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Histone H3

 H3_CAEEL                Reviewed;         136 AA.
P08898; Q9TW44;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
23-MAY-2018, entry version 160.
RecName: Full=Histone H3;
Name=his-2; ORFNames=T10C6.13;
and
Name=his-6; ORFNames=F45F2.13;
and
Name=his-9; ORFNames=ZK131.3;
and
Name=his-13; ORFNames=ZK131.7;
and
Name=his-17; ORFNames=K06C4.5;
and
Name=his-25; ORFNames=ZK131.2;
and
Name=his-27; ORFNames=K06C4.13;
and
Name=his-32; ORFNames=F17E9.10;
and
Name=his-42; ORFNames=F08G2.3;
and
Name=his-45; ORFNames=B0035.10;
and
Name=his-49; ORFNames=F07B7.5;
and
Name=his-55; ORFNames=F54E12.1;
and
Name=his-59; ORFNames=F55G1.2;
and
Name=his-63; ORFNames=F22B3.2;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIS-10).
STRAIN=Bristol N2;
PubMed=2544730; DOI=10.1016/0022-2836(89)90566-4;
Roberts S.B., Emmons S.W., Childs G.;
"Nucleotide sequences of Caenorhabditis elegans core histone genes.
Genes for different histone classes share common flanking sequence
elements.";
J. Mol. Biol. 206:567-577(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2;
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (HIS-4).
STRAIN=Bristol N2;
Kohara Y., Shin-i T., Suzuki Y., Sugano S., Potdevin M.,
Thierry-Mieg Y., Thierry-Mieg D., Thierry-Mieg J.;
"The Caenorhabditis elegans transcriptome project, a complementary
view of the genome.";
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
[4]
PROTEIN SEQUENCE OF 2-136, ACETYLATION AT LYS-5; LYS-15 AND LYS-24,
AND METHYLATION AT LYS-10; LYS-28; LYS-37 AND LYS-80.
STRAIN=DR27;
PubMed=3803587; DOI=10.1016/0014-5793(87)81274-7;
Vanfleteren J.R., van Bun S.M., van Beeumen J.J.;
"The primary structure of histone H3 from the nematode Caenorhabditis
elegans.";
FEBS Lett. 211:59-63(1987).
[5]
PHOSPHORYLATION AT SER-11.
PubMed=10975519; DOI=10.1016/S0092-8674(00)00034-9;
Hsu J.-Y., Sun Z.-W., Li X., Reuben M., Tatchell K., Bishop D.K.,
Grushcow J.M., Brame C.J., Caldwell J.A., Hunt D.F., Lin R.,
Smith M.M., Allis C.D.;
"Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora
kinase and Glc7/PP1 phosphatase in budding yeast and nematodes.";
Cell 102:279-291(2000).
[6]
PHOSPHORYLATION AT SER-11 AND SER-29.
PubMed=12015116; DOI=10.1016/S0960-9822(02)00820-5;
Kaitna S., Pasierbek P., Jantsch M., Loidl J., Glotzer M.;
"The aurora B kinase AIR-2 regulates kinetochores during mitosis and
is required for separation of homologous Chromosomes during meiosis.";
Curr. Biol. 12:798-812(2002).
[7]
METHYLATION AT LYS-5 AND LYS-10, PHOSPHORYLATION AT SER-11, AND
ACETYLATION AT LYS-10 AND LYS-15.
PubMed=11807039;
Kelly W.G., Schaner C.E., Dernburg A.F., Lee M.-H., Kim S.K.,
Villeneuve A.M., Reinke V.;
"X-chromosome silencing in the germline of C. elegans.";
Development 129:479-492(2002).
[8]
METHYLATION AT LYS-5 AND LYS-10.
PubMed=11969256; DOI=10.1006/dbio.2002.0634;
Reuben M., Lin R.;
"Germline X chromosomes exhibit contrasting patterns of histone H3
methylation in Caenorhabditis elegans.";
Dev. Biol. 245:71-82(2002).
[9]
PHOSPHORYLATION AT SER-11, AND METHYLATION AT LYS-5; LYS-10 AND
LYS-37.
