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

Histone H2A.2

 H2A2_YEAST              Reviewed;         132 AA.
P04912; D6VPZ9;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
22-NOV-2017, entry version 169.
RecName: Full=Histone H2A.2;
Name=HTA2; Synonyms=H2A2; OrderedLocusNames=YBL003C; ORFNames=YBL0103;
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].
PubMed=7041122; DOI=10.1073/pnas.79.5.1484;
Choe J., Kolodrubetz D., Grunstein M.;
"The two yeast histone H2A genes encode similar protein subtypes.";
Proc. Natl. Acad. Sci. U.S.A. 79:1484-1487(1982).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8091860; DOI=10.1002/yea.320100006;
Wolfe K.H., Lohan A.J.E.;
"Sequence around the centromere of Saccharomyces cerevisiae chromosome
II: similarity of CEN2 to CEN4.";
Yeast 10:S41-S46(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7813418;
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J.,
Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C.,
Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M.,
Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L.,
Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J.,
Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T.,
Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A.,
Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B.,
Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I.,
Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M.,
Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A.,
van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I.,
Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H.,
Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.;
"Complete DNA sequence of yeast chromosome II.";
EMBO J. 13:5795-5809(1994).
[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]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[6]
ACETYLATION AT LYS-5 AND LYS-8.
PubMed=10082517; DOI=10.1128/MCB.19.4.2515;
Clarke A.S., Lowell J.E., Jacobson S.J., Pillus L.;
"Esa1p is an essential histone acetyltransferase required for cell
cycle progression.";
Mol. Cell. Biol. 19:2515-2526(1999).
[7]
FUNCTION, MUTAGENESIS OF SER-129, AND PHOSPHORYLATION AT SER-129.
PubMed=11140636; DOI=10.1038/35050000;
Downs J.A., Lowndes N.F., Jackson S.P.;
"A role for Saccharomyces cerevisiae histone H2A in DNA repair.";
Nature 408:1001-1004(2000).
[8]
ACETYLATION AT LYS-8.
PubMed=11545749; DOI=10.1016/S1097-2765(01)00301-X;
Suka N., Suka Y., Carmen A.A., Wu J., Grunstein M.;
"Highly specific antibodies determine histone acetylation site usage
in yeast heterochromatin and euchromatin.";
Mol. Cell 8:473-479(2001).
[9]
ACETYLATION AT SER-2.
PubMed=12915400; DOI=10.1074/jbc.C300355200;
Song O.-K., Wang X., Waterborg J.H., Sternglanz R.;
"An Nalpha-acetyltransferase responsible for acetylation of the N-
terminal residues of histones H4 and H2A.";
J. Biol. Chem. 278:38109-38112(2003).
[10]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[11]
FUNCTION, AND PHOSPHORYLATION.
PubMed=15458641; DOI=10.1016/j.cub.2004.09.047;
Shroff R., Arbel-Eden A., Pilch D.R., Ira G., Bonner W.M.,
Petrini J.H.J., Haber J.E., Lichten M.;
"Distribution and dynamics of chromatin modification induced by a
defined DNA double-strand break.";
Curr. Biol. 14:1703-1711(2004).
[12]
FUNCTION, AND PHOSPHORYLATION.
PubMed=15610741; DOI=10.1016/j.molcel.2004.11.027;
Uenal E., Arbel-Eden A., Sattler U., Shroff R., Lichten M.,
Haber J.E., Koshland D.;
"DNA damage response pathway uses histone modification to assemble a
double-strand break-specific cohesin domain.";
Mol. Cell 16:991-1002(2004).
[13]
INTERACTION WITH ARP4.
PubMed=15610740; DOI=10.1016/j.molcel.2004.12.003;
Downs J.A., Allard S., Jobin-Robitaille O., Javaheri A., Auger A.,
Bouchard N., Kron S.J., Jackson S.P., Cote J.;
"Binding of chromatin-modifying activities to phosphorylated histone
H2A at DNA damage sites.";
Mol. Cell 16:979-990(2004).
[14]
SUMOYLATION AT LYS-127.
