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Histone H2A type 1-C

 H2A1C_MOUSE             Reviewed;         130 AA.
C0HKE2; P10812; P22752; Q149U0; Q5SZZ2;
10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
10-MAY-2017, sequence version 1.
23-MAY-2018, entry version 11.
RecName: Full=Histone H2A type 1-C {ECO:0000305};
Name=Hist1h2ac {ECO:0000312|MGI:MGI:2448287};
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 [GENOMIC DNA].
PubMed=12408966; DOI=10.1006/geno.2002.6850;
Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.;
"The human and mouse replication-dependent histone genes.";
Genomics 80:487-498(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC28337.1};
TISSUE=Colon {ECO:0000312|EMBL:BAC28337.1};
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
PHOSPHORYLATION AT SER-2, AND ACETYLATION AT SER-2 AND LYS-6.
PubMed=7217105;
Pantazis P., Bonner W.M.;
"Quantitative determination of histone modification. H2A acetylation
and phosphorylation.";
J. Biol. Chem. 256:4669-4675(1981).
[5]
UBIQUITINATION AT LYS-120.
PubMed=15525528; DOI=10.1016/j.devcel.2004.10.005;
de Napoles M., Mermoud J.E., Wakao R., Tang Y.A., Endoh M.,
Appanah R., Nesterova T.B., Silva J., Otte A.P., Vidal M., Koseki H.,
Brockdorff N.;
"Polycomb group proteins Ring1A/B link ubiquitylation of histone H2A
to heritable gene silencing and X inactivation.";
Dev. Cell 7:663-676(2004).
[6]
UBIQUITINATION AT LYS-120.
PubMed=15509584; DOI=10.1074/jbc.C400493200;
Fang J., Chen T., Chadwick B., Li E., Zhang Y.;
"Ring1b-mediated H2A ubiquitination associates with inactive X
chromosomes and is involved in initiation of X inactivation.";
J. Biol. Chem. 279:52812-52815(2004).
[7]
METHYLATION AT ARG-4.
PubMed=16699504; DOI=10.1038/ncb1413;
Ancelin K., Lange U.C., Hajkova P., Schneider R., Bannister A.J.,
Kouzarides T., Surani M.A.;
"Blimp1 associates with Prmt5 and directs histone arginine methylation
in mouse germ cells.";
Nat. Cell Biol. 8:623-630(2006).
[8]
CROTONYLATION AT LYS-37 AND LYS-119.
PubMed=21925322; DOI=10.1016/j.cell.2011.08.008;
Tan M., Luo H., Lee S., Jin F., Yang J.S., Montellier E., Buchou T.,
Cheng Z., Rousseaux S., Rajagopal N., Lu Z., Ye Z., Zhu Q.,
Wysocka J., Ye Y., Khochbin S., Ren B., Zhao Y.;
"Identification of 67 histone marks and histone lysine crotonylation
as a new type of histone modification.";
Cell 146:1016-1028(2011).
[9]
HYDROXYBUTYRYLATION AT LYS-6; LYS-10; LYS-37; LYS-75; LYS-76; LYS-96
AND LYS-119.
PubMed=24681537; DOI=10.1038/nchembio.1497;
Dai L., Peng C., Montellier E., Lu Z., Chen Y., Ishii H.,
Debernardi A., Buchou T., Rousseaux S., Jin F., Sabari B.R., Deng Z.,
Allis C.D., Ren B., Khochbin S., Zhao Y.;
"Lysine 2-hydroxyisobutyrylation is a widely distributed active
histone mark.";
Nat. Chem. Biol. 10:365-370(2014).
[10]
METHYLATION AT GLN-105.
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).
[11]
HYDROXYBUTYRYLATION AT LYS-6; LYS-37; LYS-120 AND LYS-126.
PubMed=27105115; DOI=10.1016/j.molcel.2016.03.036;
Xie Z., Zhang D., Chung D., Tang Z., Huang H., Dai L., Qi S., Li J.,
Colak G., Chen Y., Xia C., Peng C., Ruan H., Kirkey M., Wang D.,
Jensen L.M., Kwon O.K., Lee S., Pletcher S.D., Tan M., Lombard D.B.,
White K.P., Zhao H., Li J., Roeder R.G., Yang X., Zhao Y.;
"Metabolic regulation of gene expression by histone lysine beta-
hydroxybutyrylation.";
Mol. Cell 62:194-206(2016).
-!- FUNCTION: Core component of nucleosome. 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.
-!- 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.
-!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
-!- PTM: Deiminated on Arg-4 in granulocytes upon calcium entry.
{ECO:0000250|UniProtKB:P0C0S8}.
