLCLECAYPLPLHLVNSYSSKTQLHCLH
LWEACPAYSRQNQSFPP (in isoform 3).
{ECO:0000303|PubMed:9774669}.
/FTId=VSP_011077.
VAR_SEQ 303 411 Missing (in isoform 3).
{ECO:0000303|PubMed:9774669}.
/FTId=VSP_011078.
HELIX 366 388 {ECO:0000244|PDB:2L2L}.
TURN 389 392 {ECO:0000244|PDB:2L2L}.
SEQUENCE 411 AA; 43255 MW; FC4E5E0CF9BA0FFA CRC64;
MRAHPGGGRC CPEQEEGESA AGGSGAGGDS AIEQGGQGSA LAPSPVSGVR REGARGGGRG
RGRWKQAGRG GGVCGRGRGR GRGRGRGRGR GRGRGRPPSG GSGLGGDGGG CGGGGSGGGG
APRREPVPFP SGSAGPGPRG PRATESGKRM DCPALPPGWK KEEVIRKSGL SAGKSDVYYF
SPSGKKFRSK PQLARYLGNT VDLSSFDFRT GKMMPSKLQK NKQRLRNDPL NQNKGKPDLN
TTLPIRQTAS IFKQPVTKVT NHPSNKVKSD PQRMNEQPRQ LFWEKRLQGL SASDVTEQII
KTMELPKGLQ GVGPGSNDET LLSAVASALH TSSAPITGQV SAAVEKNPAV WLNTSQPLCK
AFIVTDEDIR KQEERVQQVR KKLEEALMAD ILSRAADTEE MDIEMDSGDE A


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E9572h Human Methyl CpG Binding Domain Protein 2 ELISA Ki 96T
MBD3 MBD1 Gene methyl-CpG binding domain protein 1
pro-1243 Recombinant Human Methyl-CpG Binding Domain Protein 3 10
EpiQuik Methyl-CpG Binding Domain Protein 2 ChIP Kit (24 reactions)


 

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