09-838 Anti-Histone H3.3 Antibody

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      Key Specifications Table

      Species ReactivityKey ApplicationsHostFormatAntibody Type
      H, M WB, ICC, DB, ChIP Rb Affinity Purified Polyclonal Antibody
      Catalogue Number09-838
      DescriptionAnti-Histone H3.3 Antibody
      Alternate Names
      • Histone H3.3
      Background InformationHistone H3 is one of the five main histone proteins involved in the structure of chromatin in eukaryotic cells. Featuring a main globular domain and a long N-terminal tail, H3 is involved with the structure of the nucleosomes of the 'beads on a string' structure. The N-terminal tail of histone H3 protrudes from the globular nucleosome core and can undergo several different types of epigenetic modifications that influence cellular processes. These modifications include the covalent attachment of methyl or acetyl groups to lysine and arginine amino acids and the phosphorylation of serine or threonine. Histone variant H3.3 is typically enriched in active chromatin.
      Product Information
      FormatAffinity Purified
      • HeLa acid extract
      PresentationPurified rabbit polyclonal in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.
      Quality LevelMQ100
      ApplicationUse Anti-Histone H3.3 Antibody (Rabbit Polyclonal Antibody) validated in WB, ICC, DB, ChIP to detect Histone H3.3 also known as Histone H3.3.
      Key Applications
      • Western Blotting
      • Immunocytochemistry
      • Dot Blot
      • Chromatin Immunoprecipitation (ChIP)
      Application NotesImmunocytochemistry Analysis: A representative lot was used by an independent laboratory to detect Histone H3.3 in HeLa cells.
      Image courtesy of Simon Elsässer of David Allis' Laboratory, Rockefeller University, New York.

      Chromatin Immunoprecipitation Analysis: A representative lot was used by an independent laboratory in ChIP.
      Image courtesy of Simon Elsässer of David Allis' Laboratory, Rockefeller University, New York.

      Dot Blot Analysis: A representative lot was used by an independent laboratory in DB.
      Reported by Simon Elsässer, Laboratory of Dr. David Allis, Rockefeller University, New York.
      Biological Information
      ImmunogenKLH-conjugated linear peptide corresponding to human Histone H3.3.
      ConcentrationPlease refer to the Certificate of Analysis for the lot-specific concentration.
      Species Reactivity
      • Human
      • Mouse
      Species Reactivity NoteDemonstrated to react with Human and Mouse. Broad species cross-reactivity expected based on 100% sequence homology.
      Antibody TypePolyclonal Antibody
      Entrez Gene Number
      Entrez Gene SummaryHistones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which approximately 146 bp of DNA is wrapped in repeating units, called nucleosomes. The linker histone, H1, interacts with linker DNA between cleosomes and functions in the compaction of chromatin into higher order structures. This gene contains introns and its mRNA is polyadenylated, unlike most histone genes. The protein encoded is a replication-independent member of the histone H3 family. [provided by RefSeq].
      Gene Symbol
      • H3F3A
      • H3.3A
      • H3F3
      • PP781
      • H3F3B
      • H3.3B
      Purification MethodAffinity Purfied
      UniProt Number
      UniProt SummaryFUNCTION: Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes. Constitutes the predominant form of histone H3 in non-dividing cells and is incorporated into chromatin independently of DNA synthesis. Deposited at sites of nucleosomal displacement throughout transcribed genes, suggesting that it represents an epigenetic imprint of transcriptionally active chromatin. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.

      SUBUNIT STRUCTURE: The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. Interacts with HIRA, a chaperone required for its incorporation into nucleosomes.


      DEVELOPMENTAL STAGE: Expressed throughout the cell cycle independently of DNA synthesis.

      PTM: Acetylation is generally linked to gene activation. Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9 (H3R8sme2). Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18 (H3R17me).

      Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription.

      Asymmetric dimethylation at Arg-18 (H3R17me2a) by CARM1 is linked to gene activation. Symmetric dimethylation at Arg-9 (H3R8sme2) by PRMT5 is linked to gene repression. Asymmetric dimethylation at Arg-3 (H3R2me2a) by PRMT6 is linked to gene repression and is mutually exclusive with H3 Lys-5 methylation (H3K4me2 and H3K4me3). H3R2me2a is present at the 3' of genes regardless of their transcription state and is enriched on inactive promoters, while it is absent on active promoters.

      Specifically enriched in modifications associated with active chromatin such as methylation at Lys-5 (H3K4me), Lys-37 and Lys-80. Methylation at Lys-5 (H3K4me) facilitates subsequent acetylation of H3 and H4. Methylation at Lys-80 (H3K79me) is associated with DNA double-strand break (DSB) responses and is a specific target for TP53BP1. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me), which are linked to gene repression, are underrepresented. Methylation at Lys-10 (H3K9me) is a specific target for HP1 proteins (CBX1, CBX3 and CBX5) and prevents subsequent phosphorylation at Ser-11 (H3S10ph) and acetylation of H3 and H4. Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me) require preliminary monoubiquitination of H2B at 'Lys-120'. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are enriched in inactive X chromosome chromatin.