PubMed=14614817; DOI=10.1016/j.cub.2003.10.035;
Han Z., Saam J.R., Adams H.P., Mango S.E., Schumacher J.M.;
"The C. elegans Tousled-like kinase (TLK-1) has an essential role in
transcription.";
Curr. Biol. 13:1921-1929(2003).
[10]
PHOSPHORYLATION AT SER-11.
PubMed=12837290; DOI=10.1016/S0014-4827(03)00157-5;
Sassa T., Ueda-Ohba H., Kitamura K., Harada S., Hosono R.;
"Role of Caenorhabditis elegans protein phosphatase type 1, CeGLC-7
beta, in metaphase to anaphase transition during embryonic
development.";
Exp. Cell Res. 287:350-360(2003).
[11]
PHOSPHORYLATION AT SER-11 AND SER-29.
PubMed=14622138; DOI=10.1046/j.1365-2443.2003.00682.x;
Sasagawa Y., Urano T., Kohara Y., Takahashi H., Higashitani A.;
"Caenorhabditis elegans RBX1 is essential for meiosis, mitotic
chromosomal condensation and segregation, and cytokinesis.";
Genes Cells 8:857-872(2003).
[12]
METHYLATION AT LYS-28.
PubMed=15380065; DOI=10.1016/j.cub.2004.08.062;
Bender L.B., Cao R., Zhang Y., Strome S.;
"The MES-2/MES-3/MES-6 complex and regulation of histone H3
methylation in C. elegans.";
Curr. Biol. 14:1639-1643(2004).
[13]
ACETYLATION AT LYS-10 AND LYS-15, METHYLATION AT LYS-5 AND LYS-10, AND
PHOSPHORYLATION AT SER-11.
PubMed=14702046; DOI=10.1038/ng1283;
Bean C.J., Schaner C.E., Kelly W.G.;
"Meiotic pairing and imprinted X chromatin assembly in Caenorhabditis
elegans.";
Nat. Genet. 36:100-105(2004).
[14]
METHYLATION AT LYS-10 AND LYS-37.
PubMed=16603238; DOI=10.1016/j.cell.2006.03.028;
Whetstine J.R., Nottke A., Lan F., Huarte M., Smolikov S., Chen Z.,
Spooner E., Li E., Zhang G., Colaiacovo M., Shi Y.;
"Reversal of histone lysine trimethylation by the JMJD2 family of
histone demethylases.";
Cell 125:467-481(2006).
-!- 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: Phosphorylated at Ser-11 and Ser-29 during M phase.
Phosphorylation of Ser-11 requires air-2 but not air-1.
Dephosphorylated by gsp-1 and/or gsp-2 during chromosome
segregation. {ECO:0000269|PubMed:10975519,
ECO:0000269|PubMed:11807039, ECO:0000269|PubMed:12015116,
ECO:0000269|PubMed:12837290, ECO:0000269|PubMed:14614817,
ECO:0000269|PubMed:14622138, ECO:0000269|PubMed:14702046}.
-!- PTM: Acetylation is generally linked to gene activation.
{ECO:0000250}.
-!- PTM: Methylation at Lys-5 is linked to gene activation and is
absent from male inactive X chromosome chromatin. Methylation at
Lys-10 is linked to gene repression and is enriched in male
inactive X chromosome chromatin. Methylation at Lys-37 occurs on
the entire length of autosomes during meiotic prophase.
Trimethylation at Lys-10 and Lys-37 is specifically antagonized by
jmjd-2. Dimethylation and trimethylation at Lys-28 occurs in all
nuclei. The mes-2-mes-3-mes-6 complex may be responsible for Lys-
28 methylation in most of the germline and in the early embryo.
{ECO:0000269|PubMed:11807039, ECO:0000269|PubMed:11969256,
ECO:0000269|PubMed:14614817, ECO:0000269|PubMed:14702046,
ECO:0000269|PubMed:15380065, ECO:0000269|PubMed:16603238,
ECO:0000269|PubMed:3803587}.
-!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
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EMBL; X15634; CAA33644.1; -; Genomic_DNA.
EMBL; FO081018; CCD68531.1; -; Genomic_DNA.