-!- PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM27
and RNF2/RING2 complex gives a specific tag for epigenetic
transcriptional repression and participates in X chromosome
inactivation of female mammals. It is involved in the initiation
of both imprinted and random X inactivation. Ubiquitinated H2A is
enriched in inactive X chromosome chromatin. Ubiquitination of H2A
functions downstream of methylation of 'Lys-27' of histone H3
(H3K27me). H2AK119Ub by RNF2/RING2 can also be induced by
ultraviolet and may be involved in DNA repair. Following DNA
double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63'
linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3
ligases RNF8 and RNF168, leading to the recruitment of repair
proteins to sites of DNA damage. Ubiquitination at Lys-14 and Lys-
16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage
is initiated by RNF168 that mediates monoubiquitination at these 2
sites, and 'Lys-63'-linked ubiquitin are then conjugated to
monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin
chains in vitro. Deubiquitinated by USP51 at Lys-14 and Lys-16
(H2AK13Ub and H2AK15Ub, respectively) after damaged DNA is
repaired (By similarity). H2AK119Ub and ionizing radiation-induced
'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are
distinct events. {ECO:0000250|UniProtKB:P0C0S8,
ECO:0000269|PubMed:15509584, ECO:0000269|PubMed:15525528,
ECO:0000269|PubMed:24352239}.
-!- PTM: Phosphorylation on Ser-2 (H2AS1ph) is enhanced during
mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly
represses transcription. Acetylation of H3 inhibits Ser-2
phosphorylation by RPS6KA5/MSK1. Phosphorylation at Thr-121
(H2AT120ph) by DCAF1 is present in the regulatory region of many
tumor suppresor genes and down-regulates their transcription.
{ECO:0000250|UniProtKB:P0C0S8, ECO:0000269|PubMed:7217105}.
-!- PTM: Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex
may play a crucial role in the germ-cell lineage.
{ECO:0000269|PubMed:16699504}.
-!- PTM: Glutamine methylation at Gln-105 (H2AQ104me) by FBL is
specifically dedicated to polymerase I. It is present at 35S
ribosomal DNA locus and impairs binding of the FACT complex.
{ECO:0000269|PubMed:24352239}.
-!- PTM: Crotonylation (Kcr) is specifically present in male germ
cells and marks testis-specific genes in post-meiotic cells,
including X-linked genes that escape sex chromosome inactivation
in haploid cells. Crotonylation marks active promoters and
enhancers and confers resistance to transcriptional repressors. It
is also associated with post-meiotically activated genes on
autosomes. {ECO:0000269|PubMed:21925322}.
-!- PTM: Hydroxybutyrylation of histones is induced by starvation.
{ECO:0000269|PubMed:27105115}.
-!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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EMBL; AY158919; AAO06229.1; -; Genomic_DNA.
EMBL; AK033518; BAC28337.1; -; mRNA.
EMBL; AL592149; CAI24893.1; -; Genomic_DNA.
CCDS; CCDS26356.1; -.
RefSeq; NP_001171015.1; NM_001177544.2.
RefSeq; NP_783591.2; NM_175660.3.
RefSeq; NP_835489.1; NM_178182.2.
RefSeq; NP_835491.1; NM_178184.2.
RefSeq; NP_835492.1; NM_178185.2.
RefSeq; NP_835493.1; NM_178186.3.
RefSeq; NP_835494.1; NM_178187.4.
RefSeq; NP_835495.1; NM_178188.4.
RefSeq; NP_835496.1; NM_178189.5.
UniGene; Mm.14767; -.
UniGene; Mm.250564; -.
UniGene; Mm.261665; -.
UniGene; Mm.261973; -.
UniGene; Mm.263165; -.
UniGene; Mm.390553; -.
UniGene; Mm.422826; -.
UniGene; Mm.423402; -.
SMR; C0HKE2; -.
iPTMnet; C0HKE2; -.
Ensembl; ENSMUST00000070124; ENSMUSP00000088285; ENSMUSG00000071516.
Ensembl; ENSMUST00000078369; ENSMUSP00000077477; ENSMUSG00000061615.
Ensembl; ENSMUST00000081342; ENSMUSP00000080088; ENSMUSG00000094777.
Ensembl; ENSMUST00000090776; ENSMUSP00000088281; ENSMUSG00000071478.
Ensembl; ENSMUST00000091741; ENSMUSP00000089335; ENSMUSG00000069301.
Ensembl; ENSMUST00000091745; ENSMUSP00000089339; ENSMUSG00000094248.
Ensembl; ENSMUST00000091751; ENSMUSP00000089345; ENSMUSG00000069309.
Ensembl; ENSMUST00000102969; ENSMUSP00000100034; ENSMUSG00000069272.
Ensembl; ENSMUST00000171127; ENSMUSP00000127684; ENSMUSG00000069270.
GeneID; 319164; -.
GeneID; 319165; -.
GeneID; 319166; -.
GeneID; 319167; -.
