Histone H2B antibody

Catalog No. ABIN7938172

This Rabbit Polyclonal antibody specifically detects Histone H2B in WB and ChIP. It exhibits reactivity toward Saccharomyces cerevisiae and Schizosaccharomyces pombe. It has been mentioned in 17+ publications

Quick Overview for Histone H2B antibody (ABIN7938172)

Target: Histone H2B

Reactivity: Saccharomyces cerevisiae, Schizosaccharomyces pombe

Host: Rabbit

Clonality: Polyclonal

Conjugate: This Histone H2B antibody is un-conjugated

Application: Western Blotting (WB), Chromatin Immunoprecipitation (ChIP)

Product Details anti-Histone H2B Antibody

Purpose: Histone H2B antibody (pAb)

Purification: Unpurified

Immunogen: This yeast histone H2B antibody was raised against recombinant yeast histone H2B.

Application Details

Application Notes: WB: 1:1,000 - 1:5,000 dilution

Restrictions: For Research Use only

Handling

Format: Liquid

Buffer: Rabbit serum containing 30 % glycerol and 0.035 % sodium azide.

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 by aliquoting items into single-use fractions,Keep all reagents on ice when not in storage

Storage: -20 °C

Storage Comment: Some products may be shipped at room temperature. This will not affect their stability or performance. Avoid repeated freeze/thaw cycles by aliquoting items into single-use fractions for storage at -20°C for up to 2 years. Keep all reagents on ice when not in storage.

Expiry Date: 24 months

References for anti-Histone H2B antibody (ABIN7938172)

Brahma, Henikoff: "RSC-Associated Subnucleosomes Define MNase-Sensitive Promoters in Yeast." in: Molecular cell, Vol. 73, Issue 2, pp. 238-249.e3, (2019) (PubMed).

Chen, DArcy, Radebaugh, Krzizike, Giebler, Huang, Nyborg, Luger, Stargell: "Histone Chaperone Nap1 Is a Major Regulator of Histone H2A-H2B Dynamics at the Inducible GAL Locus." in: Molecular and cellular biology, Vol. 36, Issue 8, pp. 1287-96, (2016) (PubMed).

Materne, Vázquez, Sánchez, Yague-Sanz, Anandhakumar, Migeot, Antequera, Hermand: "Histone H2B ubiquitylation represses gametogenesis by opposing RSC-dependent chromatin remodeling at the ste11 master regulator locus." in: eLife, Vol. 5, (2016) (PubMed).

Stulemeijer, De Vos, van Harten, Joshi, Blomberg, van Welsem, Terweij, Vlaming, de Graaf, Altelaar, Bakker, van Leeuwen: "Dot1 histone methyltransferases share a distributive mechanism but have highly diverged catalytic properties." in: Scientific reports, Vol. 5, pp. 9824, (2015) (PubMed).

Zheng, Crickard, Srikanth, Reese: "A highly conserved region within H2B is important for FACT to act on nucleosomes." in: Molecular and cellular biology, Vol. 34, Issue 3, pp. 303-14, (2014) (PubMed).

Bonizec, Hérissant, Pokrzywa, Geng, Wenzel, Howard, Rodriguez, Krause, Tansey, Hoppe, Dargemont: "The ubiquitin-selective chaperone Cdc48/p97 associates with Ubx3 to modulate monoubiquitylation of histone H2B." in: Nucleic acids research, Vol. 42, Issue 17, pp. 10975-86, (2014) (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).

Bennett, Papamichos-Chronakis, Peterson: "DNA repair choice defines a common pathway for recruitment of chromatin regulators." in: Nature communications, Vol. 4, pp. 2084, (2013) (PubMed).

Rizzardi, Dorn, Strahl, Cook: "DNA replication origin function is promoted by H3K4 di-methylation in Saccharomyces cerevisiae." in: Genetics, Vol. 192, Issue 2, pp. 371-84, (2012) (PubMed).

Samel, Cuomo, Bonaldi, Ehrenhofer-Murray: "Methylation of CenH3 arginine 37 regulates kinetochore integrity and chromosome segregation." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 109, Issue 23, pp. 9029-34, (2012) (PubMed).

Moehle, Ryan, Krogan, Kress, Guthrie: "The yeast SR-like protein Npl3 links chromatin modification to mRNA processing." in: PLoS genetics, Vol. 8, Issue 11, pp. e1003101, (2012) (PubMed).

Gardner, Zhou, Parra, Chen, Strahl: "Identification of lysine 37 of histone H2B as a novel site of methylation." in: PLoS ONE, Vol. 6, Issue 1, pp. e16244, (2011) (PubMed).

Chandrasekharan, Huang, Sun: "Decoding the trans-histone crosstalk: methods to analyze H2B ubiquitination, H3 methylation and their regulatory factors." in: Methods (San Diego, Calif.), Vol. 54, Issue 3, pp. 304-14, (2011) (PubMed).

Batta, Zhang, Yen, Goffman, Pugh: "Genome-wide function of H2B ubiquitylation in promoter and genic regions." in: Genes & development, Vol. 25, Issue 21, pp. 2254-65, (2011) (PubMed).

Kyriss, Jin, Gallegos, Sanford, Wyrick: "Novel functional residues in the core domain of histone H2B regulate yeast gene expression and silencing and affect the response to DNA damage." in: Molecular and cellular biology, Vol. 30, Issue 14, pp. 3503-18, (2010) (PubMed).

Nag, Kyriss, Smerdon, Wyrick, Smerdon: "A cassette of N-terminal amino acids of histone H2B are required for efficient cell survival, DNA repair and Swi/Snf binding in UV irradiated yeast." in: Nucleic acids research, Vol. 38, Issue 5, pp. 1450-60, (2010) (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).

Target Details for Histone H2B

Target: Histone H2B

Background: Histone H2B 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, it 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, they play a major role in regulating gene expression.

Molecular Weight: 14 kDa

NCBI Accession: NP_010510