PubMed=16598039; DOI=10.1101/gad.1404206;
Nathan D., Ingvarsdottir K., Sterner D.E., Bylebyl G.R.,
Dokmanovic M., Dorsey J.A., Whelan K.A., Krsmanovic M., Lane W.S.,
Meluh P.B., Johnson E.S., Berger S.L.;
"Histone sumoylation is a negative regulator in Saccharomyces
cerevisiae and shows dynamic interplay with positive-acting histone
modifications.";
Genes Dev. 20:966-976(2006).
[15]
FUNCTION, AND DEPHOSPHORYLATION.
PubMed=16299494; DOI=10.1038/nature04384;
Keogh M.-C., Kim J.-A., Downey M., Fillingham J., Chowdhury D.,
Harrison J.C., Onishi M., Datta N., Galicia S., Emili A.,
Lieberman J., Shen X., Buratowski S., Haber J.E., Durocher D.,
Greenblatt J.F., Krogan N.J.;
"A phosphatase complex that dephosphorylates gamma-H2AX regulates DNA
damage checkpoint recovery.";
Nature 439:497-501(2006).
[16]
INTERACTION WITH NAP1, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=18086883; DOI=10.1128/MCB.01035-07;
Calvert M.E.K., Keck K.M., Ptak C., Shabanowitz J., Hunt D.F.,
Pemberton L.F.;
"Phosphorylation by casein kinase 2 regulates Nap1 localization and
function.";
Mol. Cell. Biol. 28:1313-1325(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[18]
SUCCINYLATION AT LYS-14 AND LYS-22, AND MALONYLATION AT LYS-120.
PubMed=22389435; DOI=10.1074/mcp.M111.015875;
Xie Z., Dai J., Dai L., Tan M., Cheng Z., Wu Y., Boeke J.D., Zhao Y.;
"Lysine succinylation and lysine malonylation in histones.";
Mol. Cell. Proteomics 11:100-107(2012).
[19]
METHYLATION AT GLN-106.
PubMed=24352239; DOI=10.1038/nature12819;
Tessarz P., Santos-Rosa H., Robson S.C., Sylvestersen K.B.,
Nelson C.J., Nielsen M.L., Kouzarides T.;
"Glutamine methylation in histone H2A is an RNA-polymerase-I-dedicated
modification.";
Nature 505:564-568(2014).
-!- FUNCTION: Core component of nucleosome which plays a central role
in DNA double strand break (DSB) repair. Nucleosomes wrap and
compact DNA into chromatin, limiting DNA accessibility to the
cellular machineries which require DNA as a template. Histones
thereby play a central role in transcription regulation, DNA
repair, DNA replication and chromosomal stability. DNA
accessibility is regulated via a complex set of post-translational
modifications of histones, also called histone code, and
nucleosome remodeling. {ECO:0000269|PubMed:11140636,
ECO:0000269|PubMed:15458641, ECO:0000269|PubMed:15610741,
ECO:0000269|PubMed:16299494}.
-!- SUBUNIT: The nucleosome is a histone octamer containing two
molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4
heterotetramer and two H2A-H2B heterodimers. The octamer wraps
approximately 147 bp of DNA. Interacts with NAP1.
{ECO:0000269|PubMed:15610740, ECO:0000269|PubMed:18086883}.
-!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
-!- DOMAIN: The [ST]-Q motif constitutes a recognition sequence for
kinases from the PI3/PI4-kinase family.
-!- PTM: Phosphorylated to form H2AS128ph (gamma-H2A) in response to
DNA double-strand breaks (DSBs) generated by exogenous genotoxic
agents and by stalled replication forks. Phosphorylation is
dependent on the DNA damage checkpoint kinases MEC1/ATR and
TEL1/ATM, spreads on either side of a detected DSB site and may
mark the surrounding chromatin for recruitment of proteins
required for DNA damage signaling and repair. Gamma-H2A interacts
with ARP4, a shared component of the NuA4 histone
acetyltransferase complex and the INO80 and SWR1 chromatin
remodeling complexes, and serves to recruit first NuA4, mediating
histone H4 acetylation, and subsequently the INO80/SWR1 complexes,
facilitating DNA resection, to DSB sites. Gamma-H2A is required
for sequestering cohesin around the break site, which is important
for efficient post-replicative double-strand break repair by
homologous recombination, holding the damaged chromatid close to
its undamaged sister template. Gamma-H2A is removed from the DNA
prior to the strand invasion-primer extension step of the repair
process and subsequently dephosphorylated by PPH3, a component of
the histone H2A phosphatase complex (HTP-C). Dephosphorylation is
necessary for efficient recovery from the DNA damage checkpoint.