EMBL; FO081059; CCD68868.1; -; Genomic_DNA.
EMBL; FO081135; CCD69390.1; -; Genomic_DNA.
EMBL; FO081223; CCD70027.1; -; Genomic_DNA.
EMBL; FO081551; CCD72363.1; -; Genomic_DNA.
EMBL; FO081551; CCD72373.1; -; Genomic_DNA.
EMBL; Z68336; CAA92733.1; -; Genomic_DNA.
EMBL; Z73102; CAA97411.1; -; Genomic_DNA.
EMBL; Z81495; CAB04057.1; -; Genomic_DNA.
EMBL; Z82271; CAB05209.1; -; Genomic_DNA.
EMBL; Z83245; CAB05831.1; -; Genomic_DNA.
EMBL; Z83245; CAB05833.1; -; Genomic_DNA.
EMBL; Z83245; CAB05834.1; -; Genomic_DNA.
EMBL; Z93388; CAB07653.1; -; Genomic_DNA.
EMBL; AF304122; AAG50235.1; -; mRNA.
PIR; S04241; HSKW3.
RefSeq; NP_001263958.1; NM_001277029.1.
RefSeq; NP_496890.1; NM_064489.1.
RefSeq; NP_496894.1; NM_064493.5.
RefSeq; NP_496895.1; NM_064494.1.
RefSeq; NP_496899.1; NM_064498.1.
RefSeq; NP_501204.1; NM_068803.3.
RefSeq; NP_501407.1; NM_069006.3.
RefSeq; NP_502134.1; NM_069733.3.
RefSeq; NP_502138.1; NM_069737.1.
RefSeq; NP_502153.1; NM_069752.3.
RefSeq; NP_505199.1; NM_072798.1.
RefSeq; NP_505276.1; NM_072875.1.
RefSeq; NP_505292.1; NM_072891.1.
RefSeq; NP_505297.1; NM_072896.3.
RefSeq; NP_507033.1; NM_074632.3.
UniGene; Cel.12716; -.
UniGene; Cel.12871; -.
UniGene; Cel.21447; -.
UniGene; Cel.21596; -.
UniGene; Cel.21806; -.
UniGene; Cel.21871; -.
UniGene; Cel.2350; -.
UniGene; Cel.27007; -.
UniGene; Cel.29106; -.
UniGene; Cel.29299; -.
UniGene; Cel.32605; -.
UniGene; Cel.32856; -.
UniGene; Cel.33056; -.
PDB; 3N9L; X-ray; 2.80 A; B=2-16.
PDB; 3N9N; X-ray; 2.30 A; B/C=2-33.
PDB; 3N9O; X-ray; 2.31 A; B=2-16, C=2-18.
PDB; 3N9P; X-ray; 2.39 A; B/C=2-33.
PDB; 3N9Q; X-ray; 2.30 A; B=2-16, C=20-36.
PDBsum; 3N9L; -.
PDBsum; 3N9N; -.
PDBsum; 3N9O; -.
PDBsum; 3N9P; -.
PDBsum; 3N9Q; -.
ProteinModelPortal; P08898; -.
SMR; P08898; -.
BioGrid; 42741; 1.
BioGrid; 45065; 3.
BioGrid; 50996; 1.
IntAct; P08898; 1.
STRING; 6239.ZK131.7; -.
iPTMnet; P08898; -.
PaxDb; P08898; -.
PeptideAtlas; P08898; -.
PRIDE; P08898; -.
GeneID; 13221387; -.
GeneID; 175030; -.
GeneID; 175031; -.
GeneID; 177628; -.
GeneID; 180074; -.
GeneID; 181821; -.
GeneID; 184113; -.
GeneID; 184200; -.
GeneID; 184804; -.
GeneID; 186250; -.
GeneID; 186325; -.
GeneID; 191668; -.
GeneID; 191672; -.
GeneID; 191673; -.
GeneID; 246024; -.
KEGG; cel:CELE_B0035.10; -.
KEGG; cel:CELE_F07B7.5; -.
KEGG; cel:CELE_F08G2.3; -.
KEGG; cel:CELE_F17E9.10; -.
