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

Histone H3.3

 H33_BOVIN               Reviewed;         136 AA.
Q5E9F8; A4IFS1; Q862G6; Q862V0; Q862W6;
17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
23-MAY-2018, entry version 121.
RecName: Full=Histone H3.3;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
PubMed=12658628; DOI=10.1002/mrd.10292;
Ishiwata H., Katsuma S., Kizaki K., Patel O.V., Nakano H.,
Takahashi T., Imai K., Hirasawa A., Shiojima S., Ikawa H., Suzuki Y.,
Tsujimoto G., Izaike Y., Todoroki J., Hashizume K.;
"Characterization of gene expression profiles in early bovine
pregnancy using a custom cDNA microarray.";
Mol. Reprod. Dev. 65:9-18(2003).
PubMed=16305752; DOI=10.1186/1471-2164-6-166;
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
"Characterization of 954 bovine full-CDS cDNA sequences.";
BMC Genomics 6:166-166(2005).
STRAIN=Hereford; TISSUE=Fetal cerebellum, and Fetal liver;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
PubMed=10464286; DOI=10.1074/jbc.274.36.25543;
Goto H., Tomono Y., Ajiro K., Kosako H., Fujita M., Sakurai M.,
Okawa K., Iwamatsu A., Okigaki T., Takahashi T., Inagaki M.;
"Identification of a novel phosphorylation site on histone H3 coupled
with mitotic chromosome condensation.";
J. Biol. Chem. 274:25543-25549(1999).
-!- FUNCTION: Variant histone H3 which replaces conventional H3 in a
wide range of nucleosomes in active genes. Constitutes the
predominant form of histone H3 in non-dividing cells and is
incorporated into chromatin independently of DNA synthesis.
Deposited at sites of nucleosomal displacement throughout
transcribed genes, suggesting that it represents an epigenetic
imprint of transcriptionally active chromatin. 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:0000250|UniProtKB:P84243}.
-!- 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 HIRA, a chaperone
required for its incorporation into nucleosomes. Interacts with
ZMYND11; when trimethylated at 'Lys-36' (H3.3K36me3).
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome
-!- DEVELOPMENTAL STAGE: Expressed throughout the cell cycle
independently of DNA synthesis.
-!- DOMAIN: Specific interaction of trimethylated form at 'Lys-36'
(H3.3K36me3) with ZMYND11 is mediated by the encapsulation of Ser-
32 residue with a composite pocket formed by the tandem bromo-PWWP
domains. {ECO:0000250|UniProtKB:P84243}.
-!- PTM: Acetylation is generally linked to gene activation.
Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9
(H3R8me2s). Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac)
favors methylation at Arg-18 (H3R17me). Acetylation at Lys-123
(H3K122ac) by EP300/p300 plays a central role in chromatin
structure: localizes at the surface of the histone octamer and
stimulates transcription, possibly by promoting nucleosome
instability. {ECO:0000250|UniProtKB:P84243}.
-!- PTM: Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by
PADI4 impairs methylation and represses transcription.
-!- PTM: Asymmetric dimethylation at Arg-18 (H3R17me2a) by CARM1 is
linked to gene activation. Symmetric dimethylation at Arg-9
(H3R8me2s) by PRMT5 is linked to gene repression. Asymmetric
dimethylation at Arg-3 (H3R2me2a) by PRMT6 is linked to gene
repression and is mutually exclusive with H3 Lys-5 methylation
(H3K4me2 and H3K4me3). H3R2me2a is present at the 3' of genes
regardless of their transcription state and is enriched on
inactive promoters, while it is absent on active promoters.
-!- PTM: Specifically enriched in modifications associated with active
chromatin such as methylation at Lys-5 (H3K4me), Lys-37 and Lys-
80. Methylation at Lys-5 (H3K4me) facilitates subsequent
acetylation of H3 and H4. Methylation at Lys-80 (H3K79me) is
associated with DNA double-strand break (DSB) responses and is a
specific target for TP53BP1. Methylation at Lys-10 (H3K9me) and
