Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Single-stranded DNA-binding protein (SSB) (Helix-destabilizing protein)

 SSB_ECOLI               Reviewed;         178 AA.
P0AGE0; P02339; Q2M6P5;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
28-MAR-2018, entry version 109.
RecName: Full=Single-stranded DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_00984};
Short=SSB {ECO:0000255|HAMAP-Rule:MF_00984};
AltName: Full=Helix-destabilizing protein;
Name=ssb; Synonyms=exrB, lexC; OrderedLocusNames=b4059, JW4020;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-53.
PubMed=6270666; DOI=10.1073/pnas.78.7.4274;
Sancar A., Williams K.R., Chase J.W., Rupp W.D.;
"Sequences of the ssb gene and protein.";
Proc. Natl. Acad. Sci. U.S.A. 78:4274-4278(1981).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6351061; DOI=10.1073/pnas.80.18.5480;
Chase J.W., Merrill B.M., Williams K.R.;
"F sex factor encodes a single-stranded DNA binding protein (SSB) with
extensive sequence homology to Escherichia coli SSB.";
Proc. Natl. Acad. Sci. U.S.A. 80:5480-5484(1983).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=8265357; DOI=10.1093/nar/21.23.5408;
Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J.,
Daniels D.L.;
"Analysis of the Escherichia coli genome. IV. DNA sequence of the
region from 89.2 to 92.8 minutes.";
Nucleic Acids Res. 21:5408-5417(1993).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
PROTEIN SEQUENCE OF 2-41.
PubMed=7042342; DOI=10.1111/j.1432-1033.1982.tb19784.x;
Beyreuther K., Berthold-Schmidt V., Geider K.;
"Biological activity and a partial amino-acid sequence of Escherichia
coli DNA-binding protein I isolated from overproducing cells.";
Eur. J. Biochem. 123:415-420(1982).
[7]
CHARACTERIZATION, AND SEQUENCE REVISION TO 134.
PubMed=6363409;
Chase J.W., L'Italien J.J., Murphy J.B., Spicer E.K., Williams K.R.;
"Characterization of the Escherichia coli SSB-113 mutant single-
stranded DNA-binding protein. Cloning of the gene, DNA and protein
sequence analysis, high pressure liquid chromatography peptide
mapping, and DNA-binding studies.";
J. Biol. Chem. 259:805-814(1984).
[8]
MUTANT SSB-1.
PubMed=6384214;
Williams K.R., Murphy J.B., Chase J.W.;
"Characterization of the structural and functional defect in the
Escherichia coli single-stranded DNA binding protein encoded by the
ssb-1 mutant gene. Expression of the ssb-1 gene under lambda pL
regulation.";
J. Biol. Chem. 259:11804-11811(1984).
[9]
MUTAGENESIS, AND DNA-BINDING.
PubMed=3301414; DOI=10.1016/0014-5793(87)80844-X;
Casas-Finet J.R., Khamis M.I., Maki A.W., Chase J.W.;
"Tryptophan 54 and phenylalanine 60 are involved synergistically in
the binding of E. coli SSB protein to single-stranded
polynucleotides.";
FEBS Lett. 220:347-352(1987).
[10]
REVIEW.
PubMed=2087220;
Meyer R.R., Laine P.S.;
"The single-stranded DNA-binding protein of Escherichia coli.";
Microbiol. Rev. 54:342-380(1990).
[11]
MUTANT SSB-1, AND DNA-BINDING.
PubMed=1988680; DOI=10.1016/0022-2836(91)90611-9;
Bujalowski W., Lohman T.M.;
"Monomers of the Escherichia coli SSB-1 mutant protein bind single-
stranded DNA.";
J. Mol. Biol. 217:63-74(1991).
[12]
INTERACTION WITH RECO.
PubMed=7962001;
Umezu K., Kolodner R.D.;
"Protein interactions in genetic recombination in Escherichia coli.
Interactions involving RecO and RecR overcome the inhibition of RecA
by single-stranded DNA-binding protein.";
J. Biol. Chem. 269:30005-30013(1994).
[13]
IDENTIFICATION BY 2D-GEL.
PubMed=9298644; DOI=10.1002/elps.1150180805;
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R.,
Neidhardt F.C.;
"Escherichia coli proteome analysis using the gene-protein database.";
Electrophoresis 18:1243-1251(1997).