KEGG; cel:CELE_F22B3.2; -.
KEGG; cel:CELE_F45F2.13; -.
KEGG; cel:CELE_F54E12.1; -.
KEGG; cel:CELE_F55G1.2; -.
KEGG; cel:CELE_K03A1.1; -.
KEGG; cel:CELE_K06C4.13; -.
KEGG; cel:CELE_K06C4.5; -.
KEGG; cel:CELE_T10C6.13; -.
KEGG; cel:CELE_ZK131.2; -.
KEGG; cel:CELE_ZK131.3; -.
KEGG; cel:CELE_ZK131.7; -.
UCSC; ZK131.7; c. elegans.
CTD; 13221387; -.
CTD; 175030; -.
CTD; 175031; -.
CTD; 177628; -.
CTD; 180074; -.
CTD; 181821; -.
CTD; 184113; -.
CTD; 184200; -.
CTD; 184804; -.
CTD; 186250; -.
CTD; 186325; -.
CTD; 191668; -.
CTD; 191672; -.
CTD; 191673; -.
CTD; 246024; -.
WormBase; B0035.10; CE03253; WBGene00001919; his-45.
WormBase; F07B7.5; CE03253; WBGene00001923; his-49.
WormBase; F08G2.3; CE03253; WBGene00001916; his-42.
WormBase; F17E9.10; CE03253; WBGene00001906; his-32.
WormBase; F22B3.2; CE03253; WBGene00001937; his-63.
WormBase; F45F2.13; CE03253; WBGene00001880; his-6.
WormBase; F54E12.1; CE03253; WBGene00001929; his-55.
WormBase; F55G1.2; CE03253; WBGene00001933; his-59.
WormBase; K06C4.13; CE03253; WBGene00001901; his-27.
WormBase; K06C4.5; CE03253; WBGene00001891; his-17.
WormBase; T10C6.13; CE03253; WBGene00001876; his-2.
WormBase; ZK131.2; CE03253; WBGene00001899; his-25.
WormBase; ZK131.3; CE03253; WBGene00001883; his-9.
WormBase; ZK131.7; CE03253; WBGene00001887; his-13.
eggNOG; KOG1745; Eukaryota.
eggNOG; COG2036; LUCA.
HOGENOM; HOG000155290; -.
InParanoid; P08898; -.
KO; K11253; -.
OrthoDB; EOG091G0XGD; -.
PhylomeDB; P08898; -.
Reactome; R-CEL-212300; PRC2 methylates histones and DNA.
Reactome; R-CEL-2299718; Condensation of Prophase Chromosomes.
Reactome; R-CEL-2559580; Oxidative Stress Induced Senescence.
Reactome; R-CEL-3214815; HDACs deacetylate histones.
Reactome; R-CEL-3214841; PKMTs methylate histone lysines.
Reactome; R-CEL-3214842; HDMs demethylate histones.
Reactome; R-CEL-3214847; HATs acetylate histones.
Reactome; R-CEL-3214858; RMTs methylate histone arginines.
Reactome; R-CEL-427359; SIRT1 negatively regulates rRNA expression.
Reactome; R-CEL-5578749; Transcriptional regulation by small RNAs.
Reactome; R-CEL-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
Reactome; R-CEL-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-CEL-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
Reactome; R-CEL-9018519; Estrogen-dependent gene expression.
Reactome; R-CEL-983231; Factors involved in megakaryocyte development and platelet production.
EvolutionaryTrace; P08898; -.
PRO; PR:P08898; -.
Proteomes; UP000001940; Chromosome II.
Proteomes; UP000001940; Chromosome IV.
Proteomes; UP000001940; Chromosome V.
Bgee; WBGene00001876; -.
ExpressionAtlas; P08898; baseline and differential.
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:0006334; P:nucleosome assembly; IBA:GO_Central.
Gene3D; 1.10.20.10; -; 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.
PRINTS; PR00622; HISTONEH3.
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;
3D-structure; Acetylation; Chromosome; Complete proteome;
Direct protein sequencing; DNA-binding; Methylation; Nucleosome core;
Nucleus; Phosphoprotein; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:3803587}.
