Histone H2A Type 1 (HIST1H2AG) Human Recombinant Protein

Core component of nucleosome. 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 human histone gene cluster at the D6S105 locus.Albig W., Doenecke D.Hum. Genet. 101:284-294(1997) The human H2A and H2B histone gene complement.Albig W., Trappe R., Kardalinou E., Eick S., Doenecke D.Biol. Chem. 380:7-18(1999) A novel divergently transcribed human histone H2A/H2B gene pair.Dobner T., Wolf I., Mai B., Lipp M.DNA Seq. 1:409-413(1991) The relative expression of human histone H2A genes is similar in different types of proliferating cells.Mannironi C., Orr A., Hatch C., Pilch D., Ivanova V., Bonner W.DNA Cell Biol. 13:161-170(1994) The human and mouse replication-dependent histone genes.Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.Genomics 80:487-498(2002) The DNA sequence and analysis of human chromosome 6.Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.Nature 425:805-811(2003) Human spleen histone H2A. Isolation and four variant sequences.Hayashi T., Ohe Y., Hayashi H., Iwai K.J. Biochem. 88:27-34(1980) Global regulation of post-translational modifications on core histones.Galasinski S.C., Louie D.F., Gloor K.K., Resing K.A., Ahn N.G.J. Biol. Chem. 277:2579-2588(2002) Nucleosomal histone kinase-1 phosphorylates H2A Thr 119 during mitosis in the early Drosophila embryo.Aihara H., Nakagawa T., Yasui K., Ohta T., Hirose S., Dhomae N., Takio K., Kaneko M., Takeshima Y., Muramatsu M., Ito T.Genes Dev. 18:877-888(2004) Phosphorylation of histone H2A inhibits transcription on chromatin templates.Zhang Y., Griffin K., Mondal N., Parvin J.D.J. Biol. Chem. 279:21866-21872(2004) Role of histone H2A ubiquitination in Polycomb silencing.Wang H., Wang L., Erdjument-Bromage H., Vidal M., Tempst P., Jones R.S., Zhang Y.Nature 431:873-878(2004) Deimination of histone H2A and H4 at arginine 3 in HL-60 granulocytes.Hagiwara T., Hidaka Y., Yamada M.Biochemistry 44:5827-5834(2005) Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing.Cao R., Tsukada Y., Zhang Y.Mol. Cell 20:845-854(2005) DNA damage triggers nucleotide excision repair-dependent monoubiquitylation of histone H2A.Bergink S., Salomons F.A., Hoogstraten D., Groothuis T.A.M., de Waard H., Wu J., Yuan L., Citterio E., Houtsmuller A.B., Neefjes J., Hoeijmakers J.H.J., Vermeulen W., Dantuma N.P.Genes Dev. 20:1343-1352(2006) Precise characterization of human histones in the H2A gene family by top down mass spectrometry.Boyne M.T. II, Pesavento J.J., Mizzen C.A., Kelleher N.L.J. Proteome Res. 5:248-253(2006) RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteins.Mailand N., Bekker-Jensen S., Faustrup H., Melander F., Bartek J., Lukas C., Lukas J.Cell 131:887-900(2007) RNF8 transduces the DNA-damage signal via histone ubiquitylation and checkpoint protein assembly.Huen M.S.Y., Grant R., Manke I., Minn K., Yu X., Yaffe M.B., Chen J.Cell 131:901-914(2007) The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling cascade at sites of DNA damage.Stewart G.S., Panier S., Townsend K., Al-Hakim A.K., Kolas N.K., Miller E.S., Nakada S., Ylanko J., Olivarius S., Mendez M., Oldreive C., Wildenhain J., Tagliaferro A., Pelletier L., Taubenheim N., Durandy A., Byrd P.J., Stankovic T., Taylor A.M.R., Durocher D.Cell 136:420-434(2009) RNF168 binds and amplifies ubiquitin conjugates on damaged chromosomes to allow accumulation of repair proteins.Doil C., Mailand N., Bekker-Jensen S., Menard P., Larsen D.H., Pepperkok R., Ellenberg J., Panier S., Durocher D., Bartek J., Lukas J., Lukas C.Cell 136:435-446(2009) 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) RNF168 ubiquitinates K13-15 on H2A/H2AX to drive DNA Damage signaling.Mattiroli F., Vissers J.H., van Dijk W.J., Ikpa P., Citterio E., Vermeulen W., Marteijn J.A., Sixma T.K.Cell 150:1182-1195(2012) A novel ubiquitin mark at the N-terminal tail of histone H2As targeted by RNF168 ubiquitin ligase.Gatti M., Pinato S., Maspero E., Soffientini P., Polo S., Penengo L.Cell Cycle 11:2538-2544(2012) VprBP has intrinsic kinase activity targeting histone H2A and represses gene transcription.Kim K., Kim J.M., Kim J.S., Choi J., Lee Y.S., Neamati N., Song J.S., Heo K., An W.Mol. Cell 52:459-467(2013) Glutamine methylation in histone H2A is an RNA-polymerase-I-dedicated modification.Tessarz P., Santos-Rosa H., Robson S.C., Sylvestersen K.B., Nelson C.J., Nielsen M.L., Kouzarides T.Nature 505:564-568(2014) TRIM37 is a new histone H2A ubiquitin ligase and breast cancer oncoprotein.Bhatnagar S., Gazin C., Chamberlain L., Ou J., Zhu X., Tushir J.S., Virbasius C.M., Lin L., Zhu L.J., Wajapeyee N., Green M.R.Nature 516:116-120(2014)

Small volumes of HIST1H2AG recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

MBS947929 is a recombinant protein targeting HIST1H2AG. Also known as Recombinant Human Histone H2A type 1. Host: E Coli or Yeast or Baculovirus or Mammalian Cell.