Histone H3.1 (HIST1H3B) (pSer10) antibody

Antigen: Histone H3.1 (HIST1H3B)

Synonyms: H3/l, H3FL, HIST1H3A, HIST1H3C, HIST1H3D, HIST1H3E, HIST1H3F, HIST1H3G, HIST1H3H, HIST1H3I, HIST1H3J, H3/A, H3FA, HIST1H3B, H3.1, H3/c, H3FC, H3/d, H3FD, H3.f, H3/f, H3FF, H3/h, H3FH, H3/j, H3FJ, H3/k, H3FK, H3F1K, FLJ92264, H3/i, H3FI, M32460, H3.1-221, Hist1h2ai, H3 histone, H3-H, Hist1h3a, Hist1h3g, Hist1h3h, MGC144390, Hist1h3i, H3F3, H3.3A, H3F3B, MGC87782, MGC87783, H3.3B, H3F3A, h3f3a, MGC52829, MGC86731, MGC165454, zgc:56193, zgc:86731, wu:fb58e10, MGC89877

Binding Site: pSer10

Clonality: Monoclonal

Host: Mouse

Reactivity: Human, Rat (Rattus)

Application: Western Blotting (WB), Immunohistochemistry (IHC), Immunofluorescence (IF)

Certificates: ISO 9001:2008

Catalog no.: ABIN658964

Additional Information

Alternative name: Histone H3.1

Gene ID: 8968

UniProt: P68431

Isotype: IgG

Description: Other names: Histone H3/l, Histone H3/k, Histone H3/j, Histone H3/i, Histone H3/h, Histone H3/f, Histone H3/d, Histone H3/c, Histone H3/b, Histone H3/a, Histone H3.1

Characteristics: Purified Rabbit Polyclonal Antibody (Pab)

Specificity: The antibody was affinity-purified from rabbit antiserum using epitope-specific phosphopeptide column, and the antibody against non-phosphopeptide was removed using non-phosphopeptide column corresponding to the phosphorylation site.

Molecular Weight: 15404 DA

Comments:

Background: Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. This structure consists of approximately 146 bp of DNA wrapped around a nucleosome, an octamer composed of pairs of each of the four core histones (H2A, H2B, H3, and H4). The chromatin fiber is further compacted through the interaction of a linker histone, H1, with the DNA between the nucleosomes to form higher order chromatin structures. This gene is intronless and encodes a member of the histone H3 family. Transcripts from this gene lack polyA tails, instead, they contain a palindromic termination element. This gene is found in the large histone gene cluster on chromosome 6p22-p21.3.

Synonyms: H3/l, H3FL, HIST1H3A, HIST1H3C, HIST1H3D, HIST1H3E, HIST1H3F, HIST1H3G, HIST1H3H, HIST1H3I, HIST1H3J, H3/A, H3FA, HIST1H3B, H3.1, H3/c, H3FC, H3/d, H3FD, H3.f, H3/f, H3FF, H3/h, H3FH, H3/j, H3FJ, H3/k, H3FK, H3F1K, FLJ92264, H3/i, H3FI, M32460, H3.1-221, Hist1h2ai, H3 histone, H3-H, Hist1h3a, Hist1h3g, Hist1h3h, MGC144390, Hist1h3i, H3F3, H3.3A, H3F3B, MGC87782, MGC87783, H3.3B, H3F3A, h3f3a, MGC52829, MGC86731, MGC165454, zgc:56193, zgc:86731, wu:fb58e10, MGC89877

Application Details

Application Notes: The suggested dilution is: WB: 1:500~1:1000 IHC: 1:50-1:100 IF: 1:100-200

Concentration: 1mg/ml

Purification: Purified

Buffer: affinity Purified IgG, in PBS, 0.02% sodium azide and 50% glycerol.

Storage: Maintain refrigerated at 2-8 deg C for up to 6 months. For long term storage store at -20 deg C in small aliquots to prevent freeze-thaw cycles

Research Area: Ubiquitin-related antibodies, Signaling, Phospho-specific antibodies, Protein Modifications, Transcription Factors, Chromatin, Cell Structure

Restrictions: For Research Use only

Publications

Product: Citterio, Papait, Nicassio et al.: "Np95 is a histone-binding protein endowed with ubiquitin ligase activity." in: Molecular and cellular biology, Vol. 24, Issue 6, pp. 2526-35, 2004 (PubMed).

Berndsen, Tsubota, Lindner et al.: "Molecular functions of the histone acetyltransferase chaperone complex Rtt109-Vps75." in: Nature structural & molecular biology, Vol. 15, Issue 9, pp. 948-56, 2009 (PubMed).

Wu, Min, Lunin et al.: "Structural biology of human H3K9 methyltransferases." in: PLoS ONE, Vol. 5, Issue 1, pp. e8570, 2010 (PubMed).

Osakabe, Tachiwana, Matsunaga et al.: "Nucleosome formation activity of human somatic nuclear autoantigenic sperm protein (sNASP)." in: The Journal of biological chemistry, Vol. 285, Issue 16, pp. 11913-21, 2010 (PubMed).

Feng, Yonezawa, Ye et al.: "PHF8 activates transcription of rRNA genes through H3K4me3 binding and H3K9me1/2 demethylation." in: Nature structural & molecular biology, Vol. 17, Issue 4, pp. 445-50, 2010 (PubMed).