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Transcription factor Sp1

 SP1_MOUSE               Reviewed;         784 AA.
O89090; O89087; Q62251; Q64167;
09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
21-JUN-2005, sequence version 2.
18-JUL-2018, entry version 165.
RecName: Full=Transcription factor Sp1;
AltName: Full=Specificity protein 1 {ECO:0000303|PubMed:27918959};
Name=Sp1;
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] (ISOFORM 1).
TISSUE=Neuroblastoma;
PubMed=9628590; DOI=10.1089/dna.1998.17.471;
Yajima S., Lee S.H., Minowa T., Mouradian M.M.;
"Sp family transcription factors regulate expression of rat D2
dopamine receptor gene.";
DNA Cell Biol. 17:471-479(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=7568082; DOI=10.1073/pnas.92.20.9107;
Persengiev S.P., Saffer J.D., Kilpatrick D.L.;
"An alternatively spliced form of the transcription factor Sp1
containing only a single glutamine-rich transactivation domain.";
Proc. Natl. Acad. Sci. U.S.A. 92:9107-9111(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Thymus;
Park E.J., Kim J.H., Kim C.G., Park S.D., Hong S.S.;
"Isolation of cDNA encoding transcription factor sp1 containing two
glutamine-rich transactivation domain.";
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 684-784.
PubMed=1633330; DOI=10.3109/10425179209030966;
Chestier A., Charnay P.;
"Difference in the genomic organizations of the related transcription
factors Sp1 and Krox-20; possible evolutionary significance.";
DNA Seq. 2:325-327(1992).
[5]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
FUNCTION.
PubMed=24030830; DOI=10.1074/jbc.M113.507038;
Xiao J., Zhou Y., Lai H., Lei S., Chi L.H., Mo X.;
"Transcription factor NF-Y is a functional regulator of the
transcription of core clock gene Bmal1.";
J. Biol. Chem. 288:31930-31936(2013).
[8]
FUNCTION, INTERACTION WITH RNF112, INDUCTION, AND SUBCELLULAR
LOCATION.
PubMed=27918959; DOI=10.1016/j.redox.2016.11.012;
Chuang J.Y., Kao T.J., Lin S.H., Wu A.C., Lee P.T., Su T.P., Yeh S.H.,
Lee Y.C., Wu C.C., Chang W.C.;
"Specificity protein 1-zinc finger protein 179 pathway is involved in
the attenuation of oxidative stress following brain injury.";
Redox Biol. 11:135-143(2017).
-!- FUNCTION: Transcription factor that can activate or repress
transcription in response to physiological and pathological
stimuli. Binds with high affinity to GC-rich motifs and regulates
the expression of a large number of genes involved in a variety of
processes such as cell growth, apoptosis, differentiation and
immune responses. Highly regulated by post-translational
modifications (phosphorylations, sumoylation, proteolytic
cleavage, glycosylation and acetylation). Binds also the PDGFR-
alpha G-box promoter. May have a role in modulating the cellular
response to DNA damage. Implicated in chromatin remodeling. Plays
a role in the recruitment of SMARCA4/BRG1 on the c-FOS promoter
Plays an essential role in the regulation of FE65 gene expression
(By similarity). Positively regulates the transcription of the
core clock component ARNTL/BMAL1 (PubMed:24030830). Plays a role
in protecting cells against oxidative stress following brain
injury by regulating the expression of RNF112 (PubMed:27918959).
{ECO:0000250|UniProtKB:P08047, ECO:0000250|UniProtKB:Q01714,
ECO:0000269|PubMed:24030830, ECO:0000269|PubMed:27918959}.
-!- SUBUNIT: Interacts with ATF7IP, ATF7IP2, BAHD1, POGZ, HCFC1, AATF
and PHC2. Interacts with SV40 VP2/3 proteins. Interacts with SV40
major capsid protein VP1; this interaction leads to a
cooperativity between the 2 proteins in DNA binding. Interacts
with HLTF; the interaction may be required for basal
transcriptional activity of HLTF. Interacts (deacetylated form)
with EP300; the interaction enhances gene expression. Interacts
with HDAC1 and JUN. Interacts with ELF1; the interaction is
inhibited by glycosylation of SP1. Interaction with NFYA; the
interaction is inhibited by glycosylation of SP1. Interacts with
SMARCA4/BRG1. Interacts with ATF7IP and TBP. Interacts with MEIS2
isoform 4 and PBX1 isoform PBX1a. Interacts with EGR1 (By
similarity). Interacts with RNF112 in an oxidative stress-
regulated manner (PubMed:27918959). {ECO:0000250|UniProtKB:P08047,
ECO:0000250|UniProtKB:Q01714, ECO:0000269|PubMed:27918959}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27918959}.