CHAIN 2 136 Histone H3.
/FTId=PRO_0000221297.
MOD_RES 5 5 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000269|PubMed:11807039,
ECO:0000269|PubMed:11969256,
ECO:0000269|PubMed:14614817,
ECO:0000269|PubMed:14702046}.
MOD_RES 5 5 N6,N6-dimethyllysine; alternate.
{ECO:0000269|PubMed:11807039,
ECO:0000269|PubMed:11969256,
ECO:0000269|PubMed:14614817,
ECO:0000269|PubMed:14702046}.
MOD_RES 5 5 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:3803587}.
MOD_RES 5 5 N6-methyllysine; alternate.
{ECO:0000269|PubMed:11807039,
ECO:0000269|PubMed:11969256,
ECO:0000269|PubMed:14614817,
ECO:0000269|PubMed:14702046}.
MOD_RES 10 10 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000269|PubMed:11807039,
ECO:0000269|PubMed:11969256,
ECO:0000269|PubMed:14614817,
ECO:0000269|PubMed:14702046,
ECO:0000269|PubMed:16603238,
ECO:0000269|PubMed:3803587}.
MOD_RES 10 10 N6,N6-dimethyllysine; alternate.
{ECO:0000269|PubMed:11807039,
ECO:0000269|PubMed:11969256,
ECO:0000269|PubMed:14614817,
ECO:0000269|PubMed:14702046,
ECO:0000269|PubMed:16603238,
ECO:0000269|PubMed:3803587}.
MOD_RES 10 10 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:11807039,
ECO:0000269|PubMed:14702046}.
MOD_RES 11 11 Phosphoserine.
{ECO:0000269|PubMed:10975519,
ECO:0000269|PubMed:11807039,
ECO:0000269|PubMed:12015116,
ECO:0000269|PubMed:12837290,
ECO:0000269|PubMed:14614817,
ECO:0000269|PubMed:14622138,
ECO:0000269|PubMed:14702046}.
MOD_RES 15 15 N6-acetyllysine.
{ECO:0000269|PubMed:11807039,
ECO:0000269|PubMed:14702046,
ECO:0000269|PubMed:3803587}.
MOD_RES 24 24 N6-acetyllysine.
{ECO:0000269|PubMed:3803587}.
MOD_RES 28 28 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000269|PubMed:15380065,
ECO:0000269|PubMed:3803587}.
MOD_RES 28 28 N6,N6-dimethyllysine; alternate.
{ECO:0000269|PubMed:15380065,
ECO:0000269|PubMed:3803587}.
MOD_RES 28 28 N6-methyllysine; alternate.
{ECO:0000269|PubMed:15380065,
ECO:0000269|PubMed:3803587}.
MOD_RES 29 29 Phosphoserine.
{ECO:0000269|PubMed:12015116,
ECO:0000269|PubMed:14622138}.
MOD_RES 37 37 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000269|PubMed:14614817,
ECO:0000269|PubMed:16603238,
ECO:0000269|PubMed:3803587}.
MOD_RES 37 37 N6,N6-dimethyllysine; alternate.
{ECO:0000269|PubMed:14614817,
ECO:0000269|PubMed:16603238,
ECO:0000269|PubMed:3803587}.
MOD_RES 37 37 N6-methyllysine; alternate.
{ECO:0000269|PubMed:14614817,
ECO:0000269|PubMed:16603238,
ECO:0000269|PubMed:3803587}.
MOD_RES 80 80 N6-methyllysine.
{ECO:0000269|PubMed:3803587}.
VARIANT 97 97 C -> A.
VARIANT 101 101 L -> I.
STRAND 4 6 {ECO:0000244|PDB:3N9N}.
SEQUENCE 136 AA; 15376 MW; 40D7DE0EF5BA6F1F CRC64;
MARTKQTARK STGGKAPRKQ LATKAARKSA PASGGVKKPH RYRPGTVALR EIRRYQKSTE
LLIRRAPFQR LVREIAQDFK TDLRFQSSAV MALQEACEAY LVGLFEDTNL CAIHAKRVTI
MPKDIQLARR IRGERA


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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


 

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