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SDS-PAGE

Histone H3.3 Recombinant Protein | H3F3A recombinant protein

Recombinant Human Histone H3.3

Gene Names
H3F3A; H3F3; H3.3A
Purity
Greater or equal to 85% purity as determined by SDS-PAGE.
Synonyms
Histone H3.3; Recombinant Human Histone H3.3; H3F3A recombinant protein
Ordering
For Research Use Only!
Host
E Coli
Purity/Purification
Greater or equal to 85% purity as determined by SDS-PAGE.
Form/Format
Liquid containing glycerol
Sequence Positions
2-136aa; Full Length
Sequence
ARTKQTARKSTGGKAPRKQLATKAARKSAPSTGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSAAIGALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA
Sequence Length
136
Preparation and Storage
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

SDS-PAGE
Related Product Information for H3F3A recombinant protein
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 displacent 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.
Product Categories/Family for H3F3A recombinant protein
References
Structure of a human histone cDNA evidence that basally expressed histone genes have intervening sequences and encode polyadenylylated mRNAs.Wells D., Kedes L.Proc. Natl. Acad. Sci. U.S.A. 82:2834-2838(1985) Unusual structure, evolutionary conservation of non-coding sequences and numerous pseudogenes characterize the human H3.3 histone multigene family.Wells D., Hoffman D., Kedes L.Nucleic Acids Res. 15:2871-2889(1987) The human replacement histone H3.3B gene (H3F3B) .Albig W., Bramlage B., Gruber K., Klobeck H.-G., Kunz J., Doenecke D.Genomics 30:264-272(1995) Large-scale cDNA transfection screening for genes related to cancer development and progression.Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) The full-ORF clone resource of the German cDNA consortium.Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.BMC Genomics 8:399-399(2007) The DNA sequence and biological annotation of human chromosome 1.Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.Nature 441:315-321(2006) Human spleen histone H3. Isolation and amino acid sequence.Ohe Y., Iwai K.J. Biochem. 90:1205-1211(1981) Modifications of human histone H3 variants during mitosis.Garcia B.A., Barber C.M., Hake S.B., Ptak C., Turner F.B., Busby S.A., Shabanowitz J., Moran R.G., Allis C.D., Hunt D.F.Biochemistry 44:13202-13213(2005) Identification of a novel phosphorylation site on histone H3 coupled with mitotic chromosome condensation.Goto H., Tomono Y., Ajiro K., Kosako H., Fujita M., Sakurai M., Okawa K., Iwamatsu A., Okigaki T., Takahashi T., Inagaki M.J. Biol. Chem. 274:25543-25549(1999) Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins.Lachner M., O'Carroll D., Rea S., Mechtler K., Jenuwein T.Nature 410:116-120(2001) Aurora-B phosphorylates Histone H3 at serine28 with regard to the mitotic chromosome condensation.Goto H., Yasui Y., Nigg E.A., Inagaki M.Genes Cells 7:11-17(2002) Novel mitosis-specific phosphorylation of histone H3 at Thr11 mediated by Dlk/ZIP kinase.Preuss U., Landsberg G., Scheidtmann K.H.Nucleic Acids Res. 31:878-885(2003) Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways dependent or independent of DNA synthesis.Tagami H., Ray-Gallet D., Almouzni G., Nakatani Y.Cell 116:51-61(2004) Ligand-dependent activation of the farnesoid X-receptor directs arginine methylation of histone H3 by CARM1.Ananthanarayanan M., Li S., Balasubramaniyan N., Suchy F.J., Walsh M.J.J. Biol. Chem. 279:54348-54357(2004) Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks.Huyen Y., Zgheib O., Ditullio R.A. Jr., Gorgoulis V.G., Zacharatos P., Petty T.J., Sheston E.A., Mellert H.S., Stavridi E.S., Halazonetis T.D.Nature 432:406-411(2004) Human PAD4 regulates histone arginine methylation levels via demethylimination.Wang Y., Wysocka J., Sayegh J., Lee Y.-H., Perlin J.R., Leonelli L., Sonbuchner L.S., McDonald C.H., Cook R.G., Dou Y., Roeder R.G., Clarke S., Stallcup M.R., Allis C.D., Coonrod S.A.Science 306:279-283(2004) Variant histone H3.3 marks promoters of transcriptionally active genes during mammalian cell division.Chow C.-M., Georgiou A., Szutorisz H., Maia e Silva A., Pombo A., Barahona I., Dargelos E., Canzonetta C., Dillon N.EMBO Rep. 6:354-360(2005) The kinase haspin is required for mitotic histone H3 Thr 3 phosphorylation and normal metaphase chromosome alignment.Dai J., Sultan S., Taylor S.S., Higgins J.M.G.Genes Dev. 19:472-488(2005) Phosphorylation of Ser28 in histone H3 mediated by mixed lineage kinase-like mitogen-activated protein triple kinase alpha.Choi H.S., Choi B.Y., Cho Y.