Lys-28 (H3K27me), which are linked to gene repression, are
underrepresented. Methylation at Lys-10 (H3K9me) is a specific
target for HP1 proteins (CBX1, CBX3 and CBX5) and prevents
subsequent phosphorylation at Ser-11 (H3S10ph) and acetylation of
H3 and H4. Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me)
require preliminary monoubiquitination of H2B at 'Lys-120'.
Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are enriched
in inactive X chromosome chromatin. Monomethylation at Lys-57
(H3K56me1) by EHMT2/G9A in G1 phase promotes interaction with PCNA
and is required for DNA replication.
-!- PTM: Phosphorylated at Thr-4 (H3T3ph) by HASPIN during prophase
and dephosphorylated during anaphase. Phosphorylation at Ser-11
(H3S10ph) by AURKB is crucial for chromosome condensation and
cell-cycle progression during mitosis and meiosis. In addition
phosphorylation at Ser-11 (H3S10ph) by RPS6KA4 and RPS6KA5 is
important during interphase because it enables the transcription
of genes following external stimulation, like mitogens, stress,
growth factors or UV irradiation and result in the activation of
genes, such as c-fos and c-jun. Phosphorylation at Ser-11
(H3S10ph), which is linked to gene activation, prevents
methylation at Lys-10 (H3K9me) but facilitates acetylation of H3
and H4. Phosphorylation at Ser-11 (H3S10ph) by AURKB mediates the
dissociation of HP1 proteins (CBX1, CBX3 and CBX5) from
heterochromatin. Phosphorylation at Ser-11 (H3S10ph) is also an
essential regulatory mechanism for neoplastic cell transformation.
Phosphorylated at Ser-29 (H3S28ph) by MAP3K20 isoform 1, RPS6KA5
or AURKB during mitosis or upon ultraviolet B irradiation.
Phosphorylation at Thr-7 (H3T6ph) by PRKCB is a specific tag for
epigenetic transcriptional activation that prevents demethylation
of Lys-5 (H3K4me) by LSD1/KDM1A. At centromeres, specifically
phosphorylated at Thr-12 (H3T11ph) from prophase to early
anaphase, by DAPK3 and PKN1. Phosphorylation at Thr-12 (H3T11ph)
by PKN1 is a specific tag for epigenetic transcriptional
activation that promotes demethylation of Lys-10 (H3K9me) by
KDM4C/JMJD2C. Phosphorylation at Tyr-42 (H3Y41ph) by JAK2 promotes
exclusion of CBX5 (HP1 alpha) from chromatin. Phosphorylation on
Ser-32 (H3S31ph) is specific to regions bordering centromeres in
metaphase chromosomes. {ECO:0000250|UniProtKB:P84243}.
-!- PTM: Ubiquitinated. Monoubiquitinated by RAG1 in lymphoid cells,
monoubiquitination is required for V(D)J recombination (By
similarity). {ECO:0000250|UniProtKB:P84245}.
-!- PTM: Lysine deamination at Lys-5 (H3K4all) to form allysine is
mediated by LOXL2. Allysine formation by LOXL2 only takes place on
H3K4me3 and results in gene repression.
-!- 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:0000250|UniProtKB:P84243}.
-!- PTM: Butyrylation of histones marks active promoters and competes
with histone acetylation. It is present during late
spermatogenesis. {ECO:0000250|UniProtKB:P68433}.
-!- PTM: Succinylation at Lys-80 (H3K79succ) by KAT2A takes place with
a maximum frequency around the transcription start sites of genes.
It gives a specific tag for epigenetic transcription activation.
-!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
Sequence=BAC56518.1; Type=Frameshift; Positions=90, 133; Evidence={ECO:0000305};
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
EMBL; AB099028; BAC56518.1; ALT_FRAME; mRNA.
EMBL; BT020962; AAX08979.1; -; mRNA.
EMBL; BT025472; ABF57428.1; -; mRNA.
EMBL; BC103071; AAI03072.1; -; mRNA.
EMBL; BC134734; AAI34735.1; -; mRNA.
RefSeq; NP_001014411.1; NM_001014389.2.
RefSeq; NP_001229500.1; NM_001242571.2.
UniGene; Bt.15474; -.
UniGene; Bt.60099; -.
UniGene; Bt.65132; -.
ProteinModelPortal; Q5E9F8; -.
SMR; Q5E9F8; -.
BioGrid; 160074; 16.
IntAct; Q5E9F8; 3.
MINT; Q5E9F8; -.
STRING; 9913.ENSBTAP00000034581; -.