[14]
MUTANTS SSB-200; SSB-201 AND SSB-202.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9139905; DOI=10.1128/jb.179.9.2892-2899.1997;
Reddy M., Gowrishankar J.;
"Identification and characterization of ssb and uup mutants with
increased frequency of precise excision of transposon Tn10
derivatives: nucleotide sequence of uup in Escherichia coli.";
J. Bacteriol. 179:2892-2899(1997).
[15]
INTERACTION WITH HOLC.
PubMed=9545254; DOI=10.1093/emboj/17.8.2436;
Kelman Z., Yuzhakov A., Andjelkovic J., O'Donnell M.;
"Devoted to the lagging strand-the subunit of DNA polymerase III
holoenzyme contacts SSB to promote processive elongation and sliding
clamp assembly.";
EMBO J. 17:2436-2449(1998).
[16]
INTERACTION WITH EXONUCLEASE I (SBCB).
PubMed=10782989; DOI=10.1515/BC.2000.025;
Genschel J., Curth U., Urbanke C.;
"Interaction of E. coli single-stranded DNA binding protein (SSB) with
exonuclease I. The carboxy-terminus of SSB is the recognition site for
the nuclease.";
Biol. Chem. 381:183-192(2000).
[17]
DNA-BINDING, AND INTERACTION WITH PRIA.
PubMed=15576682; DOI=10.1093/nar/gkh980;
Cadman C.J., McGlynn P.;
"PriA helicase and SSB interact physically and functionally.";
Nucleic Acids Res. 32:6378-6387(2004).
[18]
PHOSPHORYLATION.
PubMed=16549871; DOI=10.1093/nar/gkj514;
Mijakovic I., Petranovic D., Macek B., Cepo T., Mann M., Davies J.,
Jensen P.R., Vujaklija D.;
"Bacterial single-stranded DNA-binding proteins are phosphorylated on
tyrosine.";
Nucleic Acids Res. 34:1588-1596(2006).
[19]
INTERACTION WITH RECQ.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=17483090; DOI=10.1074/jbc.M608011200;
Shereda R.D., Bernstein D.A., Keck J.L.;
"A central role for SSB in Escherichia coli RecQ DNA helicase
function.";
J. Biol. Chem. 282:19247-19258(2007).
[20]
REVIEW, AND FUNCTION.
PubMed=18937104; DOI=10.1080/10409230802341296;
Shereda R.D., Kozlov A.G., Lohman T.M., Cox M.M., Keck J.L.;
"SSB as an organizer/mobilizer of genome maintenance complexes.";
Crit. Rev. Biochem. Mol. Biol. 43:289-318(2008).
[21]
INTERACTION WITH EXONUCLEASE I (SBCB), AND MUTAGENESIS OF PRO-177.
PubMed=18591666; DOI=10.1073/pnas.0800741105;
Lu D., Keck J.L.;
"Structural basis of Escherichia coli single-stranded DNA-binding
protein stimulation of exonuclease I.";
Proc. Natl. Acad. Sci. U.S.A. 105:9169-9174(2008).
[22]
FUNCTION, DNA-BINDING, AND ENZYME REGULATION.
PubMed=20360609; DOI=10.1074/jbc.M110.118273;
Kozlov A.G., Cox M.M., Lohman T.M.;
"Regulation of single-stranded DNA binding by the C termini of
Escherichia coli single-stranded DNA-binding (SSB) protein.";
J. Biol. Chem. 285:17246-17252(2010).
[23]
INTERACTION WITH EXONUCLEASE I (SBCB).
PubMed=20018747; DOI=10.1073/pnas.0909191107;
Lu D., Bernstein D.A., Satyshur K.A., Keck J.L.;
"Small-molecule tools for dissecting the roles of SSB/protein
interactions in genome maintenance.";
Proc. Natl. Acad. Sci. U.S.A. 107:633-638(2010).
[24]
FUNCTION.
PubMed=21784244; DOI=10.1016/j.cell.2011.06.036;
Zhou R., Kozlov A.G., Roy R., Zhang J., Korolev S., Lohman T.M.,
Ha T.;
"SSB functions as a sliding platform that migrates on DNA via
reptation.";
Cell 146:222-232(2011).