-Y., Zhu F., Bode A.M., Dong Z.J. Biol. Chem. 280:13545-13553(2005) Serine 31 phosphorylation of histone variant H3.3 is specific to regions bordering centromeres in metaphase chromosomes.Hake S.B., Garcia B.A., Kauer M., Baker S.P., Shabanowitz J., Hunt D.F., Allis C.D.Proc. Natl. Acad. Sci. U.S.A. 102:6344-6349(2005) Histone H3.3 deposition at E2F-regulated genes is linked to transcription.Daury L., Chailleux C., Bonvallet J., Trouche D.EMBO Rep. 7:66-71(2006) Expression patterns and post-translational modifications associated with mammalian histone H3 variants.Hake S.B., Garcia B.A., Duncan E.M., Kauer M., Dellaire G., Shabanowitz J., Bazett-Jones D.P., Allis C.D., Hunt D.F.J. Biol. Chem. 281:559-568(2006) Mass spectrometric characterization of human histone H3 a bird's eye view.Thomas C.E., Kelleher N.L., Mizzen C.A.J. Proteome Res. 5:240-247(2006) Coactivator-associated arginine methyltransferase-1 enhances nuclear factor-kappaB-mediated gene transcription through methylation of histone H3 at arginine 17.Miao F., Li S., Chavez V., Lanting L., Natarajan R.Mol. Endocrinol. 20:1562-1573(2006) PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylation.Hyllus D., Stein C., Schnabel K., Schiltz E., Imhof A., Dou Y., Hsieh J., Bauer U.M.Genes Dev. 21:3369-3380(2007) Structural basis for histone N-terminal recognition by human peptidylarginine deiminase 4.Arita K., Shimizu T., Hashimoto H., Hidaka Y., Yamada M., Sato M.Proc. Natl. Acad. Sci. U.S.A. 103:5291-5296(2006) Organismal differences in post-translational modifications in histones H3 and H4.Garcia B.A., Hake S.B., Diaz R.L., Kauer M., Morris S.A., Recht J., Shabanowitz J., Mishra N., Strahl B.D., Allis C.D., Hunt D.F.J. Biol. Chem. 282:7641-7655(2007) Identification of histone H3 lysine 36 acetylation as a highly conserved histone modification.Morris S.A., Rao B., Garcia B.A., Hake S.B., Diaz R.L., Shabanowitz J., Hunt D.F., Allis C.D., Lieb J.D., Strahl B.D.J. Biol. Chem. 282:7632-7640(2007) Methylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex are mutually exclusive.Guccione E., Bassi C., Casadio F., Martinato F., Cesaroni M., Schuchlautz H., Luescher B., Amati B.Nature 449:933-937(2007) Arginine methylation of the histone H3 tail impedes effector binding.Iberg A.N., Espejo A., Cheng D., Kim D., Michaud-Levesque J., Richard S., Bedford M.T.J. Biol. Chem. 283:3006-3010(2008) Phosphorylation of histone H3 at threonine 11 establishes a novel chromatin mark for transcriptional regulation.Metzger E., Yin N., Wissmann M., Kunowska N., Fischer K., Friedrichs N., Patnaik D., Higgins J.M., Potier N., Scheidtmann K.H., Buettner R., Schule R.Nat. Cell Biol. 10:53-60(2008) Acetylation of histone H3 at the nucleosome dyad alters DNA-histone binding.Manohar M., Mooney A.M., North J.A., Nakkula R.J., Picking J.W., Edon A., Fishel R., Poirier M.G., Ottesen J.J.J. Biol. Chem. 284:23312-23321(2009) JAK2 phosphorylates histone H3Y41 and excludes HP1alpha from chromatin.Dawson M.A., Bannister A.J., Gottgens B., Foster S.D., Bartke T., Green A.R., Kouzarides T.Nature 461:819-822(2009) Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.Sci. Signal. 2:RA46-RA46(2009) Lysine acetylation targets protein complexes and co-regulates major cellular functions.Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.Science 325:834-840(2009) Quantitative interaction proteomics and genome-wide profiling of epigenetic histone marks and their readers.Vermeulen M., Eberl H.C., Matarese F., Marks H., Denissov S., Butter F., Lee K.K., Olsen J.V., Hyman A.A., Stunnenberg H.G., Mann M.Cell 142:967-980(2010) Phosphorylation of histone H3T6 by PKCbeta(I) controls demethylation at histone H3K4.Metzger E., Imhof A., Patel D., Kahl P., Hoffmeyer K., Friedrichs N., Muller J.M., Greschik H., Kirfel J., Ji S., Kunowska N., Beisenherz-Huss C., Gunther T., Buettner R., Schule R.Nature 464:792-796(2010) Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification.Tan M., Luo H., Lee S., Jin F., Yang J.S., Montellier E., Buchou T., Cheng Z., Rousseaux S., Rajagopal N., Lu Z., Ye Z., Zhu Q., Wysocka J., Ye Y., Khochbin S., Ren B., Zhao Y.Cell 146:1016-1028(2011) Histone H3 lysine 56 methylation regulates DNA replication through its interaction with PCNA.Yu Y., Song C., Zhang Q., Dimaggio P.A., Garcia B.A., York A., Carey M.F., Grunstein M.Mol. Cell 46:7-17(2012) Lysyl oxidase-like 2 deaminates lysine 4 in histone H3.Herranz N., Dave N., Millanes-Romero A., Morey L., Diaz V.M., Lorenz-Fonfria V., Gutierrez-Gallego R., Jeronimo C., Di Croce L., Garcia de Herreros A., Peiro S.Mol. Cell 46:369-376(2012) Regulation of transcription through acetylation of H3K122 on the lateral surface of the histone octamer.Tropberger P., Pott S., Keller C., Kamieniarz-Gdula K., Caron M., Richter F., Li G., Mittler G., Liu E.T., Buhler M., Margueron R., Schneider R.Cell 152:859-872(2013) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014) ZMYND11 links histone H3.3K36me3 to transcription elongation and tumour suppression.Wen H., Li Y., Xi Y., Jiang S., Stratton S., Peng D., Tanaka K., Ren Y., Xia Z., Wu J., Li B., Barton M.C., Li W., Li H., Shi X.Nature 508:263-268(2014) +Additional computationally mapped references.<p>Provides general information on the entry.

