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Transcriptional repressor CTCF (11-zinc finger protein) (CCCTC-binding factor) (CTCFL paralog)

 CTCF_MOUSE              Reviewed;         736 AA.
Q61164;
23-APR-2003, integrated into UniProtKB/Swiss-Prot.
23-APR-2003, sequence version 2.
22-NOV-2017, entry version 153.
RecName: Full=Transcriptional repressor CTCF;
AltName: Full=11-zinc finger protein;
AltName: Full=CCCTC-binding factor;
AltName: Full=CTCFL paralog;
Name=Ctcf;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
STRAIN=BDF1;
PubMed=8649389; DOI=10.1128/MCB.16.6.2802;
Filippova G.N., Fagerlie S., Klenova E.M., Myers C., Dehner Y.,
Goodwin G., Neiman P.E., Collins S.J., Lobanenkov V.V.;
"An exceptionally conserved transcriptional repressor, CTCF, employs
different combinations of zinc fingers to bind diverged promoter
sequences of avian and mammalian c-myc oncogenes.";
Mol. Cell. Biol. 16:2802-2813(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Brain, Mammary gland, and Olfactory epithelium;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-201.
STRAIN=C57BL/6J; TISSUE=Extraembryonic tissue, and Placenta;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
FUNCTION.
PubMed=11743158; DOI=10.1126/science.1065982;
Chao W., Huynh K.D., Spencer R.J., Davidow L.S., Lee J.T.;
"CTCF, a candidate trans-acting factor for X-inactivation choice.";
Science 295:345-347(2002).
[5]
FUNCTION.
PubMed=15669143; DOI=10.1016/j.devcel.2004.10.018;
Filippova G.N., Cheng M.K., Moore J.M., Truong J.-P., Hu Y.J.,
Nguyen D.K., Tsuchiya K.D., Disteche C.M.;
"Boundaries between chromosomal domains of X inactivation and escape
bind CTCF and lack CpG methylation during early development.";
Dev. Cell 8:31-42(2005).
[6]
FUNCTION.
PubMed=16951251; DOI=10.1101/gad.399506;
Splinter E., Heath H., Kooren J., Palstra R.-J., Klous P.,
Grosveld F., Galjart N., de Laat W.;
"CTCF mediates long-range chromatin looping and local histone
modification in the beta-globin locus.";
Genes Dev. 20:2349-2354(2006).
[7]
INTERACTION WITH CHD8.
PubMed=16949368; DOI=10.1016/j.molcel.2006.08.008;
Ishihara K., Oshimura M., Nakao M.;
"CTCF-dependent chromatin insulator is linked to epigenetic
remodeling.";
Mol. Cell 23:733-742(2006).
[8]
FUNCTION.
PubMed=16614224; DOI=10.1126/science.1123191;
Ling J.Q., Li T., Hu J.F., Vu T.H., Chen H.L., Qiu X.W., Cherry A.M.,
Hoffman A.R.;
"CTCF mediates interchromosomal colocalization between Igf2/H19 and
Wsb1/Nf1.";
Science 312:269-272(2006).
[9]
FUNCTION.
PubMed=17329968; DOI=10.4161/cc.6.4.3854;
Bergstroem R., Whitehead J., Kurukuti S., Ohlsson R.;
"CTCF regulates asynchronous replication of the imprinted H19/Igf2
domain.";
Cell Cycle 6:450-454(2007).
[10]
FUNCTION.
PubMed=17952071; DOI=10.1038/ng.2007.5;
Xu N., Donohoe M.E., Silva S.S., Lee J.T.;
"Evidence that homologous X-chromosome pairing requires transcription
and Ctcf protein.";
Nat. Genet. 39:1390-1396(2007).
[11]
FUNCTION.
PubMed=18614575; DOI=10.1242/dev.024539;
Wan L.-B., Pan H., Hannenhalli S., Cheng Y., Ma J., Fedoriw A.,
Lobanenkov V., Latham K.E., Schultz R.M., Bartolomei M.S.;
"Maternal depletion of CTCF reveals multiple functions during oocyte
and preimplantation embryo development.";
Development 135:2729-2738(2008).
[12]
SUMOYLATION AT LYS-74 AND LYS-698, AND MUTAGENESIS OF LYS-74 AND
LYS-698.