[25]
INTERACTION WITH DNAG.
PubMed=23430154; DOI=10.1093/nar/gkt107;
Naue N., Beerbaum M., Bogutzki A., Schmieder P., Curth U.;
"The helicase-binding domain of Escherichia coli DnaG primase
interacts with the highly conserved C-terminal region of single-
stranded DNA-binding protein.";
Nucleic Acids Res. 41:4507-4517(2013).
[26]
INTERACTION WITH PRIB.
PubMed=23963891; DOI=10.1007/s10930-013-9509-y;
Huang Y.H., Lin M.J., Huang C.Y.;
"Yeast two-hybrid analysis of PriB-interacting proteins in replication
restart primosome: a proposed PriB-SSB interaction model.";
Protein J. 32:477-483(2013).
[27]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-136, AND SUBUNIT.
PubMed=9192620; DOI=10.1073/pnas.94.13.6652;
Raghunathan S., Ricard C.S., Lohman T.M., Waksman G.;
"Crystal structure of the homo-tetrameric DNA binding domain of
Escherichia coli single-stranded DNA-binding protein determined by
multiwavelength X-ray diffraction on the selenomethionyl protein at
2.9-A resolution.";
Proc. Natl. Acad. Sci. U.S.A. 94:6652-6657(1997).
[28]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-136, DNA-BINDING, AND
SUBUNIT.
PubMed=10932248; DOI=10.1038/77943;
Raghunathan S., Kozlov A.G., Lohman T.M., Waksman G.;
"Structure of the DNA binding domain of E. coli SSB bound to ssDNA.";
Nat. Struct. Biol. 7:648-652(2000).
-!- FUNCTION: Plays an important role in DNA replication,
recombination and repair. Binds to ssDNA and to an array of
partner proteins to recruit them to their sites of action during
DNA metabolism. Acts as a sliding platform that migrates on DNA
via reptation. {ECO:0000255|HAMAP-Rule:MF_00984,
ECO:0000269|PubMed:18937104, ECO:0000269|PubMed:20360609,
ECO:0000269|PubMed:21784244}.
-!- ENZYME REGULATION: The C-terminal tail exerts an inhibitory effect
on ssDNA binding. {ECO:0000269|PubMed:20360609}.
-!- SUBUNIT: Homotetramer. Interacts, via its C-terminus, with several
proteins involved in DNA metabolism such as DnaG, HolC, PriA,
PriB, RecO, RecQ and SbcB. {ECO:0000255|HAMAP-Rule:MF_00984,
ECO:0000269|PubMed:10782989, ECO:0000269|PubMed:10932248,
ECO:0000269|PubMed:15576682, ECO:0000269|PubMed:17483090,
ECO:0000269|PubMed:18591666, ECO:0000269|PubMed:20018747,
ECO:0000269|PubMed:23430154, ECO:0000269|PubMed:23963891,
ECO:0000269|PubMed:7962001, ECO:0000269|PubMed:9192620,
ECO:0000269|PubMed:9545254}.
-!- INTERACTION:
P27296:dinG; NbExp=2; IntAct=EBI-1118620, EBI-1114590;
P0ABS5:dnaG; NbExp=2; IntAct=EBI-1118620, EBI-549259;
P06710:dnaX; NbExp=2; IntAct=EBI-1118620, EBI-549140;
P28905:holC; NbExp=10; IntAct=EBI-1118620, EBI-549169;
P17888:priA; NbExp=3; IntAct=EBI-1118620, EBI-552050;
-!- PTM: Phosphorylated on tyrosine residue(s).
{ECO:0000269|PubMed:16549871}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; J01704; AAA24649.1; -; Genomic_DNA.
EMBL; U00006; AAC43153.1; -; Genomic_DNA.
EMBL; U00096; AAC77029.1; -; Genomic_DNA.
EMBL; AP009048; BAE78061.1; -; Genomic_DNA.
PIR; B65214; DDEC.
RefSeq; NP_418483.1; NC_000913.3.
RefSeq; WP_000168305.1; NZ_LN832404.1.
PDB; 1EQQ; X-ray; 3.20 A; A/B/C/D=1-178.
PDB; 1EYG; X-ray; 2.80 A; A/B/C/D=1-116.