iPTMnet; Q5E9F8; -.
PaxDb; Q5E9F8; -.
PRIDE; Q5E9F8; -.
Ensembl; ENSBTAT00000034186; ENSBTAP00000034086; ENSBTAG00000024561.
Ensembl; ENSBTAT00000034695; ENSBTAP00000034581; ENSBTAG00000024909.
GeneID; 326601; -.
GeneID; 617051; -.
KEGG; bta:326601; -.
KEGG; bta:617051; -.
CTD; 3020; -.
CTD; 3021; -.
eggNOG; KOG1745; Eukaryota.
eggNOG; COG2036; LUCA.
GeneTree; ENSGT00760000118967; -.
HOGENOM; HOG000155290; -.
HOVERGEN; HBG001172; -.
InParanoid; Q5E9F8; -.
KO; K11253; -.
OrthoDB; EOG091G0XGD; -.
TreeFam; TF314241; -.
Reactome; R-BTA-201722; Formation of the beta-catenin:TCF transactivating complex.
Reactome; R-BTA-212300; PRC2 methylates histones and DNA.
Reactome; R-BTA-2299718; Condensation of Prophase Chromosomes.
Reactome; R-BTA-2559580; Oxidative Stress Induced Senescence.
Reactome; R-BTA-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-BTA-427359; SIRT1 negatively regulates rRNA expression.
Reactome; R-BTA-427413; NoRC negatively regulates rRNA expression.
Reactome; R-BTA-5250924; B-WICH complex positively regulates rRNA expression.
Reactome; R-BTA-5578749; Transcriptional regulation by small RNAs.
Reactome; R-BTA-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
Reactome; R-BTA-73728; RNA Polymerase I Promoter Opening.
Reactome; R-BTA-73777; RNA Polymerase I Chain Elongation.
Reactome; R-BTA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
Reactome; R-BTA-9018519; Estrogen-dependent gene expression.
Reactome; R-BTA-983231; Factors involved in megakaryocyte development and platelet production.
Proteomes; UP000009136; Chromosome 16.
Proteomes; UP000009136; Chromosome 19.
Bgee; ENSBTAG00000024561; -.
GO; GO:0001740; C:Barr body; IEA:Ensembl.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IEA:Ensembl.
GO; GO:0000788; C:nuclear nucleosome; IEA:Ensembl.
GO; GO:0000786; C:nucleosome; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0031492; F:nucleosomal DNA binding; IBA:GO_Central.
GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0000980; F:RNA polymerase II distal enhancer sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
GO; GO:0006336; P:DNA replication-independent nucleosome assembly; IEA:Ensembl.
GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
GO; GO:0008584; P:male gonad development; IEA:Ensembl.
GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
GO; GO:0042692; P:muscle cell differentiation; IEA:Ensembl.
GO; GO:1902340; P:negative regulation of chromosome condensation; IEA:Ensembl.
GO; GO:0006334; P:nucleosome assembly; IBA:GO_Central.
GO; GO:0006997; P:nucleus organization; IEA:Ensembl.
GO; GO:0048477; P:oogenesis; IEA:Ensembl.
GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
GO; GO:0031508; P:pericentric heterochromatin assembly; IEA:Ensembl.
GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
GO; GO:0090230; P:regulation of centromere complex assembly; IEA:Ensembl.
GO; GO:0007338; P:single fertilization; IEA:Ensembl.
GO; GO:0007286; P:spermatid development; IEA:Ensembl.
GO; GO:0031509; P:telomeric heterochromatin assembly; IEA:Ensembl.
Gene3D;; -; 1.
InterPro; IPR009072; Histone-fold.
InterPro; IPR007125; Histone_H2A/H2B/H3.
InterPro; IPR000164; Histone_H3/CENP-A.
PANTHER; PTHR11426; PTHR11426; 1.
Pfam; PF00125; Histone; 1.
SMART; SM00428; H3; 1.
SUPFAM; SSF47113; SSF47113; 1.
PROSITE; PS00322; HISTONE_H3_1; 1.
PROSITE; PS00959; HISTONE_H3_2; 1.
1: Evidence at protein level;
Acetylation; ADP-ribosylation; Chromosome; Citrullination;
Complete proteome; DNA-binding; Hydroxylation; Methylation;
Nucleosome core; Nucleus; Phosphoprotein; Reference proteome;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000305}.
CHAIN 2 136 Histone H3.3.
SITE 32 32 Interaction with ZMYND11.
MOD_RES 3 3 Asymmetric dimethylarginine; by PRMT6;
MOD_RES 3 3 Citrulline; alternate.
MOD_RES 4 4 Phosphothreonine; by HASPIN.