PubMed=19029252; DOI=10.1128/MCB.00825-08;
MacPherson M.J., Beatty L.G., Zhou W., Du M., Sadowski P.D.;
"The CTCF insulator protein is posttranslationally modified by SUMO.";
Mol. Cell. Biol. 29:714-725(2009).
[13]
INTERACTION WITH LLPH.
PubMed=26961175; DOI=10.1038/srep22892;
Yu N.K., Kim H.F., Shim J., Kim S., Kim D.W., Kwak C., Sim S.E.,
Choi J.H., Ahn S., Yoo J., Choi S.L., Jang D.J., Lim C.S., Lee Y.S.,
Kang C., Choi S.Y., Kaang B.K.;
"A transducible nuclear/nucleolar protein, mLLP, regulates neuronal
morphogenesis and synaptic transmission.";
Sci. Rep. 6:22892-22892(2016).
-!- FUNCTION: Chromatin binding factor that binds to DNA sequence
specific sites. Involved in transcriptional regulation by binding
to chromatin insulators and preventing interaction between
promoter and nearby enhancers and silencers. Acts as
transcriptional repressor binding to promoters of vertebrate MYC
gene and BAG1 gene. Also binds to the PLK and PIM1 promoters. Acts
as a transcriptional activator of APP. Regulates APOA1/C3/A4/A5
gene cluster and controls MHC class II gene expression. Plays an
essential role in oocyte and preimplantation embryo development by
activating or repressing transcription. Seems to act as tumor
suppressor. Plays a critical role in the epigenetic regulation.
Participates in the allele-specific gene expression at the
imprinted IGF2/H19 gene locus. On the maternal allele, binding
within the H19 imprinting control region (ICR) mediates maternally
inherited higher-order chromatin conformation to restrict enhancer
access to IGF2. Plays a critical role in gene silencing over
considerable distances in the genome. Preferentially interacts
with unmethylated DNA, preventing spreading of CpG methylation and
maintaining methylation-free zones. Inversely, binding to target
sites is prevented by CpG methylation. Plays a important role in
chromatin remodeling. Can dimerize when it is bound to different
DNA sequences, mediating long-range chromatin looping (By
similarity). Mediates interchromosomal association between
IGF2/H19 and WSB1/NF1 and may direct distant DNA segments to a
common transcription factory. Causes local loss of histone
acetylation and gain of histone methylation in the beta-globin
locus, without affecting transcription. When bound to chromatin,
it provides an anchor point for nucleosomes positioning. Seems to
be essential for homologous X-chromosome pairing. May participate
with Tsix in establishing a regulatable epigenetic switch for X
chromosome inactivation. May play a role in preventing the
propagation of stable methylation at the escape genes from X-
inactivation. Involved in sister chromatid cohesion. Associates
with both centromeres and chromosomal arms during metaphase and
required for cohesin localization to CTCF sites. Regulates
asynchronous replication of IGF2/H19. Plays a role in the
recruitment of CENPE to the pericentromeric/centromeric regions of
the chromosome during mitosis (By similarity).
{ECO:0000250|UniProtKB:P49711, ECO:0000269|PubMed:11743158,
ECO:0000269|PubMed:15669143, ECO:0000269|PubMed:16614224,
ECO:0000269|PubMed:16951251, ECO:0000269|PubMed:17329968,
ECO:0000269|PubMed:17952071, ECO:0000269|PubMed:18614575}.
-!- SUBUNIT: Interacts with CHD8 (PubMed:16949368). Interacts with
LLPH (PubMed:26961175). Interacts with CENPE (By similarity).
{ECO:0000250|UniProtKB:P49711, ECO:0000269|PubMed:16949368,
ECO:0000269|PubMed:26961175}.
-!- INTERACTION:
Q09XV5:Chd8; NbExp=3; IntAct=EBI-932785, EBI-1169080;
-!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
{ECO:0000305|PubMed:8649389}. Chromosome
{ECO:0000250|UniProtKB:P49711}. Chromosome, centromere
{ECO:0000250|UniProtKB:P49711}. Note=May translocate to the
nucleolus upon cell differentiation. Associates with both
centromeres and chromosomal arms during metaphase. Associates with
the H19 ICR in mitotic chromosomes. May be preferentially excluded
from heterochromatin during interphase.
{ECO:0000250|UniProtKB:P49711}.