PDB; 1KAW; X-ray; 2.90 A; A/B/C/D=2-136.
PDB; 1QVC; X-ray; 2.20 A; A/B/C/D=2-146.
PDB; 1SRU; X-ray; 3.30 A; A/B/C/D=1-113.
PDB; 3C94; X-ray; 2.70 A; B/C=170-178.
PDB; 3SXU; X-ray; 1.85 A; C=175-178.
PDB; 3UF7; X-ray; 1.20 A; B/C=170-178.
PDB; 4MZ9; X-ray; 2.20 A; A/B/C/D=1-178.
PDB; 4Z0U; X-ray; 2.00 A; D/E=170-178.
PDBsum; 1EQQ; -.
PDBsum; 1EYG; -.
PDBsum; 1KAW; -.
PDBsum; 1QVC; -.
PDBsum; 1SRU; -.
PDBsum; 3C94; -.
PDBsum; 3SXU; -.
PDBsum; 3UF7; -.
PDBsum; 4MZ9; -.
PDBsum; 4Z0U; -.
ProteinModelPortal; P0AGE0; -.
SMR; P0AGE0; -.
BioGrid; 4262671; 106.
DIP; DIP-35980N; -.
IntAct; P0AGE0; 56.
MINT; P0AGE0; -.
STRING; 316385.ECDH10B_4248; -.
DrugBank; DB04243; 5-Methyluridine 5'-Monophosphate.
SWISS-2DPAGE; P0AGE0; -.
EPD; P0AGE0; -.
PaxDb; P0AGE0; -.
PRIDE; P0AGE0; -.
EnsemblBacteria; AAC77029; AAC77029; b4059.
EnsemblBacteria; BAE78061; BAE78061; BAE78061.
GeneID; 948570; -.
KEGG; ecj:JW4020; -.
KEGG; eco:b4059; -.
PATRIC; fig|511145.12.peg.4180; -.
EchoBASE; EB0969; -.
EcoGene; EG10976; ssb.
eggNOG; ENOG4108UUM; Bacteria.
eggNOG; COG0629; LUCA.
HOGENOM; HOG000106483; -.
InParanoid; P0AGE0; -.
KO; K03111; -.
OMA; ASGFDDM; -.
PhylomeDB; P0AGE0; -.
BioCyc; EcoCyc:EG10976-MONOMER; -.
EvolutionaryTrace; P0AGE0; -.
PRO; PR:P0AGE0; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0008047; F:enzyme activator activity; IMP:UniProtKB.
GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
GO; GO:0003697; F:single-stranded DNA binding; IDA:EcoCyc.
GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
GO; GO:0006298; P:mismatch repair; TAS:EcoCyc.
GO; GO:0043085; P:positive regulation of catalytic activity; IMP:UniProtKB.
GO; GO:0000725; P:recombinational repair; TAS:EcoCyc.
GO; GO:0009432; P:SOS response; TAS:EcoCyc.
CDD; cd04496; SSB_OBF; 1.
HAMAP; MF_00984; SSB; 1.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR000424; Primosome_PriB/ssb.
InterPro; IPR011344; ssDNA-bd.
PANTHER; PTHR10302; PTHR10302; 1.
PANTHER; PTHR10302:SF0; PTHR10302:SF0; 1.
Pfam; PF00436; SSB; 1.
SUPFAM; SSF50249; SSF50249; 1.
TIGRFAMs; TIGR00621; ssb; 1.
PROSITE; PS50935; SSB; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
DNA damage; DNA recombination; DNA repair; DNA replication;
DNA-binding; Phosphoprotein; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:6270666,
ECO:0000269|PubMed:7042342}.
CHAIN 2 178 Single-stranded DNA-binding protein.
/FTId=PRO_0000096036.
DOMAIN 6 111 SSB. {ECO:0000255|HAMAP-Rule:MF_00984}.
DNA_BIND 55 61 {ECO:0000255|HAMAP-Rule:MF_00984}.
MOTIF 173 178 Important for interaction with partner
proteins.
MUTAGEN 5 5 G->D: Increased frequency of precise
excision of transposon Tn10 derivatives
(mutant SSB-200).
{ECO:0000269|PubMed:3301414}.
MUTAGEN 11 11 L->F: Increased frequency of precise
excision of transposon Tn10 derivatives
(mutant SSB-202).
