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
164
115
115
107
92
84
82
82
81
78
74
64
60
59
58
57
43
43
41
40
37
36
35
35
34
32
32
32
30
27
24
23
22
20
20
19
19
18
18
17
17
17
16
16
16
16
16
16
15
15
15
15
12
11
11
10
10
10
9
9
9
9
9
7
7
7
6
6
6
5
5
5
5
5
5
5
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
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
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
2280
1550
969
574
94
75
73
73
71
69
60
49
37
35
33
32
23
15
10
4
4
4
3
3
2
2
2
2
2
2
2
2
1
1
1
1
1
1
1
1
1
1
1
1
1
Host
Mouse
2080
280
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)
2145
973
681
646
644
551
424
280
143
108
105
100
92
57
46
16
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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