Histone H2A antibody

Details for Product No. ABIN4889652, Supplier: Log in to see
Antigen
  • 5499
  • CG5499
  • Dmel\\CG5499
  • H2A
  • H2A.F/Z
  • H2A.X
  • H2A.Z
  • H2AV
  • H2AV_DROM
  • H2AX
  • H2AZ
  • H2Av
  • H2AvD
  • H2a.V
  • H2av
  • H2avD
  • HIS
  • HIS2AV
  • HIS2AVD
  • His
  • His2
  • His2AV
  • His2AvD
  • HisH2Av
  • Hist
  • Hist2av
  • gamma-H2Av
  • gamma-HIS2AV
  • gamma-His2Av
  • gammaH2Av
  • h2AvD
  • his
  • l(3)05146
  • l(3)810
  • l(3)97Dd
  • l(3)L1602
  • DDBDRAFT_0205974
  • DDBDRAFT_0216271
  • DDB_0205974
  • DDB_0216271
  • RGD1564767
  • H2a-221
  • H2A-III
  • HIST1H2AA
  • Histone H2A variant
  • putative histone H2A
  • histone H2A
  • histone cluster 1 H2A family member F
  • histone H2A-like
  • histone cluster 1, H2af
  • histone2A1
  • histone cluster 1, H2A, III
  • histone cluster 1, H2ac
  • His2Av
  • LMJF_17_0280
  • H2AX
  • Hist1h2af
  • LOC100425378
  • his2a1
  • HIST1H2A3
  • HIST1H2AC
  • h2a-A
Reactivity
Schizosaccharomyces pombe, Yeast (Saccharomyces cerevisiae)
144
100
94
6
5
3
3
3
3
3
2
2
2
2
2
1
1
1
1
Host
Rabbit
150
2
Clonality
Polyclonal
Conjugate
Un-conjugated
1
1
1
1
1
1
1
1
1
1
1
1
1
1
Application
Western Blotting (WB)
112
57
57
25
17
15
14
8
8
5
1
1
Options
Supplier
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Supplier Product No.
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Immunogen This Histone H2A antibody was raised against recombinant yeast histone H2A.
Purification None
Antigen
Background Histone H2A 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.
Molecular Weight 14 kDa
Application Notes Optimal working dilution should be determined by the investigator.
Restrictions For Research Use only
Format Liquid
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 H2A antibody (ABIN4889652) Histone H2A anbtibody (pAb) tested by Western blot. Detection of Histone H2A by Weste...
Product cited in: Young, Hillyer, Hokamp, Fitzpatrick, Konstantinov, Welty, Ness, Werner-Washburne, Fleming, Osley: "Distinct histone methylation and transcription profiles are established during the development of cellular quiescence in yeast." in: BMC genomics, Vol. 18, Issue 1, pp. 107, 2017 (PubMed).

Ferrari, Bruhn, Peretti, Cassani, Carotenuto, Elgendy, Shubassi, Lucca, Bermejo, Varasi, Minucci, Longhese, Foiani: "PP2A Controls Genome Integrity by Integrating Nutrient-Sensing and Metabolic Pathways with the DNA Damage Response." in: Molecular cell, Vol. 67, Issue 2, pp. 266-281.e4, 2017 (PubMed).

Fleming, Beggs, Church, Tsukihashi, Pennings: "The yeast Cyc8-Tup1 complex cooperates with Hda1p and Rpd3p histone deacetylases to robustly repress transcription of the subtelomeric FLO1 gene." in: Biochimica et biophysica acta, Vol. 1839, Issue 11, pp. 1242-55, 2014 (PubMed).

Bandhu, Kang, Fukunaga, Goto, Sugimoto: "Ddc2 mediates Mec1 activation through a Ddc1- or Dpb11-independent mechanism." in: PLoS genetics, Vol. 10, Issue 2, pp. e1004136, 2014 (PubMed).

Tessarz, Santos-Rosa, Robson, Sylvestersen, Nelson, Nielsen, Kouzarides: "Glutamine methylation in histone H2A is an RNA-polymerase-I-dedicated modification." in: Nature, Vol. 505, Issue 7484, pp. 564-8, 2014 (PubMed).

Jha, Strahl: "An RNA polymerase II-coupled function for histone H3K36 methylation in checkpoint activation and DSB repair." in: Nature communications, Vol. 5, pp. 3965, 2014 (PubMed).

Limbo, Moiani, Kertokalio, Wyman, Tainer, Russell: "Mre11 ATLD17/18 mutation retains Tel1/ATM activity but blocks DNA double-strand break repair." in: Nucleic acids research, Vol. 40, Issue 22, pp. 11435-49, 2012 (PubMed).

Andrews, Chen, Zevin, Stargell, Luger: "The histone chaperone Nap1 promotes nucleosome assembly by eliminating nonnucleosomal histone DNA interactions." in: Molecular cell, Vol. 37, Issue 6, pp. 834-42, 2010 (PubMed).

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