{ECO:0000269|PubMed:3301414}.
MUTAGEN 25 25 P->S: Increased frequency of precise
excision of transposon Tn10 derivatives
(mutant SSB-202).
{ECO:0000269|PubMed:3301414}.
MUTAGEN 56 56 H->L: Reduces DNA-binding affinity.
{ECO:0000269|PubMed:3301414}.
MUTAGEN 56 56 H->Y: Destabilizes the tetramer (mutant
SSB-1). {ECO:0000269|PubMed:3301414}.
MUTAGEN 61 61 F->A: Reduces DNA-binding affinity.
{ECO:0000269|PubMed:3301414}.
MUTAGEN 103 103 V->M: Increased frequency of precise
excision of transposon Tn10 derivatives
(mutant SSB-201).
{ECO:0000269|PubMed:3301414}.
MUTAGEN 177 177 P->S: Strongly reduced exonuclease I
(sbcB) stimulation.
{ECO:0000269|PubMed:18591666}.
CONFLICT 121 121 A -> AQ (in Ref. 2; no nucleotide entry).
{ECO:0000305}.
CONFLICT 134 134 G -> S (in Ref. 1; AAA24649).
{ECO:0000305}.
CONFLICT 171 171 D -> DG (in Ref. 2; no nucleotide entry).
{ECO:0000305}.
STRAND 6 17 {ECO:0000244|PDB:1QVC}.
STRAND 20 22 {ECO:0000244|PDB:1QVC}.
STRAND 25 27 {ECO:0000244|PDB:1QVC}.
STRAND 30 37 {ECO:0000244|PDB:1QVC}.
STRAND 45 48 {ECO:0000244|PDB:1QVC}.
STRAND 54 61 {ECO:0000244|PDB:1QVC}.
HELIX 63 71 {ECO:0000244|PDB:1QVC}.
STRAND 77 89 {ECO:0000244|PDB:1QVC}.
STRAND 91 94 {ECO:0000244|PDB:1QVC}.
STRAND 96 103 {ECO:0000244|PDB:1QVC}.
STRAND 105 107 {ECO:0000244|PDB:1EQQ}.
STRAND 108 111 {ECO:0000244|PDB:1QVC}.
STRAND 120 124 {ECO:0000244|PDB:1QVC}.
STRAND 136 139 {ECO:0000244|PDB:1QVC}.
SEQUENCE 178 AA; 18975 MW; F0AF43B6DC8D02FC CRC64;
MASRGVNKVI LVGNLGQDPE VRYMPNGGAV ANITLATSES WRDKATGEMK EQTEWHRVVL
FGKLAEVASE YLRKGSQVYI EGQLRTRKWT DQSGQDRYTT EVVVNVGGTM QMLGGRQGGG
APAGGNIGGG QPQGGWGQPQ QPQGGNQFSG GAQSRPQQSA PAAPSNEPPM DFDDDIPF


Related products :

Catalog number Product name Quantity
18-003-43578 Heterogeneous nuclear ribonucleoprotein A1 - Helix-destabilizing protein; Single-strand RNA-binding protein; hnRNP core protein A1 Polyclonal 0.1 mg Protein A
18-003-43577 Heterogeneous nuclear ribonucleoprotein A1 - Helix-destabilizing protein; Single-strand RNA-binding protein; hnRNP core protein A1 Polyclonal 0.1 mg Protein A
EIAAB35658 Bos taurus,Bovine,Helix-destabilizing protein,Heterogeneous nuclear ribonucleoprotein A1,hnRNP A1,hnRNP core protein A1,HNRNPA1,HNRPA1,Single-strand RNA-binding protein,Unwinding protein 1,UP1
EIAAB35657 HDP,Helix-destabilizing protein,Heterogeneous nuclear ribonucleoprotein A1,hnRNP A1,hnRNP core protein A1,Hnrnpa1,Hnrpa1,Rat,Rattus norvegicus,Single-strand RNA-binding protein
EIAAB35655 Helix-destabilizing protein,Heterogeneous nuclear ribonucleoprotein A1,hnRNP A1,hnRNP core protein A1,HNRNPA1,HNRPA1,Homo sapiens,Human,Single-strand RNA-binding protein
EIAAB35656 Fli-2,HDP-1,Helix-destabilizing protein,Heterogeneous nuclear ribonucleoprotein A1,hnRNP A1,hnRNP core protein A1,Hnrnpa1,Hnrpa1,Mouse,Mus musculus,Single-strand-binding protein,Tis,Topoisomerase-inhi
EIAAB40014 Homo sapiens,Human,Sequence-specific single-stranded-DNA-binding protein,Single-stranded DNA-binding protein 3,SSBP3,SSDP,SSDP1