{ECO:0000269|PubMed:11140636, ECO:0000269|PubMed:15458641,
ECO:0000269|PubMed:15610741}.
-!- PTM: N-acetylated by NAT4.
-!- PTM: Acetylated by ESA1, a component of the NuA4 histone
acetyltransferase (HAT) complex, to form H2AK4ac and H2AK7ac.
-!- PTM: Glutamine methylation at Gln-106 (H2AQ105me) by NOP1 is
specifically dedicated to polymerase I. It is present at 35S
ribosomal DNA locus and impairs binding of the FACT complex
(PubMed:24352239). {ECO:0000269|PubMed:24352239}.
-!- PTM: Sumoylated to from H2AK126su. May lead to transcriptional
repression. {ECO:0000269|PubMed:16598039}.
-!- MISCELLANEOUS: In contrast to vertebrates and insects, its C-
terminus is not monoubiquitinated. {ECO:0000305}.
-!- MISCELLANEOUS: Present with 32100 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
-!- CAUTION: To ensure consistency between histone entries, we follow
the 'Brno' nomenclature for histone modifications, with positions
referring to those used in the literature for the 'closest' model
organism. Due to slight variations in histone sequences between
organisms and to the presence of initiator methionine in
UniProtKB/Swiss-Prot sequences, the actual positions of modified
amino acids in the sequence generally differ. In this entry the
following conventions are used: H2AK4ac = acetylated Lys-5;
H2AK7ac = acetylated Lys-8; H2AK126su = sumoylated Lys-127;
H2AS128ph = phosphorylated Ser-129. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; V01305; CAA24612.1; -; Genomic_DNA.
EMBL; Z26494; CAA81267.1; -; Genomic_DNA.
EMBL; Z35764; CAA84818.1; -; Genomic_DNA.
EMBL; AY693115; AAT93134.1; -; Genomic_DNA.
EMBL; BK006936; DAA07119.1; -; Genomic_DNA.
PIR; S05814; HSBYA2.
RefSeq; NP_009552.1; NM_001178243.1.
PDB; 4JJN; X-ray; 3.09 A; C/G=2-132.
PDB; 4KUD; X-ray; 3.20 A; C/G=1-132.
PDBsum; 4JJN; -.
PDBsum; 4KUD; -.
ProteinModelPortal; P04912; -.
SMR; P04912; -.
BioGrid; 32699; 307.
DIP; DIP-6377N; -.
IntAct; P04912; 161.
MINT; MINT-637879; -.
STRING; 4932.YBL003C; -.
iPTMnet; P04912; -.
MaxQB; P04912; -.
PRIDE; P04912; -.
TopDownProteomics; P04912; -.
EnsemblFungi; YBL003C; YBL003C; YBL003C.
GeneID; 852283; -.
KEGG; sce:YBL003C; -.
EuPathDB; FungiDB:YBL003C; -.
SGD; S000000099; HTA2.
GeneTree; ENSGT00900000140854; -.
HOGENOM; HOG000234652; -.
InParanoid; P04912; -.
KO; K11251; -.
OMA; FANVTIR; -.
OrthoDB; EOG092C5QJX; -.
BioCyc; YEAST:G3O-28909-MONOMER; -.
Reactome; R-SCE-2299718; Condensation of Prophase Chromosomes.
Reactome; R-SCE-2559580; Oxidative Stress Induced Senescence.
Reactome; R-SCE-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-SCE-3214815; HDACs deacetylate histones.
Reactome; R-SCE-3214858; RMTs methylate histone arginines.
Reactome; R-SCE-427359; SIRT1 negatively regulates rRNA expression.