Cytoplasm {ECO:0000250}. Note=Nuclear location is governed by
glycosylated/phosphorylated states. Insulin promotes nuclear
location, while glucagon favors cytoplasmic location (By
similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O89090-1; Sequence=Displayed;
Name=2; Synonyms=Sp1-S;
IsoId=O89090-2; Sequence=VSP_007376;
-!- INDUCTION: Up-regulated by traumatic brain injury and hydrogen
peroxide (at protein level)(PubMed:27918959).
{ECO:0000269|PubMed:27918959}.
-!- PTM: Phosphorylated on multiple serine and threonine residues.
Phosphorylation is coupled to ubiquitination, sumoylation and
proteolytic processing. Phosphorylation on Ser-61 enhances
proteolytic cleavage. Phosphorylation on Ser-7 enhances
ubiquitination and protein degradation. Hyperphosphorylation on
Ser-103 in response to DNA damage has no effect on transcriptional
activity. MAPK1/MAPK3-mediated phosphorylation on Thr-455 and Thr-
738 enhances VEGF transcription but, represses FGF2-triggered
PDGFR-alpha transcription. Also implicated in the repression of
RECK by ERBB2. Hyperphosphorylated on Thr-280 and Thr-738 during
mitosis by MAPK8 shielding SP1 from degradation by the ubiquitin-
dependent pathway. Phosphorylated in the zinc-finger domain by
calmodulin-activated PKCzeta. Phosphorylation on Ser-642 by
PKCzeta is critical for TSA-activated LHR gene expression through
release of its repressor, p107. Phosphorylation on Thr-669, Ser-
671 and Thr-682 is stimulated by angiotensin II via the AT1
receptor inducing increased binding to the PDGF-D promoter. This
phosphorylation is increased in injured artey wall. Ser-61 and
Thr-682 can both be dephosphorylated by PP2A during cell-cycle
interphase. Dephosphorylation on Ser-61 leads to increased
chromatin association during interphase and increases the
transcriptional activity. On insulin stimulation, sequentially
glycosylated and phosphorylated on several C-terminal serine and
threonine residues (By similarity). {ECO:0000250}.
-!- PTM: Acetylated. Acetylation/deacetylation events affect
transcriptional activity. Deacetylation leads to an increase in
the expression the 12(s)-lipooxygenase gene though recruitment of
p300 to the promoter (By similarity). {ECO:0000250}.
-!- PTM: Ubiquitinated. Ubiquitination occurs on the C-terminal
proteolytically-cleaved peptide and is triggered by
phosphorylation (By similarity). {ECO:0000250}.
-!- PTM: Sumoylated with SUMO1. Sumoylation modulates proteolytic
cleavage of the N-terminal repressor domain. Sumoylation levels
are attenuated during tumorigenesis. Phosphorylation mediates SP1
desumoylation (By similarity). {ECO:0000250}.
-!- PTM: Proteolytic cleavage in the N-terminal repressor domain is
prevented by sumoylation. The C-terminal cleaved product is
susceptible to degradation (By similarity). {ECO:0000250}.
-!- PTM: O-glycosylated; Contains 8 N-acetylglucosamine side chains.
Levels are controlled by insulin and the SP1 phosphorylation
states. Insulin-mediated O-glycosylation locates SP1 to the
nucleus, where it is sequentially deglycosylated and
phosphorylated. O-glycosylation affects transcriptional activity
through disrupting the interaction with a number of transcription
factors including ELF1 and NFYA. Inhibited by peroxisomome
proliferator receptor gamma (PPARgamma) (By similarity).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein
family. {ECO:0000305}.
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EMBL; AF062566; AAC16484.1; -; mRNA.
EMBL; S79832; AAB35321.1; -; mRNA.
EMBL; AF022363; AAC08527.1; -; mRNA.
EMBL; X60136; CAA42721.1; -; Genomic_DNA.
PIR; S30493; S30493.
RefSeq; NP_038700.2; NM_013672.2.
UniGene; Mm.4618; -.
ProteinModelPortal; O89090; -.
SMR; O89090; -.
BioGrid; 203414; 28.
CORUM; O89090; -.
DIP; DIP-35276N; -.
IntAct; O89090; 10.
MINT; O89090; -.
STRING; 10090.ENSMUSP00000001326; -.
iPTMnet; O89090; -.
PhosphoSitePlus; O89090; -.
EPD; O89090; -.
MaxQB; O89090; -.
PaxDb; O89090; -.
PeptideAtlas; O89090; -.
PRIDE; O89090; -.
DNASU; 20683; -.
Ensembl; ENSMUST00000163709; ENSMUSP00000130747; ENSMUSG00000001280. [O89090-2]
GeneID; 20683; -.
KEGG; mmu:20683; -.
UCSC; uc012aab.1; mouse. [O89090-2]
CTD; 6667; -.
MGI; MGI:98372; Sp1.
eggNOG; KOG1721; Eukaryota.
eggNOG; COG5048; LUCA.
GeneTree; ENSGT00760000118984; -.
HOGENOM; HOG000234295; -.
HOVERGEN; HBG008933; -.
InParanoid; O89090; -.
KO; K04684; -.
Reactome; R-MMU-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
Reactome; R-MMU-6807505; RNA polymerase II transcribes snRNA genes.
Reactome; R-MMU-9018519; Estrogen-dependent gene expression.
PRO; PR:O89090; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000001280; -.
CleanEx; MM_SP1; -.
ExpressionAtlas; O89090; baseline and differential.
Genevisible; O89090; MM.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0032993; C:protein-DNA complex; ISO:MGI.
GO; GO:0017053; C:transcriptional repressor complex; ISO:MGI.
GO; GO:0043425; F:bHLH transcription factor binding; IPI:BHF-UCL.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0003700; F:DNA binding transcription factor activity; IDA:MGI.
GO; GO:0003690; F:double-stranded DNA binding; IDA:MGI.
GO; GO:0035326; F:enhancer binding; IDA:MGI.
GO; GO:0035035; F:histone acetyltransferase binding; ISO:MGI.
GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
GO; GO:0071837; F:HMG box domain binding; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0000987; F:proximal promoter sequence-specific DNA binding; IDA:MGI.
GO; GO:0070491; F:repressing transcription factor binding; ISO:MGI.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; ISO:MGI.
GO; GO:0001103; F:RNA polymerase II repressing transcription factor binding; IPI:BHF-UCL.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
GO; GO:0000982; F:transcription factor activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:MGI.
GO; GO:0008134; F:transcription factor binding; ISO:MGI.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISO:MGI.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:MGI.
GO; GO:0032869; P:cellular response to insulin stimulus; ISO:MGI.
GO; GO:0060216; P:definitive hemopoiesis; IGI:MGI.
GO; GO:0048596; P:embryonic camera-type eye morphogenesis; IGI:MGI.
GO; GO:0001892; P:embryonic placenta development; IGI:MGI.
GO; GO:0060136; P:embryonic process involved in female pregnancy; IGI:MGI.
GO; GO:0048706; P:embryonic skeletal system development; IGI:MGI.
GO; GO:0043353; P:enucleate erythrocyte differentiation; IGI:MGI.
GO; GO:0001701; P:in utero embryonic development; IGI:MGI.
GO; GO:0001889; P:liver development; IGI:MGI.
GO; GO:0030324; P:lung development; IGI:MGI.
GO; GO:0030219; P:megakaryocyte differentiation; IGI:MGI.
GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IDA:MGI.
GO; GO:0001503; P:ossification; IGI:MGI.
GO; GO:0043923; P:positive regulation by host of viral transcription; ISO:MGI.
GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISO:MGI.
GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
GO; GO:1904828; P:positive regulation of hydrogen sulfide biosynthetic process; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:1905564; P:positive regulation of vascular endothelial cell proliferation; ISO:MGI.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0033194; P:response to hydroperoxide; IDA:UniProtKB.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
GO; GO:0001829; P:trophectodermal cell differentiation; IGI:MGI.
InterPro; IPR030449; SP1.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
PANTHER; PTHR23235:SF16; PTHR23235:SF16; 1.
SMART; SM00355; ZnF_C2H2; 3.
SUPFAM; SSF57667; SSF57667; 1.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
1: Evidence at protein level;
Acetylation; Activator; Alternative splicing; Biological rhythms;
Complete proteome; Cytoplasm; DNA-binding; Glycoprotein;
Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:17242355}.
CHAIN 2 784 Transcription factor Sp1.
/FTId=PRO_0000047138.
ZN_FING 627 656 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 657 686 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 687 714 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
REGION 2 84 Repressor domain. {ECO:0000250}.
REGION 148 253 Transactivation domain A (Gln-rich).
{ECO:0000250}.
REGION 263 497 Transactivation domain B (Gln-rich).
{ECO:0000250}.
REGION 498 611 Transactivation domain C (highly
charged). {ECO:0000250}.
REGION 620 784 VZV IE62-binding. {ECO:0000250}.
REGION 709 784 Domain D. {ECO:0000250}.
COMPBIAS 37 145 Ser/Thr-rich.
COMPBIAS 273 381 Ser/Thr-rich.
SITE 65 66 Cleavage. {ECO:0000250}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:17242355}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000250|UniProtKB:P08047}.
MOD_RES 7 7 Phosphoserine.
{ECO:0000250|UniProtKB:P08047}.
MOD_RES 61 61 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 103 103 Phosphoserine; by ATM.
{ECO:0000250|UniProtKB:P08047}.
MOD_RES 280 280 Phosphothreonine; by MAPK8.
{ECO:0000250|UniProtKB:P08047}.
MOD_RES 455 455 Phosphothreonine; by MAPK1 and MAPK3.
{ECO:0000250|UniProtKB:P08047}.
MOD_RES 613 613 Phosphoserine; alternate.
{ECO:0000250|UniProtKB:P08047}.
MOD_RES 641 641 Phosphothreonine; alternate.
{ECO:0000250|UniProtKB:P08047}.
MOD_RES 642 642 Phosphoserine; by PKC/PRKCZ; alternate.
{ECO:0000250|UniProtKB:P08047}.
MOD_RES 652 652 Phosphothreonine; by PKC/PRKCZ.
{ECO:0000250|UniProtKB:P08047}.
MOD_RES 669 669 Phosphothreonine.
{ECO:0000250|UniProtKB:P08047}.
MOD_RES 671 671 Phosphoserine; by PKC/PRKCZ.
{ECO:0000250|UniProtKB:P08047}.
MOD_RES 682 682 Phosphothreonine; by PKC/PRKCZ.
{ECO:0000250|UniProtKB:P08047}.
MOD_RES 699 699 Phosphoserine; alternate.
{ECO:0000250|UniProtKB:P08047}.
MOD_RES 703 703 Phosphoserine; alternate.
{ECO:0000250|UniProtKB:P08047}.
MOD_RES 704 704 N6-acetyllysine.
{ECO:0000250|UniProtKB:P08047}.
MOD_RES 738 738 Phosphothreonine; by MAPK1, MAPK3 and
MAPK8. {ECO:0000250|UniProtKB:P08047}.
CARBOHYD 493 493 O-linked (GlcNAc) serine. {ECO:0000250}.
CARBOHYD 613 613 O-linked (GlcNAc) serine; alternate.
{ECO:0000250}.
CARBOHYD 641 641 O-linked (GlcNAc) threonine; alternate.
{ECO:0000250}.
CARBOHYD 642 642 O-linked (GlcNAc) serine; alternate.
{ECO:0000250}.
CARBOHYD 699 699 O-linked (GlcNAc) serine; alternate.
{ECO:0000250}.
CARBOHYD 703 703 O-linked (GlcNAc) serine; alternate.
{ECO:0000250}.
CROSSLNK 16 16 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000250}.
CROSSLNK 16 16 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P08047}.
VAR_SEQ 56 372 Missing (in isoform 2).
{ECO:0000303|PubMed:7568082}.
/FTId=VSP_007376.
CONFLICT 100 100 T -> A (in Ref. 1; AAC16484).
{ECO:0000305}.
CONFLICT 131 133 Missing (in Ref. 1; AAC16484).
{ECO:0000305}.
CONFLICT 220 220 R -> E (in Ref. 3; AAC08527).
{ECO:0000305}.
CONFLICT 462 462 G -> V (in Ref. 1; AAC16484).
{ECO:0000305}.
SEQUENCE 784 AA; 80732 MW; B6B989F0A252CEE5 CRC64;
MSDQDHSMDE VTAVVKIEKD VGGNNGGSGN GGGAAFSQTR SSSTGSSSSS GGGGGQESQP
SPLALLAATC SRIESPNENS NNSQGPSQSG GTGELDLTAT QLSQGANGWQ IISSSSGATP
TSKEQSGNST NGSNGSESSK NRTVSGGQYV VAATPNLQNQ QVLTGLPGVM PNIQYQVIPQ
FQTVDGQQLQ FAATGAQVQQ DGSGQIQIIP GANQQIIPNR GSGGNIIAAM PNLLQQAVPL
QGLANNVLSG QTQYVTNVPV ALNGNITLLP VNSVSAATLT PSSQAGTISS SGSQESSSQP
VTSGTAISSA SLVSSQASSS SFFTNANSYS TTTTTSNMGI MNFTSSGSSG TSSQGQTPQR
VGGLQGSDSL NIQQNQTSGG SLQGSQQKEG EQSQQTQQQQ ILIQPQLVQG GQALQALQAA
PLSGQTFTTQ AISQETLQNL QLQAVQNSGP IIIRTPTVGP NGQVSWQTLQ LQNLQVQNPQ
AQTITLAPMQ GVSLGQTSSS NTTLTPIASA ASIPAGTVTV NAAQLSSMPG LQTINLSALG
TSGIQVHQLP GLPLAIANTP GDHGTQLGLH GSGGDGIHDE TAGGEGENSS DLQPQAGRRT
RREACTCPYC KDSEGRASGD PGKKKQHICH IQGCGKVYGK TSHLRAHLRW HTGERPFMCN
WSYCGKRFTR SDELQRHKRT HTGEKKFACP ECPKRFMRSD HLSKHIKTHQ NKKGGPGVAL
SVGTLPLDSG AGSEGTATPS ALITTNMVAM EAICPEGIAR LANSGINVMQ VTELQSINIS
GNGF


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18-003-42234 POU domain. class 2. transcription factor 3 - Octamer-binding transcription factor 11; Oct-11; Transcription factor Skn-1; PLA-1 protein Polyclonal 0.05 mg Aff Pur
18-003-42234 POU domain. class 2. transcription factor 3 - Octamer-binding transcription factor 11; Oct-11; Transcription factor Skn-1; PLA-1 protein Polyclonal 0.1 mg Protein A
EIAAB25651 Metal regulatory transcription factor 1,Mouse,MRE-binding transcription factor,Mtf1,Mtf-1,Mus musculus,Transcription factor MTF-1
18-003-42235 POU domain. class 2. transcription factor 3 - Octamer-binding transcription factor 11; Oct-11; Transcription factor Skn-1; PLA-1 protein Polyclonal 0.05 mg Aff Pur
18-003-43070 T-box transcription factor TBX21 - T-box protein 21; Transcription factor TBLYM; T-cell-specific T-box transcription factor T-bet Polyclonal 0.1 mg Protein A
18-003-42235 POU domain. class 2. transcription factor 3 - Octamer-binding transcription factor 11; Oct-11; Transcription factor Skn-1; PLA-1 protein Polyclonal 0.1 mg Protein A
EIAAB42078 HMG box transcription factor 4,Homo sapiens,hTCF-4,Human,T-cell factor 4,T-cell-specific transcription factor 4,TCF4,TCF-4,TCF7L2,Transcription factor 7-like 2
EIAAB42042 Basic transcription factor 2 44 kDa subunit,BTF2 p44,General transcription factor IIH polypeptide 2,General transcription factor IIH subunit 2,Gtf2h2,Rat,Rattus norvegicus,TFIIH basal transcription fa
EIAAB32964 bHLH transcription factor p48,Mouse,Mus musculus,p48 DNA-binding subunit of transcription factor PTF1,Pancreas transcription factor 1 subunit alpha,Pancreas-specific transcription factor 1a,Ptf1a,Ptf1
18-003-42999 Cyclic AMP-dependent transcription factor ATF-5 - Activating transcription factor 5; Transcription factor ATFx Polyclonal 0.05 mg Aff Pur
EIAAB42079 HMG box transcription factor 4,Mouse,mTCF-4,Mus musculus,T-cell factor 4,T-cell-specific transcription factor 4,Tcf4,TCF-4,Tcf7l2,Transcription factor 7-like 2
EIAAB47163 CREB_ATF bZIP transcription factor,Crebzf,HCF-binding transcription factor Zhangfei,Host cell factor-binding transcription factor Zhangfei,Mouse,Mus musculus,Tyrosine kinase-associated leucine zipper


 

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