EIAAB40017 Last,Lck-associated signal transducer,Mouse,Mus musculus,Sequence-specific single-stranded-DNA-binding protein,Single-stranded DNA-binding protein 3,Ssbp3,Ssdp1
EIAAB40016 Rat,Rattus norvegicus,Sequence-specific single-stranded-DNA-binding protein,Single-stranded DNA-binding protein 3,Ssbp3,Ssdp,Ssdp1,Ssdp3
EIAAB40012 Homo sapiens,Human,Sequence-specific single-stranded-DNA-binding protein 2,Single-stranded DNA-binding protein 2,SSBP2,SSDP2
EIAAB40013 Mouse,Mus musculus,Sequence-specific single-stranded-DNA-binding protein 2,Single-stranded DNA-binding protein 2,Ssbp2,Ssdp2
EIAAB34030 C2orf12,Homo sapiens,Human,MSSP,MSSP1,RBMS1,RNA-binding motif, single-stranded-interacting protein 1,SCR2,Single-stranded DNA-binding protein MSSP-1,Suppressor of CDC2 with RNA-binding motif 2
18-003-44184 RNA-binding motif. single-stranded-interacting protein 1 - Single-stranded DNA-binding protein MSSP-1; Suppressor of CDC2 with RNA-binding motif 2 Polyclonal 0.1 mg Protein A
18-003-43583 RNA-binding motif. single-stranded-interacting protein 1 - Single-stranded DNA-binding protein MSSP-1; Suppressor of CDC2 with RNA-binding motif 2 Polyclonal 0.1 mg Protein A
EIAAB34029 Mouse,Mssp,Mssp1,Mus musculus,Rbms1,RNA-binding motif, single-stranded-interacting protein 1,Single-stranded DNA-binding protein MSSP-1
18-003-42085 Single-stranded DNA-binding protein 2 - Sequence-specific single-stranded-DNA-binding protein 2 Polyclonal 0.05 mg Aff Pur
EIAAB40015 Chicken,Gallus gallus,Sequence-specific single-stranded-DNA-binding protein,Single-stranded DNA-binding protein 3,SSBP3,SSDP
EIAAB40007 MtSSB,Mt-SSB,Rat,Rattus norvegicus,Single strand DNA-binding protein P16,Single-stranded DNA-binding protein, mitochondrial,Ssbp,Ssbp1
25-230 CNBP is a nucleic-acid binding protein with seven zinc-finger domains. The protein has a preference for binding single stranded DNA and RNA. The protein functions in cap-independent translation of orn 0.05 mg
EIAAB34342 Homo sapiens,Human,REPA1,Replication factor A protein 1,Replication protein A 70 kDa DNA-binding subunit,RF-A protein 1,RP-A p70,RPA1,RPA70,Single-stranded DNA-binding protein
29-404 NONO is DNA- and RNA binding protein, involved in several nuclear processes. It binds the conventional octamer sequence in double stranded DNA. It also binds single-stranded DNA and RNA at a site inde 0.1 mg
29-403 NONO is DNA- and RNA binding protein, involved in several nuclear processes. It binds the conventional octamer sequence in double stranded DNA. It also binds single-stranded DNA and RNA at a site inde 0.1 mg
EIAAB33191 Mouse,Mus musculus,Purb,Purine-rich element-binding protein B,Transcriptional activator protein Pur-beta,Vascular actin single-stranded DNA-binding factor 2 p44 component
18-003-43089 Oligodendrocyte transcription factor 2 - Oligo2; Basic helix-loop-helix protein class B 1; Protein kinase C-binding protein RACK17; Protein kinase C-binding protein 2 Polyclonal 0.05 mg Aff Pur
02-044 Taq SSB (Single-Stranded DNA Binding) protein 100 ug


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur