• Call +1.858.633.0165 or Fax +1.858.633.0166 or Contact Us

Histone Deacetylase 8 (HDAC8) Human Recombinant Protein

For Research Use Only. Not for use in diagnostic procedures. Catalog #: MBS1433640

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… More details

$330 / 0.02 mg (Yeast) +1 FREE 8GB USB
Product Documentation
PDF
Sample Manual Insert View PDF
PDF
Testing Data View PDF
PDF
Certificate of Analysis (COA) View PDF
PDF
QC Report View PDF
PDF
Material Safety Data Sheet View PDF
PDF
Technical Datasheet View PDF
PDF
Protocol View PDF

Product Overview

Online Datasheet in PDF
Product Name
Histone deacetylase 8 (HDAC8), Recombinant Protein
Full Product Name
Recombinant Human Histone deacetylase 8
Product Gene Name
Sequence
MEEPEEPADS GQSLVPVYIY SPEYVSMCDS LAKIPKRASM VHSLIEAYAL HKQMRIVKPK VASMEEMATF HTDAYLQHLQ KVSQEGDDDH PDSIEYGLGY DCPATEGIFD YAAAIGGATI TAAQCLIDGM CKVAINWSGG WHHAKKDEAS GFCYLNDAVL GILRLRRKFE RILYVDLDLH HGDGVEDAFS FTSKVMTVSL HKFSPGFFPG TGDVSDVGLG KGRYYSVNVP IQDGIQDEKY YQICESVLKE VYQAFNPKAV VLQLGADTIA GDPMCSFNMT PVGIGKCLKY ILQWQLATLI LGGGGYNLAN TARCWTYLTG VILGKTLSSE IPDHEFFTAY GPDYVLEITP SCRPDRNEPH RIQQILNYIK GNLKHVV
Host
E Coli or Yeast or Baculovirus or Mammalian Cell
Form/Format
Lyophilized or liquid (Format to be determined during the manufacturing process)
Purity/Purification
Greater or equal to 85% purity as determined by SDS-PAGE. (lot specific)
Preparation and Storage
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
Molecular Weight
57.8 kDa
Sequence Positions
1-377aa; Full Length
Tag Information
This protein contains an N-terminal tag and may also contain a C-terminal tag. Tag types are determined by various factors including tag-protein stability, please inquire for tag information.
Sterility
Sterile filter available upon request.
Endotoxin
Low endotoxin available upon request.
OMIM
300269
3D Structure
ModBase 3D Structure for Q9BY41

Product Categories/Family for HDAC8 recombinant protein

ISO Certification
Manufactured in an ISO 9001:2015 Certified Laboratory.

Product References and Citations for HDAC8 recombinant protein

Cloning and characterization of a novel human class I histone deacetylase that functions as a transcription repressor.Hu E., Chen Z., Fredrickson T., Zhu Y., Kirkpatrick R., Zhang G.-F., Johanson K., Sung C.-M., Liu R., Winkler J.J. Biol. Chem. 275:15254-15264(2000) Cloning and characterization of a novel human histone deacetylase, HDAC8.Buggy J.J., Sideris M.L., Mak P., Lorimer D.D., McIntosh B., Clark J.M.Biochem. J. 350:199-205(2000) Cloning and characterization of human histone deacetylase 8.Van den Wyngaert I., de Vries W., Kremer A., Neefs J.-M., Verhasselt P., Luyten W.H.M.L., Kass S.U.FEBS Lett. 478:77-83(2000) Characterization of a highly complex region in Xq13 and mapping of three isodicentric breakpoints associated with preleukemia.McDonell N., Ramser J., Francis F., Vinet M.-C., Rider S., Sudbrak R., Riesselman L., Yaspo M.-L., Reinhardt R., Monaco A.P., Ross F., Kahn A., Kearney L., Buckle V., Chelly J.Genomics 64:221-229(2000) Normalization and subtraction two approaches to facilitate gene discovery.Bonaldo M.F., Lennon G., Soares M.B.Genome Res. 6:791-806(1996) A novel gene expressed in human pheochromocytoma.Li Y., Huang Q., Peng Y., Song H., Yu Y., Xu S., Ren S., Chen Z., Han Z. Complete sequencing and characterization of 21,243 full-length human cDNAs.Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.Nat. Genet. 36:40-45(2004) 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) ETO, a target of t(8;21) in acute leukemia, makes distinct contacts with multiple histone deacetylases and binds mSin3A through its oligomerization domain.Amann J.M., Nip J., Strom D.K., Lutterbach B., Harada H., Lenny N., Downing J.R., Meyers S., Hiebert S.W.Mol. Cell. Biol. 21:6470-6483(2001) The inv(16) fusion protein associates with corepressors via a smooth muscle myosin heavy-chain domain.Durst K.L., Lutterbach B., Kummalue T., Friedman A.D., Hiebert S.W.Mol. Cell. Biol. 23:607-619(2003) Negative regulation of histone deacetylase 8 activity by cyclic AMP-dependent protein kinase A.Lee H., Rezai-Zadeh N., Seto E.Mol. Cell. Biol. 24:765-773(2004) Histone deacetylase HDAC8 associates with smooth muscle alpha-actin and is essential for smooth muscle cell contractility.Waltregny D., Glenisson W., Tran S.L., North B.J., Verdin E., Colige A., Castronovo V.FASEB J. 19:966-968(2005) Use of histone deacetylase 8 (HDAC8) , a new marker of smooth muscle differentiation, in the classification of mesenchymal tumors of the uterus.de Leval L., Waltregny D., Boniver J., Young R.H., Castronovo V., Oliva E.Am. J. Surg. Pathol. 30:319-327(2006) Histone deacetylase 8 safeguards the human ever-shorter telomeres 1B (hEST1B) protein from ubiquitin-mediated degradation.Lee H., Sengupta N., Villagra A., Rezai-Zadeh N., Seto E.Mol. Cell. Biol. 26:5259-5269(2006) X-exome sequencing identifies a HDAC8 variant in a large pedigree with X-linked intellectual disability, truncal obesity, gynaecomastia, hypogonadism and unusual face.Harakalova M., van den Boogaard M.J., Sinke R., van Lieshout S., van Tuil M.C., Duran K., Renkens I., Terhal P.A., de Kovel C., Nijman I.J., van Haelst M., Knoers N.V., van Haaften G., Kloosterman W., Hennekam R.C., Cuppen E., Ploos van Amstel H.K.J. Med. Genet. 49:539-543(2012) HDAC8 mutations in Cornelia de Lange syndrome affect the cohesin acetylation cycle.Deardorff M.A., Bando M., Nakato R., Watrin E., Itoh T., Minamino M., Saitoh K., Komata M., Katou Y., Clark D., Cole K.E., De Baere E., Decroos C., Di Donato N., Ernst S., Francey L.J., Gyftodimou Y., Hirashima K., Hullings M., Ishikawa Y., Jaulin C., Kaur M., Kiyono T., Lombardi P.M., Magnaghi-Jaulin L., Mortier G.R., Nozaki N., Petersen M.B., Seimiya H., Siu V.M., Suzuki Y., Takagaki K., Wilde J.J., Willems P.J., Prigent C., Gillessen-Kaesbach G., Christianson D.W., Kaiser F.J., Jackson L.G., Hirota T., Krantz I.D., Shirahige K.Nature 489:313-317(2012) Structural snapshots of human HDAC8 provide insights into the class I histone deacetylases.Somoza J.R., Skene R.J., Katz B.A., Mol C., Ho J.D., Jennings A.J., Luong C., Arvai A., Buggy J.J., Chi E., Tang J., Sang B.-C., Verner E., Wynands R., Leahy E.M., Dougan D.R., Snell G., Navre M., Knuth M.W., Swanson R.V., McRee D.E., Tari L.W.Structure 12:1325-1334(2004) Substrate binding to histone deacetylases as shown by the crystal structure of the HDAC8-substrate complex.Vannini A., Volpari C., Gallinari P., Jones P., Mattu M., Carfi A., De Francesco R., Steinkuehler C., Di Marco S.EMBO Rep. 8:879-884(2007) Structural studies of human histone deacetylase 8 and its site-specific variants complexed with substrate and inhibitors.Dowling D.P., Gantt S.L., Gattis S.G., Fierke C.A., Christianson D.W.Biochemistry 47:13554-13563(2008) +Additional computationally mapped references.<p>Provides general information on the entry.

Other Notes

Small volumes of HDAC8 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.

Searchable Terms for HDAC8 purchase

MBS1433640 is a recombinant protein targeting HDAC8. Also known as Recombinant Human Histone deacetylase 8. Host: E Coli or Yeast or Baculovirus or Mammalian Cell.

Additional Details

NCBI/Uniprot data below describe general gene information for HDAC8. It may not necessarily be applicable to this product.

NCBI GI #
NCBI GeneID
NCBI Accession #
UniProt Primary Accession #
UniProt Secondary Accession #
UniProt Related Accession #
GenBank Nucleotide #
NCBI Official Full Name
histone deacetylase 8 isoform 2
NCBI Official Synonym Full Names
histone deacetylase 8
NCBI Official Symbol
HDAC8
NCBI Official Synonym Symbols
HD8; WTS; RPD3; CDA07; CDLS5; MRXS6; HDACL1
UniProt Protein Name
Histone deacetylase 8
Protein Family
UniProt Gene Name
HDAC8
UniProt Synonym Gene Names
HDACL1; HD8
UniProt Entry Name
HDAC8_HUMAN
NCBI Protein Information
histone deacetylase 8

NCBI Summary for HDAC8

Histones play a critical role in transcriptional regulation, cell cycle progression, and developmental events. Histone acetylation/deacetylation alters chromosome structure and affects transcription factor access to DNA. The protein encoded by this gene belongs to class I of the histone deacetylase family. It catalyzes the deacetylation of lysine residues in the histone N-terminal tails and represses transcription in large multiprotein complexes with transcriptional co-repressors. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Oct 2009]
Show more

UniProt Comments for HDAC8

HDAC8: 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. May play a role in smooth muscle cell contractility. Belongs to the histone deacetylase family. HD type 1 subfamily. 5 isoforms of the human protein are produced by alternative splicing.

Protein type: Hydrolase; EC 3.5.1.98

Chromosomal Location of Human Ortholog: Xq13

Cellular Component: cytoplasm; cytosol; histone deacetylase complex; nuclear chromosome; nucleoplasm; nucleus; plasma membrane

Molecular Function: histone deacetylase activity; Hsp70 protein binding; Hsp90 protein binding; metal ion binding; NAD-dependent histone deacetylase activity (H3-K14 specific); protein binding; transcription factor binding

Biological Process: chromatin assembly or disassembly; chromatin modification; establishment and/or maintenance of chromatin architecture; mitotic cell cycle; negative regulation of protein ubiquitination; negative regulation of transcription from RNA polymerase II promoter; regulation of protein stability; regulation of telomere maintenance; sister chromatid cohesion; transcription, DNA-dependent

Disease: Wilson-turner X-linked Mental Retardation Syndrome
Show more

Precautions

All of MyBioSource's Products are for scientific laboratory research purposes and are not for diagnostic, therapeutics, prophylactic or in vivo use. Through your purchase, you expressly represent and warrant to MyBioSource that you will properly test and use any Products purchased from MyBioSource in accordance with industry standards. MyBioSource and its authorized distributors reserve the right to refuse to process any order where we reasonably believe that the intended use will fall outside of our acceptable guidelines.

Disclaimer

While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.

It is the responsibility of the customer to report product performance issues to MyBioSource within 30 days of receipt of the product. Please visit our Terms & Conditions page for more information.

Product Note

Select online data sheet information is drawn from bioinformatics databases, occasionally resulting in ambiguous or non-relevant product information. It is the responsibility of the customer to review, verify, and evaluate the information to make sure it matches their requirements before purchasing the kit. Our ELISA Kit assays are dynamic research tools and sometimes they may be updated and improved. If the format of this assay is important to you then please request the current manual or contact our technical support team with a presales inquiry before placing an order. We will confirm the current details of the assay. We cannot guarantee the sample manual posted online is the most current manual, it is intended to serve as an example only. Please refer to the instructions For Use provided with the assay kit for precise details.

Product PubMed Publications

Request a Quote

Please fill out the form below and our representative will get back to you shortly.

MBS000000
Contact Us

Please fill out the form below and our representative will get back to you shortly.

MBS000000