Histone 3 (H3) (2meLys27), (3meLys27) antibody

Details for Product No. ABIN4889658, Supplier: Log in to see
Antigen
  • H-3
  • histocompatibility 3
  • H3
Epitope
2meLys27, 3meLys27
159
122
115
109
92
85
85
84
81
79
74
66
61
60
57
57
44
44
41
41
38
36
35
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34
32
32
31
31
25
25
23
22
20
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11
10
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10
9
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5
5
5
5
5
4
4
4
4
4
4
4
4
4
4
4
4
4
4
4
4
3
3
3
3
3
3
3
3
3
3
3
3
3
2
2
2
2
2
2
2
2
2
2
2
2
2
2
2
2
2
2
2
2
2
2
2
2
2
2
2
2
2
2
2
2
2
2
2
2
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
Reactivity
Human
2353
1608
1030
574
94
75
74
74
71
69
60
49
37
34
34
32
31
23
15
10
4
4
3
3
3
2
2
2
2
2
2
2
2
2
1
1
1
1
1
1
1
1
1
1
1
1
1
Host
Mouse
2159
276
18
13
1
Clonality (Clone)
Monoclonal ()
Conjugate
Un-conjugated
75
68
63
51
50
47
39
39
39
39
39
26
21
19
8
8
8
7
7
7
7
7
7
3
2
2
2
Application
Immunocytochemistry (ICC), Immunofluorescence (IF), Western Blotting (WB)
2218
1034
711
683
647
592
424
320
144
133
105
100
92
57
48
15
8
7
5
3
2
1
1
1
1
1
1
1
Options
Supplier
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Supplier Product No.
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Immunogen This Histone H3 di/trimethylLys27 antibody was raised against a peptide including trimethyllysine 27 of histone H3.
Clone 7B11
Isotype IgG
Purification Protein A Chromatography
Antigen
Alternative Name Histone H3
Background Histone H3 is one of the core components of the nucleosome. The nucleosome is the smallest subunit of chromatin and consists of 147 base pairs of DNA wrapped around an octamer of core histone proteins (two each of Histone H2A, Histone H2B, Histone H3 and Histone H4). Histone H1 is a linker histone, present at the interface between the nucleosome core and DNA entry/exit points. Histone H1 is responsible for establishing higher-order chromatin structure. Chromatin is subject to a variety of chemical modifications, including post-translational modifications of the histone proteins and the methylation of cytosine residues in the DNA. Reported histone modifications include acetylation, methylation, phosphorylation, ubiquitylation, glycosylation, ADP-ribosylation, carbonylation and SUMOylation, these modifications play a major role in regulating gene expression. The methylation of histones can occur on two different residues: arginine or lysine. Histone methylation can be associated with transcriptional activation or repression, depending on the methylated residue. Lysine 27 of histone H3 can be mono-, di- or trimethylated (Histone H3 monomethyl Lys27, Histone H3 dimethyl Lys27 or H3K27me3) by different histone methyltransferases such as EZH2 or NSD3. Methylation of this residue is mainly associated with transcriptional repression.
Molecular Weight 17 kDa
Gene ID 3020
Application Notes Optimal working dilution should be determined by the investigator.
Restrictions For Research Use only
Format Liquid
Concentration 1 μg/μL
Preservative Sodium azide
Precaution of Use This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Handling Advice

Avoid repeated freeze/thaw cycles and keep on ice when not in storage.

Storage -20 °C
Storage Comment Antibodies in solution can be stored at -20 °C for 2 years.
Expiry Date 6 months
Supplier Images
Western Blotting (WB) image for anti-Histone 3 (H3) (2meLys27), (3meLys27) antibody (ABIN4889658) Histone H3 di/trimethyl Lys27 antibody (mAb) specificity data. HeLa acid extract (10 ...
Immunofluorescence (IF) image for anti-Histone 3 (H3) (2meLys27), (3meLys27) antibody (ABIN4889658) Histone H3 di/trimethyl Lys27 antibody (mAb) tested by immunofluorescence. Top: HeLa ...
Western Blotting (WB) image for anti-Histone 3 (H3) (2meLys27), (3meLys27) antibody (ABIN4889658) Histone H3 di/trimethyl Lys27 antibody (mAb) tested by Western blot. HeLa acid extrac...
Product cited in: Nolan, Franco, Hance, Hayward, Isaacs: "Tumor-secreted Hsp90 subverts polycomb function to drive prostate tumor growth and invasion." in: The Journal of biological chemistry, Vol. 290, Issue 13, pp. 8271-82, 2015 (PubMed).

Papazyan, Voronina, Chapman, Luperchio, Gilbert, Meier, Mackintosh, Shabanowitz, Tackett, Reddy, Coyne, Hunt, Liu, Taverna: "Methylation of histone H3K23 blocks DNA damage in pericentric heterochromatin during meiosis." in: eLife, Vol. 3, pp. e02996, 2014 (PubMed).

Ivanov, Pawlikowski, Manoharan, van Tuyn, Nelson, Rai, Shah, Hewitt, Korolchuk, Passos, Wu, Berger, Adams: "Lysosome-mediated processing of chromatin in senescence." in: The Journal of cell biology, Vol. 202, Issue 1, pp. 129-43, 2013 (PubMed).

Rada-Iglesias, Bajpai, Prescott, Brugmann, Swigut, Wysocka: "Epigenomic annotation of enhancers predicts transcriptional regulators of human neural crest." in: Cell stem cell, Vol. 11, Issue 5, pp. 633-48, 2012 (PubMed).

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