-!- PTM: Sumoylated on Lys-74 and Lys-698; sumoylation of CTCF
contributes to the repressive function of CTCF on the MYC P2
promoter. {ECO:0000269|PubMed:19029252}.
-!- SIMILARITY: Belongs to the CTCF zinc-finger protein family.
{ECO:0000305}.
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EMBL; U51037; AAC52928.1; -; mRNA.
EMBL; BC037456; AAH37456.1; -; mRNA.
EMBL; BC046398; AAH46398.1; -; mRNA.
EMBL; BC049131; AAH49131.1; -; mRNA.
EMBL; BC058240; AAH58240.1; -; mRNA.
EMBL; AK076192; BAC36245.1; -; mRNA.
CCDS; CCDS22606.1; -.
RefSeq; NP_851839.1; NM_181322.3.
RefSeq; XP_006530711.1; XM_006530648.2.
UniGene; Mm.269474; -.
ProteinModelPortal; Q61164; -.
SMR; Q61164; -.
BioGrid; 198963; 19.
DIP; DIP-38020N; -.
IntAct; Q61164; 16.
MINT; MINT-4092474; -.
STRING; 10090.ENSMUSP00000005841; -.
iPTMnet; Q61164; -.
PhosphoSitePlus; Q61164; -.
EPD; Q61164; -.
MaxQB; Q61164; -.
PaxDb; Q61164; -.
PeptideAtlas; Q61164; -.
PRIDE; Q61164; -.
Ensembl; ENSMUST00000005841; ENSMUSP00000005841; ENSMUSG00000005698.
GeneID; 13018; -.
KEGG; mmu:13018; -.
UCSC; uc009ndm.2; mouse.
CTD; 10664; -.
MGI; MGI:109447; Ctcf.
eggNOG; KOG1721; Eukaryota.
eggNOG; COG5048; LUCA.
GeneTree; ENSGT00890000139371; -.
HOGENOM; HOG000276534; -.
HOVERGEN; HBG000350; -.
InParanoid; Q61164; -.
OMA; EGEPMIC; -.
OrthoDB; EOG091G06B4; -.
PhylomeDB; Q61164; -.
TreeFam; TF106430; -.
ChiTaRS; Ctcf; mouse.
PRO; PR:Q61164; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000005698; -.
CleanEx; MM_CTCF; -.
Genevisible; Q61164; MM.
GO; GO:0000775; C:chromosome, centromeric region; ISS:UniProtKB.
GO; GO:0000793; C:condensed chromosome; ISO:MGI.
GO; GO:0005730; C:nucleolus; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0043035; F:chromatin insulator sequence binding; ISO:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; ISO:MGI.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; ISO:MGI.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISO:MGI.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding; IDA:MGI.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding; ISO:MGI.
GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
GO; GO:0006306; P:DNA methylation; IDA:MGI.
GO; GO:0009048; P:dosage compensation by inactivation of X chromosome; TAS:MGI.
GO; GO:0010216; P:maintenance of DNA methylation; IMP:MGI.
GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0016584; P:nucleosome positioning; ISO:MGI.
GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0071459; P:protein localization to chromosome, centromeric region; ISS:UniProtKB.
GO; GO:0006349; P:regulation of gene expression by genetic imprinting; IDA:MGI.
GO; GO:0040029; P:regulation of gene expression, epigenetic; ISO:MGI.
GO; GO:0035065; P:regulation of histone acetylation; IMP:UniProtKB.
GO; GO:0031060; P:regulation of histone methylation; IMP:UniProtKB.
GO; GO:0040030; P:regulation of molecular function, epigenetic; ISO:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
SMART; SM00355; ZnF_C2H2; 11.
SUPFAM; SSF57667; SSF57667; 7.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11.
1: Evidence at protein level;
Acetylation; Activator; Centromere; Chromatin regulator; Chromosome;
Chromosome partition; Complete proteome; DNA-binding; Isopeptide bond;
Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
Repressor; Transcription; Transcription regulation; Tumor suppressor;
Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 736 Transcriptional repressor CTCF.
/FTId=PRO_0000047229.
ZN_FING 266 288 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 294 316 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 322 345 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 351 373 C2H2-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 379 401 C2H2-type 5. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 407 430 C2H2-type 6. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 437 460 C2H2-type 7. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 467 489 C2H2-type 8. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 495 517 C2H2-type 9. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 523 546 C2H2-type 10. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 555 577 C2H2-type 11; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00042}.