GeneID; 319170; -.
GeneID; 319171; -.
GeneID; 319172; -.
GeneID; 319191; -.
GeneID; 665433; -.
KEGG; mmu:319164; -.
KEGG; mmu:319165; -.
KEGG; mmu:319166; -.
KEGG; mmu:319167; -.
KEGG; mmu:319170; -.
KEGG; mmu:319171; -.
KEGG; mmu:319172; -.
KEGG; mmu:319191; -.
KEGG; mmu:665433; -.
CTD; 3012; -.
CTD; 3013; -.
CTD; 319170; -.
CTD; 319171; -.
CTD; 665433; -.
CTD; 8329; -.
CTD; 8334; -.
CTD; 8335; -.
CTD; 8969; -.
MGI; MGI:2448287; Hist1h2ac.
KO; K11251; -.
Reactome; R-MMU-201722; Formation of the beta-catenin:TCF transactivating complex.
Reactome; R-MMU-212300; PRC2 methylates histones and DNA.
Reactome; R-MMU-2299718; Condensation of Prophase Chromosomes.
Reactome; R-MMU-2559580; Oxidative Stress Induced Senescence.
Reactome; R-MMU-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-MMU-2559586; DNA Damage/Telomere Stress Induced Senescence.
Reactome; R-MMU-3214847; HATs acetylate histones.
Reactome; R-MMU-3214858; RMTs methylate histone arginines.
Reactome; R-MMU-427359; SIRT1 negatively regulates rRNA expression.
Reactome; R-MMU-427413; NoRC negatively regulates rRNA expression.
Reactome; R-MMU-5250924; B-WICH complex positively regulates rRNA expression.
Reactome; R-MMU-5578749; Transcriptional regulation by small RNAs.
Reactome; R-MMU-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
Reactome; R-MMU-5689603; UCH proteinases.
Reactome; R-MMU-5689880; Ub-specific processing proteases.
Reactome; R-MMU-5689901; Metalloprotease DUBs.
Reactome; R-MMU-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
Reactome; R-MMU-73728; RNA Polymerase I Promoter Opening.
Reactome; R-MMU-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
Reactome; R-MMU-9018519; Estrogen-dependent gene expression.
PRO; PR:C0HKE2; -.
Proteomes; UP000000589; Chromosome 13.
ExpressionAtlas; C0HKE2; baseline and differential.
GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
CDD; cd00074; H2A; 1.
Gene3D; 1.10.20.10; -; 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;
Acetylation; Chromosome; Citrullination; Complete proteome;
DNA-binding; Hydroxylation; Isopeptide bond; Methylation;
Nucleosome core; Nucleus; Phosphoprotein; Reference proteome;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P0C169}.
CHAIN 2 130 Histone H2A type 1-C.
/FTId=PRO_0000439716.
MOD_RES 2 2 N-acetylserine.
{ECO:0000269|PubMed:7217105}.
MOD_RES 2 2 Phosphoserine; by RPS6KA5.
{ECO:0000269|PubMed:7217105}.
MOD_RES 4 4 Citrulline; alternate.
{ECO:0000250|UniProtKB:P0C0S8}.
MOD_RES 4 4 Symmetric dimethylarginine; by PRMT5;
alternate. {ECO:0000269|PubMed:16699504}.
MOD_RES 6 6 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 6 6 N6-(beta-hydroxybutyryl)lysine;
alternate. {ECO:0000269|PubMed:27105115}.
MOD_RES 6 6 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:7217105}.
MOD_RES 10 10 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 10 10 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q93077}.
MOD_RES 37 37 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 37 37 N6-(beta-hydroxybutyryl)lysine;
alternate. {ECO:0000269|PubMed:27105115}.
MOD_RES 37 37 N6-crotonyllysine; alternate.
{ECO:0000269|PubMed:21925322}.
MOD_RES 75 75 N6-(2-hydroxyisobutyryl)lysine.
{ECO:0000269|PubMed:24681537}.
MOD_RES 76 76 N6-(2-hydroxyisobutyryl)lysine.
{ECO:0000269|PubMed:24681537}.
MOD_RES 96 96 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 96 96 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q93077}.
MOD_RES 105 105 N5-methylglutamine.
{ECO:0000269|PubMed:24352239}.
MOD_RES 119 119 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 119 119 N6-crotonyllysine; alternate.
{ECO:0000269|PubMed:21925322}.
MOD_RES 120 120 N6-(beta-hydroxybutyryl)lysine;
alternate. {ECO:0000269|PubMed:27105115}.
MOD_RES 120 120 N6-crotonyllysine; alternate.
{ECO:0000250|UniProtKB:P0C0S8}.
MOD_RES 121 121 Phosphothreonine; by DCAF1.
{ECO:0000250|UniProtKB:Q93077}.