Reactome; R-SCE-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
Reactome; R-SCE-5689880; Ub-specific processing proteases.
Reactome; R-SCE-5689901; Metalloprotease DUBs.
Reactome; R-SCE-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
PRO; PR:P04912; -.
Proteomes; UP000002311; Chromosome II.
GO; GO:0000788; C:nuclear nucleosome; TAS:SGD.
GO; GO:0031298; C:replication fork protection complex; IDA:SGD.
GO; GO:0003677; F:DNA binding; TAS:SGD.
GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
GO; GO:0006333; P:chromatin assembly or disassembly; TAS:SGD.
GO; GO:0006342; P:chromatin silencing; IBA:GO_Central.
GO; GO:0006281; P:DNA repair; IMP:SGD.
CDD; cd00074; H2A; 1.
InterPro; IPR009072; Histone-fold.
InterPro; IPR002119; Histone_H2A.
InterPro; IPR007125; Histone_H2A/H2B/H3.
InterPro; IPR032454; Histone_H2A_C.
InterPro; IPR032458; Histone_H2A_CS.
Pfam; PF00125; Histone; 1.
Pfam; PF16211; Histone_H2A_C; 1.
PRINTS; PR00620; HISTONEH2A.
SMART; SM00414; H2A; 1.
SUPFAM; SSF47113; SSF47113; 1.
PROSITE; PS00046; HISTONE_H2A; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Chromosome; Complete proteome; DNA damage;
DNA repair; DNA-binding; Isopeptide bond; Methylation;
Nucleosome core; Nucleus; Phosphoprotein; Reference proteome;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:12915400}.
CHAIN 2 132 Histone H2A.2.
/FTId=PRO_0000055327.
MOTIF 129 130 [ST]-Q motif.
SITE 120 120 Not ubiquitinated. {ECO:0000305}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000269|PubMed:12915400}.
MOD_RES 5 5 N6-acetyllysine.
{ECO:0000269|PubMed:10082517}.
MOD_RES 8 8 N6-acetyllysine.
{ECO:0000269|PubMed:10082517,
ECO:0000269|PubMed:11545749}.
MOD_RES 14 14 N6-succinyllysine.
{ECO:0000269|PubMed:22389435}.
MOD_RES 22 22 N6-succinyllysine.
{ECO:0000269|PubMed:22389435}.
MOD_RES 106 106 N5-methylglutamine.
{ECO:0000269|PubMed:24352239}.
MOD_RES 120 120 N6-malonyllysine; alternate.
{ECO:0000269|PubMed:22389435}.
MOD_RES 129 129 Phosphoserine.
{ECO:0000244|PubMed:18407956,
ECO:0000269|PubMed:11140636}.
CROSSLNK 127 127 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
MUTAGEN 129 129 S->A: Causes hypersensitivity to DNA-
damage-inducing agents.
{ECO:0000269|PubMed:11140636}.
MUTAGEN 129 129 S->E,T: No effect.
{ECO:0000269|PubMed:11140636}.
HELIX 19 22 {ECO:0000244|PDB:4JJN}.
HELIX 29 37 {ECO:0000244|PDB:4JJN}.
TURN 38 40 {ECO:0000244|PDB:4JJN}.
STRAND 43 45 {ECO:0000244|PDB:4JJN}.
HELIX 49 74 {ECO:0000244|PDB:4JJN}.
STRAND 78 80 {ECO:0000244|PDB:4JJN}.
HELIX 82 89 {ECO:0000244|PDB:4JJN}.
HELIX 93 98 {ECO:0000244|PDB:4JJN}.
TURN 99 101 {ECO:0000244|PDB:4JJN}.
STRAND 102 104 {ECO:0000244|PDB:4JJN}.
HELIX 115 117 {ECO:0000244|PDB:4JJN}.