MOD_RES 5 5 Allysine; alternate.
MOD_RES 5 5 N6,N6,N6-trimethyllysine; alternate.
MOD_RES 5 5 N6,N6-dimethyllysine; alternate.
MOD_RES 5 5 N6-(2-hydroxyisobutyryl)lysine;
MOD_RES 5 5 N6-acetyllysine; alternate.
MOD_RES 5 5 N6-crotonyllysine; alternate.
MOD_RES 5 5 N6-methyllysine; alternate.
MOD_RES 7 7 Phosphothreonine; by PKC.
MOD_RES 9 9 Citrulline; alternate.
MOD_RES 9 9 Symmetric dimethylarginine; by PRMT5;
MOD_RES 10 10 N6,N6,N6-trimethyllysine; alternate.
MOD_RES 10 10 N6,N6-dimethyllysine; alternate.
MOD_RES 10 10 N6-(2-hydroxyisobutyryl)lysine;
MOD_RES 10 10 N6-acetyllysine; alternate.
MOD_RES 10 10 N6-crotonyllysine; alternate.
MOD_RES 10 10 N6-methyllysine; alternate.
MOD_RES 11 11 ADP-ribosylserine; alternate.
MOD_RES 11 11 Phosphoserine; alternate; by AURKB,
MOD_RES 12 12 Phosphothreonine; by PKC.
MOD_RES 15 15 N6-(2-hydroxyisobutyryl)lysine;
MOD_RES 15 15 N6-acetyllysine; alternate.
MOD_RES 15 15 N6-succinyllysine; alternate.
MOD_RES 18 18 Asymmetric dimethylarginine; by CARM1;
MOD_RES 18 18 Citrulline; alternate.
MOD_RES 19 19 N6-(2-hydroxyisobutyryl)lysine;
MOD_RES 19 19 N6-acetyllysine; alternate.
MOD_RES 19 19 N6-butyryllysine; alternate.
MOD_RES 19 19 N6-crotonyllysine; alternate.
MOD_RES 19 19 N6-methyllysine; alternate.
MOD_RES 24 24 N6-(2-hydroxyisobutyryl)lysine;
MOD_RES 24 24 N6-acetyllysine; alternate.
MOD_RES 24 24 N6-butyryllysine; alternate.
MOD_RES 24 24 N6-crotonyllysine; alternate.
MOD_RES 24 24 N6-methyllysine; alternate.
MOD_RES 27 27 Citrulline.
MOD_RES 28 28 N6,N6,N6-trimethyllysine; alternate.
MOD_RES 28 28 N6,N6-dimethyllysine; alternate.
MOD_RES 28 28 N6-(2-hydroxyisobutyryl)lysine;
MOD_RES 28 28 N6-acetyllysine; alternate.
MOD_RES 28 28 N6-crotonyllysine; alternate.
MOD_RES 28 28 N6-methyllysine; alternate.
MOD_RES 29 29 ADP-ribosylserine; alternate.
MOD_RES 29 29 Phosphoserine; alternate; by AURKB, AURKC
and RPS6KA5.
MOD_RES 32 32 Phosphoserine.
MOD_RES 37 37 N6,N6,N6-trimethyllysine; alternate.
MOD_RES 37 37 N6,N6-dimethyllysine; alternate.
MOD_RES 37 37 N6-(2-hydroxyisobutyryl)lysine;
MOD_RES 37 37 N6-acetyllysine; alternate.
MOD_RES 37 37 N6-methyllysine; alternate.
MOD_RES 38 38 N6-methyllysine.
MOD_RES 42 42 Phosphotyrosine.
MOD_RES 57 57 N6,N6,N6-trimethyllysine; alternate.
MOD_RES 57 57 N6-(2-hydroxyisobutyryl)lysine;
MOD_RES 57 57 N6-acetyllysine; alternate.
MOD_RES 57 57 N6-crotonyllysine; alternate.
MOD_RES 57 57 N6-methyllysine; by EHMT2; alternate.
MOD_RES 57 57 N6-succinyllysine; alternate.
MOD_RES 58 58 Phosphoserine.
MOD_RES 65 65 N6-(2-hydroxyisobutyryl)lysine;
MOD_RES 65 65 N6-methyllysine; alternate.
MOD_RES 80 80 N6,N6,N6-trimethyllysine; alternate.
MOD_RES 80 80 N6,N6-dimethyllysine; alternate.
MOD_RES 80 80 N6-(2-hydroxyisobutyryl)lysine;
MOD_RES 80 80 N6-acetyllysine; alternate.
MOD_RES 80 80 N6-methyllysine; alternate.
MOD_RES 80 80 N6-succinyllysine; alternate.
MOD_RES 81 81 Phosphothreonine.
MOD_RES 87 87 Phosphoserine.
MOD_RES 108 108 Phosphothreonine.
MOD_RES 116 116 N6-acetyllysine.
MOD_RES 123 123 N6-(2-hydroxyisobutyryl)lysine;
MOD_RES 123 123 N6-acetyllysine; alternate.
MOD_RES 123 123 N6-methyllysine; alternate.
MOD_RES 123 123 N6-succinyllysine; alternate.
SEQUENCE 136 AA; 15328 MW; 5158ED279E6F9E1C CRC64;

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

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



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


france@gentaur.com | Gentaur

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

Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,

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

spain@gentaur.com | Gentaur

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

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


Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

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