MOD_RES 126 126 N6-(beta-hydroxybutyryl)lysine;
alternate. {ECO:0000269|PubMed:27105115}.
MOD_RES 126 126 N6-crotonyllysine; alternate.
{ECO:0000250|UniProtKB:P0C0S8}.
CROSSLNK 14 14 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q93077}.
CROSSLNK 16 16 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q93077}.
CROSSLNK 120 120 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate. {ECO:0000269|PubMed:15509584,
ECO:0000269|PubMed:15525528}.
SEQUENCE 130 AA; 14135 MW; 9CFE6184B2CC89F5 CRC64;
MSGRGKQGGK ARAKAKTRSS RAGLQFPVGR VHRLLRKGNY SERVGAGAPV YLAAVLEYLT
AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGR VTIAQGGVLP NIQAVLLPKK
TESHHKAKGK


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SCH-AHP419 RABBIT ANTI HISTONE H2A (Ac5), Product Type Polyclonal Antibody, Specificity HISTONE H2A , Target Species Synthetic Peptide, Host Rabbit, Format Serum, Isotypes Polyclonal IgG, Applications E, 0.1 ml
AHP415 RABBIT ANTI HISTONE H4 (Ac8), Product Type Polyclonal Antibody, Specificity HISTONE H4 , Target Species Synthetic Peptide, Host Rabbit, Format Serum, Isotypes Polyclonal IgG, Applications E, IF 0.1 ml
SCH-AHP421 RABBIT ANTI HISTONE H2B (ACETYLATED), Product Type Polyclonal Antibody, Specificity HISTONE H2B , Target Species Mammals, Host Rabbit, Format Serum, Isotypes Polyclonal IgG, Applications E, IF, 0.1 ml
SCH-AHP1027 RABBIT ANTI HISTONE H3 (ACETYLATED), Product Type Polyclonal Antibody, Specificity HISTONE H3 , Target Species , Host Rabbit, Format Serum, Isotypes Polyclonal IgG, Applications E, IF, WB, Clon 0.1 ml
AHP418 RABBIT ANTI HISTONE H4 (ACETYLATED), Product Type Polyclonal Antibody, Specificity HISTONE H4 , Target Species Synthetic Peptide, Host Rabbit, Format Serum, Isotypes Polyclonal IgG, Applications 0.1 ml
SCH-AHP416 RABBIT ANTI HISTONE H4 (Ac12), Product Type Polyclonal Antibody, Specificity HISTONE H4 , Target Species Synthetic Peptide, Host Rabbit, Format Serum, Isotypes Polyclonal IgG, Applications E, I 0.1 ml
SCH-AHP418 RABBIT ANTI HISTONE H4 (ACETYLATED), Product Type Polyclonal Antibody, Specificity HISTONE H4 , Target Species Synthetic Peptide, Host Rabbit, Format Serum, Isotypes Polyclonal IgG, Applications 0.1 ml
AHP416 RABBIT ANTI HISTONE H4 (Ac12), Product Type Polyclonal Antibody, Specificity HISTONE H4 , Target Species Synthetic Peptide, Host Rabbit, Format Serum, Isotypes Polyclonal IgG, Applications E, I 0.1 ml
4974-7808 MOUSE ANTI HUMAN HISTONE H1, Product Type Monoclonal Antibody, Specificity HISTONE H1, Target Species Human, Host Mouse, Format Purified, Isotypes IgG2a, Applications C*, E, IF, P, WB, Clone A 0.2 mg
SCH-4974-7808 MOUSE ANTI HUMAN HISTONE H1, Product Type Monoclonal Antibody, Specificity HISTONE H1, Target Species Human, Host Mouse, Format Purified, Isotypes IgG2a, Applications C*, E, IF, P, WB, Clone A 0.2 mg
BLP028 HISTONE H2AX BLOCKING PEPTIDE, Product Type Blocking Peptide, Specificity HISTONE H2AX , Target Species Human, Host N_A, Format Purified, Isotypes , Applications IP, WB, Clone 50 µg
SCH-BLP027 HISTONE H2AX BLOCKING PEPTIDE, Product Type Blocking Peptide, Specificity HISTONE H2AX , Target Species Human, Host N_A, Format Purified, Isotypes , Applications IP, WB, Clone 50 µg
SCH-BLP028 HISTONE H2AX BLOCKING PEPTIDE, Product Type Blocking Peptide, Specificity HISTONE H2AX , Target Species Human, Host N_A, Format Purified, Isotypes , Applications IP, WB, Clone 50 µg
BLP027 HISTONE H2AX BLOCKING PEPTIDE, Product Type Blocking Peptide, Specificity HISTONE H2AX , Target Species Human, Host N_A, Format Purified, Isotypes , Applications IP, WB, Clone 50 µg


 

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