SEQUENCE 132 AA; 13989 MW; E808C94A0363CD53 CRC64;
MSGGKGGKAG SAAKASQSRS AKAGLTFPVG RVHRLLRRGN YAQRIGSGAP VYLTAVLEYL
AAEILELAGN AARDNKKTRI IPRHLQLAIR NDDELNKLLG NVTIAQGGVL PNIHQNLLPK
KSAKTAKASQ EL


Related products :

Catalog number Product name Quantity
28-858 Histone acetylation plays a key role in the regulation of eukaryotic gene expression. Histone acetylation and deacetylation are catalyzed by multisubunit complexes. SAP30 is a component of the histone 0.1 mg
28-920 Histone acetylation plays a key role in the regulation of eukaryotic gene expression. Histone acetylation and deacetylation are catalyzed by multisubunit complexes. SAP18 is a component of the histone 0.05 mg
28-857 Histone acetylation plays a key role in the regulation of eukaryotic gene expression. Histone acetylation and deacetylation are catalyzed by multisubunit complexes. SAP30 is a component of the histone 0.1 mg
25-522 UTX is a histone demethylase that specifically demethylates 'Lys-27' of histone H3, thereby playing a central role in histone code. It demethylates trimethylated and dimethylated but not monomethylate 0.05 mg
orb61320 CI-994 CI-994 is a histone deacetylase (HDAC) inhibitor and induces histone hyperacetylation in living cells. CI-994 inhibited HDAC-1 and HDAC-2 but not the prototypical histone acetyltransferase GCN5 500 mg
29-186 JMJD3 is a histone demethylase that specifically demethylates 'Lys-27' of histone H3, thereby playing a central role in histone code. It plays a central role in regulation of posterior development, by 0.1 mg
25-583 JMJD3 is a histone demethylase that specifically demethylates 'Lys-27' of histone H3, thereby playing a central role in histone code. It plays a central role in regulation of posterior development, by 0.05 mg
27-131 POLE3 is a histone-fold protein that interacts with other histone-fold proteins to bind DNA in a sequence-independent manner. These histone-fold protein dimers combine within larger enzymatic complexe 0.05 mg
27-775 POLE3 is a histone-fold protein that interacts with other histone-fold proteins to bind DNA in a sequence-independent manner. These histone-fold protein dimers combine within larger enzymatic complexe 0.1 mg
25-113 CHRAC1 is a histone-fold protein that interacts with other histone-fold proteins to bind DNA in a sequence-independent manner. These histone-fold protein dimers combine within larger enzymatic complex 0.05 mg
bs-0931P Peptides: Histone H1b(Histone H1.4) Protein Length:12-25 amino acids. 200ug lyophilized
SET3001 Histone-related : SET7_9 Histone methyltransferase Human, E.coli 0.5mg
SET3001 Histone-related : SET7_9 Histone methyltransferase Human, E.coli 100ug
E0356h ELISA H2B_s,H2BFS,Histone H2B type F-S,Histone H2B.s,Homo sapiens,Human 96T
E0356h ELISA kit H2B_s,H2BFS,Histone H2B type F-S,Histone H2B.s,Homo sapiens,Human 96T
U0356h CLIA H2B_s,H2BFS,Histone H2B type F-S,Histone H2B.s,Homo sapiens,Human 96T
303-35199 Anti_phospho Histone H3 (P_Ser10), monoclonal antibody Binds to Histone H3 phosphorylated at serine 10. 100 ul
30-333 DOT1L is a histone methyltransferase. It methylates 'Lys-79' of histone H3. Nucleosomes are preferred as substrate compared to free histones. 0.05 mg
ANTY021260 Polyclonal Antibodies: Histone H2A.X (Ab-139) ; Specificity: Histone H2A.X (Ab-139) ; Application: IHC 100ug
31-007 Histone H3, along with histone H4, plays a central role in nucleosome formation. 0.1 mg
ANTY021137 Polyclonal Antibodies: Histone H3.1 (Ab-10) ; Specificity: Histone H3.1 (Ab-10) ; Application: IHC 100ug
3623BP-50 Histone H3 Blocking Peptide target: Histone H3 50 μg
3624BP-50 Histone H4 Blocking Peptide target: Histone H4 50 μg
3621BP-50 Histone H2A Blocking Peptide target: Histone H2A 50 μg
3622BP-50 Histone H2B Blocking Peptide target: Histone H2B 50 μg


 

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