      Phosphorylated at Thr-4 (H3T3ph) by GSG2/haspin during prophase and dephosphorylated during anaphase. At centromeres, specifically phosphorylated at Thr-12 (H3T11ph) from prophase to early anaphase, probably DAPK3. Phosphorylation at Ser-11 (H3S10ph) by AURKB is crucial for chromosome condensation and cell-cycle progression during mitosis and meiosis. In addition phosphorylation at Ser-11 (H3S10ph) by RPS6KA4 and RPS6KA5 is important during interphase because it enables the transcription of genes following external stimulation, like mitogens, stress, growth factors or UV irradiation and result in the activation of genes, such as c-fos and c-jun. Phosphorylation at Ser-11 (H3S10ph), which is linked to gene activation, prevents methylation at Lys-10 (H3K9me) but facilitates acetylation of H3 and H4. Phosphorylation at Ser-11 (H3S10ph) by AURKB mediates the dissociation of HP1 proteins (CBX1, CBX3 and CBX5) from heterochromatin. Phosphorylation at Ser-11 (H3S10ph) is also an essential regulatory mechanism for neoplastic cell transformation. Phosphorylated at Ser-29 by MLTK isoform 1, RPS6KA5 or AURKB during mitosis or upon ultraviolet B irradiation. Phosphorylation on Ser-32 is specific to regions bordering centromeres in metaphase chromosomes.

      Ubiquitinated (By similarity).

      SEQUENCE SIMILARITIES: Belongs to the histone H3 family.

      SEQUENCE CAUTION: The sequence CAH73371.1 differs from that shown. Reason: Erroneous gene model prediction.
      Molecular Weight~17 kDa observed
      Physicochemical Information
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Quality AssuranceEvaluated by Western Blot in HeLa acid extract.

      Western Blot Analysis: 1 µg/mL of this antibody detected Histone H3.3 on 10 µg of HeLa acid extract.
      Usage Statement
      • Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
      Storage and Shipping Information
      Storage ConditionsStable for 1 year at 2-8°C from date of receipt.
      Packaging Information
      Material Size100 µg
      Transport Information
      Supplemental Information


      Anti-Histone H3.3 Antibody SDS


      Safety Data Sheet (SDS) 

      Anti-Histone H3.3 Antibody Certificates of Analysis

      TitleLot Number
      Anti-Histone H3.3 - 21460012146001
      Anti-Histone H3.3 - 23687772368777
      Anti-Histone H3.3 - 23958182395818
      Anti-Histone H3.3 - 24484272448427
      Anti-Histone H3.3 - 20069452006945
      Anti-Histone H3.3 - 20208732020873
      Anti-Histone H3.3 - 20336672033667
      Anti-Histone H3.3 - 20554722055472
      Anti-Histone H3.3 - 22025062202506
      Anti-Histone H3.3 - 22739842273984


      Reference overviewPub Med ID
      Suppression of the alternative lengthening of telomere pathway by the chromatin remodelling factor ATRX.
      Clynes, D; Jelinska, C; Xella, B; Ayyub, H; Scott, C; Mitson, M; Taylor, S; Higgs, DR; Gibbons, RJ
      Nature communications  6  7538  2015

      Show Abstract
      26143912 26143912
      Transcription-coupled recruitment of human CHD1 and CHD2 influences chromatin accessibility and histone H3 and H3.3 occupancy at active chromatin regions.
      Siggens, L; Cordeddu, L; Rönnerblad, M; Lennartsson, A; Ekwall, K
      Epigenetics & chromatin  8  4  2015

      Show Abstract
      25621013 25621013
      CHK1-driven histone H3.3 serine 31 phosphorylation is important for chromatin maintenance and cell survival in human ALT cancer cells.
      Chang, FT; Chan, FL; R McGhie, JD; Udugama, M; Mayne, L; Collas, P; Mann, JR; Wong, LH
      Nucleic acids research  43  2603-14  2015

      Show Abstract
      25690891 25690891
      The PML-associated protein DEK regulates the balance of H3.3 loading on chromatin and is important for telomere integrity.
      Ivanauskiene, K; Delbarre, E; McGhie, JD; Küntziger, T; Wong, LH; Collas, P
      Genome research  24  1584-94  2014

      Show Abstract
      25049225 25049225
      Viral reprogramming of the Daxx histone H3.3 chaperone during early Epstein-Barr virus infection.
      Tsai, K; Chan, L; Gibeault, R; Conn, K; Dheekollu, J; Domsic, J; Marmorstein, R; Schang, LM; Lieberman, PM
      Journal of virology  88  14350-63  2014

      Show Abstract
      25275136 25275136
      Histone H3.3 and its proteolytically processed form drive a cellular senescence programme.
      Duarte, LF; Young, AR; Wang, Z; Wu, HA; Panda, T; Kou, Y; Kapoor, A; Hasson, D; Mills, NR; Ma'ayan, A; Narita, M; Bernstein, E
      Nature communications  5  5210  2014

      Show Abstract
      25394905 25394905
      Hira-Dependent Histone H3.3 Deposition Facilitates PRC2 Recruitment at Developmental Loci in ES Cells.
      Banaszynski, Laura A, et al.
      Cell, 155: 107-20 (2013)  2013

      Show Abstract
      24074864 24074864
      The octamer is the major form of CENP-A nucleosomes at human centromeres.
      Hasson, D; Panchenko, T; Salimian, KJ; Salman, MU; Sekulic, N; Alonso, A; Warburton, PE; Black, BE
      Nature structural & molecular biology  20  687-95  2013

      Show Abstract
      23644596 23644596
      DAXX-dependent supply of soluble (H3.3-H4) dimers to PML bodies pending deposition into chromatin.
      Delbarre, E; Ivanauskiene, K; Küntziger, T; Collas, P
      Genome research  23  440-51  2013

      Show Abstract
      23222847 23222847
      Single cell analysis of RNA-mediated histone H3.3 recruitment to a cytomegalovirus promoter-regulated transcription site.
      Newhart, A; Rafalska-Metcalf, IU; Yang, T; Joo, LM; Powers, SL; Kossenkov, AV; Lopez-Jones, M; Singer, RH; Showe, LC; Skordalakes, E; Janicki, SM
      The Journal of biological chemistry  288  19882-99  2013

      Show Abstract
      23689370 23689370

      Technical Info

      White Paper - The Message in the Marks: Deciphering Cancer Epigenetics (EMD)

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