NCBI and Uniprot Product Information

NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Accession #
Molecular Weight
42.6kD
NCBI Official Full Name
histone H3.3
NCBI Official Synonym Full Names
H3 histone, family 3A
NCBI Official Symbol
H3F3A
NCBI Official Synonym Symbols
H3F3; H3.3A
NCBI Protein Information
histone H3.3
UniProt Protein Name
Histone H3.3
Protein Family
UniProt Gene Name
H3F3A
UniProt Synonym Gene Names
H3.3A; H3F3
UniProt Entry Name
H33_HUMAN

NCBI Description

Histones 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 nucleosomes 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, Jul 2008]

Uniprot Description

H3F3A: 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. 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. Belongs to the histone H3 family.

Protein type: DNA-binding

Chromosomal Location of Human Ortholog: 1q42.12

Cellular Component: extracellular region; nuclear chromosome; nuclear chromosome, telomeric region; nucleoplasm; nucleosome; nucleus; protein complex

Molecular Function: histone binding; nucleosomal DNA binding; protein binding; protein heterodimerization activity

Biological Process: blood coagulation; brain development; cellular protein metabolic process; chromatin silencing at rDNA; DNA methylation on cytosine; DNA replication-independent nucleosome assembly; gene expression; negative regulation of gene expression, epigenetic; nucleosome assembly; positive regulation of cell growth; positive regulation of gene expression, epigenetic; regulation of gene expression, epigenetic; response to hormone stimulus; RNA-mediated gene silencing; small GTPase mediated signal transduction; telomere organization and biogenesis

Research Articles on H3F3A

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Product Notes

The H3F3A h3f3a (Catalog #AAA717134) is a Recombinant Protein produced from E Coli and is intended for research purposes only. The product is available for immediate purchase. The immunogen sequence is 2-136aa; Full Length. The amino acid sequence is listed below: ARTKQTARKS TGGKAPRKQL ATKAARKSAP STGGVKKPHR YRPGTVALRE IRRYQKSTEL LIRKLPFQRL VREIAQDFKT DLRFQSAAIG ALQEASEAYL VGLFEDTNLC AIHAKRVTIM PKDIQLARRI RGERA. It is sometimes possible for the material contained within the vial of "Histone H3.3, Recombinant Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.

Precautions

All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.

Disclaimer

Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.

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