COMPBIAS 635 676 Pro-rich.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P49711}.
MOD_RES 289 289 Phosphothreonine.
{ECO:0000250|UniProtKB:P49711}.
MOD_RES 317 317 Phosphothreonine.
{ECO:0000250|UniProtKB:P49711}.
MOD_RES 374 374 Phosphothreonine.
{ECO:0000250|UniProtKB:P49711}.
MOD_RES 402 402 Phosphoserine.
{ECO:0000250|UniProtKB:P49711}.
MOD_RES 609 609 Phosphoserine.
{ECO:0000250|UniProtKB:P49711}.
MOD_RES 610 610 Phosphoserine.
{ECO:0000250|UniProtKB:P49711}.
MOD_RES 612 612 Phosphoserine.
{ECO:0000250|UniProtKB:P49711}.
CROSSLNK 18 18 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P49711}.
CROSSLNK 74 74 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
CROSSLNK 219 219 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P49711}.
CROSSLNK 698 698 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate.
CROSSLNK 698 698 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P49711}.
MUTAGEN 74 74 K->R: No sumoylation.
{ECO:0000269|PubMed:19029252}.
MUTAGEN 698 698 K->R: No sumoylation.
{ECO:0000269|PubMed:19029252}.
CONFLICT 38 38 C -> S (in Ref. 1; AAC52928).
{ECO:0000305}.
CONFLICT 257 257 I -> K (in Ref. 2; AAH37456).
{ECO:0000305}.
SEQUENCE 736 AA; 83745 MW; 7C49D4A7BDCFEFA1 CRC64;
MEGEAVEAIV EESETFIKGK ERKTYQRRRE GGQEEDACHL PQNQTDGGEV VQDVNSSVQM
VMMEQLDPTL LQMKTEVMEG TVAPEAEAAV DDTQIITLQV VNMEEQPINI GELQLVQVPV
PVTVPVATTS VEELQGAYEN EVSKEGLAES EPMICHTLPL PEGFQVVKVG ANGEVETLEQ
GELPPQEDSS WQKDPDYQPP AKKTKKTKKS KLRYTEEGKD VDVSVYDFEE EQQEGLLSEV
NAEKVVGNMK PPKPTKIKKK GVKKTFQCEL CSYTCPRRSN LDRHMKSHTD ERPHKCHLCG
RAFRTVTLLR NHLNTHTGTR PHKCPDCDMA FVTSGELVRH RRYKHTHEKP FKCSMCDYAS
VEVSKLKRHI RSHTGERPFQ CSLCSYASRD TYKLKRHMRT HSGEKPYECY ICHARFTQSG
TMKMHILQKH TENVAKFHCP HCDTVIARKS DLGVHLRKQH SYIEQGKKCR YCDAVFHERY
ALIQHQKSHK NEKRFKCDQC DYACRQERHM IMHKRTHTGE KPYACSHCDK TFRQKQLLDM
HFKRYHDPNF VPAAFVCSKC GKTFTRRNTM ARHADNCAGP DGVEGENGGE TKKSKRGRKR
KMRSKKEDSS DSEENAEPDL DDNEEEEEPA VEIEPEPEPQ PQPPPPPQPV APAPPPAKKR
RGRPPGRTNQ PKQNQPTAII QVEDQNTGAI ENIIVEVKKE PDAEPAEGEE EEAQAATTDA
PNGDLTPEMI LSMMDR


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28-436 CTCFL is a paralog of CTCF and appears to be expressed primarily in the cytoplasm of spermatocytes. CTCFL is normally expressed in a mutually exclusive pattern that correlates with resetting of methyl 0.05 mg
EIAAB47268 Beta enolase repressor factor 1,G-rich box-binding protein,Mouse,Mus musculus,Transcription factor BFCOL1,Transcription factor ZBP-89,Zbp89,Zfp148,Zinc finger DNA-binding protein 89,Zinc finger protei
abx111451 Polyclonal Rabbit Ccctc-Binding Factor (Zinc Finger Protein)-Like Antibody 50 μl
abx111450 Polyclonal Rabbit Ccctc-Binding Factor (Zinc Finger Protein) Antibody 50 μl


 

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