{"product_id":"recombinant-human-histone-deacetylase-8-hdac8","title":"Recombinant Human Histone deacetylase 8 (HDAC8)","description":"\u003cp\u003e\u003cb\u003eSize\u003c\/b\u003e: 100ug. Other sizes are also available. \u003c\/p\u003e\u003cp\u003e\u003cb\u003eActivity\u003c\/b\u003e: Not tested\u003c\/p\u003e\u003cp\u003e\u003cb\u003eResearch Areas\u003c\/b\u003e: Transcription\u003c\/p\u003e\u003cp\u003e\u003cb\u003eUniprot ID\u003c\/b\u003e: Q9BY41\u003c\/p\u003e\u003cp\u003e\u003cb\u003eGene Names\u003c\/b\u003e: HDAC8\u003c\/p\u003e\u003cp\u003e\u003cb\u003eAlternative Name(s)\u003c\/b\u003e: CDA07; CDLS5; HD 8; HD8; HDAC 8; Hdac8; HDAC8_HUMAN; HDACL 1; HDACL1; Histone deacetylase 8; Histone deacetylase like 1 ; MRXS6; RPD 3; RPD3; WTS\u003c\/p\u003e\u003cp\u003e\u003cb\u003eAbbreviation\u003c\/b\u003e: Recombinant Human HDAC8 protein\u003c\/p\u003e\u003cp\u003e\u003cb\u003eOrganism\u003c\/b\u003e: Homo sapiens (Human)\u003c\/p\u003e\u003cp\u003e\u003cb\u003eSource\u003c\/b\u003e: E.coli\u003c\/p\u003e\u003cp\u003e\u003cb\u003eExpression Region\u003c\/b\u003e: 1-377aa\u003c\/p\u003e\u003cp\u003e\u003cb\u003eProtein Length\u003c\/b\u003e: Full Length\u003c\/p\u003e\u003cp\u003e\u003cb\u003eTag  Info\u003c\/b\u003e: N-terminal 6xHis-SUMO-tagged\u003c\/p\u003e\u003cp\u003e\u003cb\u003eTarget Protein Sequence\u003c\/b\u003e: MEEPEEPADSGQSLVPVYIYSPEYVSMCDSLAKIPKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDDHPDSIEYGLGYDCPATEGIFDYAAAIGGATITAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFERILYVDLDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQWQLATLILGGGGYNLANTARCWTYLTGVILGKTLSSEIPDHEFFTAYGPDYVLEITPSCRPDRNEPHRIQQILNYIKGNLKHVV\u003c\/p\u003e\u003cp\u003e\u003cb\u003eMW\u003c\/b\u003e: 57.7 kDa\u003c\/p\u003e\u003cp\u003e\u003cb\u003ePurity\u003c\/b\u003e: Greater than 90% as determined by SDS-PAGE.\u003c\/p\u003e\u003cp\u003e\u003cb\u003eEndotoxin\u003c\/b\u003e: Not test\u003c\/p\u003e\u003cp\u003e\u003cb\u003eBiological_Activity\u003c\/b\u003e: \u003c\/p\u003e\u003cp\u003e\u003cb\u003eForm\u003c\/b\u003e: Liquid or Lyophilized powder\u003c\/p\u003e\u003cp\u003e\u003cb\u003eBuffer\u003c\/b\u003e: If the delivery form is liquid, the default storage buffer is Tris\/PBS-based buffer, 5%-50% glycerol.\nIf the delivery form is lyophilized powder, the buffer before lyophilization is Tris\/PBS-based buffer, 6% Trehalose, pH 8.0.\u003c\/p\u003e\u003cp\u003e\u003cb\u003eReconstitution\u003c\/b\u003e: We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg\/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃\/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.\u003c\/p\u003e\u003cp\u003e\u003cb\u003eStorage\u003c\/b\u003e: The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. \nGenerally, the shelf life of liquid form is 6 months at -20℃\/-80℃. The shelf life of lyophilized form is 12 months at -20℃\/-80℃.\u003c\/p\u003e\u003cp\u003e\u003cb\u003eNotes\u003c\/b\u003e: Repeated freezing and thawing is not recommended. Store working aliquots at 4℃ for up to one week.\u003c\/p\u003e\u003cp\u003e\u003cb\u003eRelevance\u003c\/b\u003e: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Also involved in the deacetylation of cohesin complex protein SMC3 regulating release of cohesin complexes from chromatin. May play a role in smooth muscle cell contractility.\u003c\/p\u003e\u003cp\u003e\u003cb\u003eReference\u003c\/b\u003e: The DNA sequence of the human X chromosome.Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.  , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.Nature 434: 325-337(2005)\u003c\/p\u003e\u003cp\u003e\u003cb\u003eFunction\u003c\/b\u003e: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Also involved in the deacetylation of cohesin complex protein SMC3 regulating release of cohesin complexes from chromatin. May play a role in smooth muscle cell contractility.\u003c\/p\u003e","brand":"GeneBio Systems","offers":[{"title":"Default Title","offer_id":47751738753124,"sku":"Q9BY41","price":90400.0,"currency_code":"JPY","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0558\/8588\/9636\/files\/no_image_default_image-jpeg_23745e65-b477-43c6-b5ce-55590cd6bfb8.jpg?v=1769108855","url":"https:\/\/www.genebiosystems.com\/en-jp\/products\/recombinant-human-histone-deacetylase-8-hdac8","provider":"GeneBio ","version":"1.0","type":"link"}