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SDS-PAGE

Histone deacetylase 1 Recombinant Protein | HDAC1 recombinant protein

Recombinant Human Histone deacetylase 1

Gene Names
HDAC1; HD1; RPD3; GON-10; RPD3L1
Purity
Greater or equal to 85% purity as determined by SDS-PAGE.
Synonyms
Histone deacetylase 1; Recombinant Human Histone deacetylase 1; HDAC1 recombinant protein
Ordering
For Research Use Only!
Host
E Coli or Yeast or Baculovirus or Mammalian Cell
Purity/Purification
Greater or equal to 85% purity as determined by SDS-PAGE.
Form/Format
Lyophilized or liquid (Format to be determined during the manufacturing process)
Sequence Positions
1-482aa; Full Length
Sequence
MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA
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 HDAC1 recombinant protein
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. Deacetylates SP proteins, SP1 and SP3, and regulates their function. Component of the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST-mediated transcription in resting neurons. Upon calcium stimulation, HDAC1 is released from the complex and CREBBP is recruited, which facilitates transcriptional activation. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Deacetylates 'Lys-310' in RELA and thereby inhibits the transcriptional activity of NF-kappa-B. Deacetylates NR1D2 and abrogates the effect of KAT5-mediated relieving of NR1D2 transcription repression activity. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. Involved in CIART-mediated transcriptional repression of the circadian transcriptional activator: CLOCK-ARNTL/BMAL1 heterodimer. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex or CRY1 through histone deacetylation
Product Categories/Family for HDAC1 recombinant protein
References
A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p.Taunton J., Hassig C.A., Schreiber S.L.Science 272:408-411(1996) Isolation and mapping of a human gene (RPD3L1) that is homologous to RPD3, a transcription factor in Saccharomyces cerevisiae.Furukawa Y., Kawakami T., Sudo K., Inazawa J., Matsumine A., Akiyama T., Nakamura Y.Cytogenet. Cell Genet. 73:130-133(1996) MEF-2 function is modified by a novel co-repressor, MITR.Sparrow D.B., Miska E.A., Langley E., Reynaud-Deonauth S., Kotecha S., Towers N., Spohr G., Kouzarides T., Mohun T.J.EMBO J. 18:5085-5098(1999) BCoR, a novel corepressor involved in BCL-6 repression.Huynh K.D., Fischle W., Verdin E., Bardwell V.J.Genes Dev. 14:1810-1823(2000) HDAC1, a histone deacetylase, forms a complex with Hus1 and Rad9, two G2/M checkpoint Rad proteins.Cai R.L., Yan-Neale Y., Cueto M.A., Xu H., Cohen D.J. Biol. Chem. 275:27909-27916(2000) Receptor-interacting protein 140 directly recruits histone deacetylases for gene silencing.Wei L.-N., Hu X., Chandra D., Seto E., Farooqui M.J. Biol. Chem. 275:40782-40787(2000) Sequestration and inhibition of Daxx-mediated transcriptional repression by PML.Li H., Leo C., Zhu J., Wu X., O'Neil J., Park E.-J., Chen J.D.Mol. Cell. Biol. 20:1784-1796(2000) Identification of a transcriptional repressor related to the noncatalytic domain of histone deacetylases 4 and 5.Zhou X., Richon V.M., Rifkind R.A., Marks P.A.Proc. Natl. Acad. Sci. U.S.A. 97:1056-1061(2000) Histone deacetylase 1 phosphorylation promotes enzymatic activity and complex formation.Pflum M.K.H., Tong J.K., Lane W.S., Schreiber S.L.J. Biol. Chem. 276:47733-47741(2001) Sharp, an inducible cofactor that integrates nuclear receptor repression and activation.Shi Y., Downes M., Xie W., Kao H.-Y., Ordentlich P., Tsai C.-C., Hon M., Evans R.M.Genes Dev. 15:1140-1151(2001) Stable histone deacetylase complexes distinguished by the presence of SANT domain proteins CoREST/kiaa0071 and Mta-L1.Humphrey G.W., Wang Y., Russanova V.R., Hirai T., Qin J., Nakatani Y., Howard B.H.J. Biol. Chem. 276:6817-6824(2001) TGIF2 interacts with histone deacetylase 1 and represses transcription.Melhuish T.A., Gallo C.M., Wotton D.J. Biol. Chem. 276:32109-32114(2001) 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 SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase.Kirsh O., Seeler J.-S., Pichler A., Gast A., Mueller S., Miska E., Mathieu M., Harel-Bellan A., Kouzarides T., Melchior F., Dejean A.EMBO J. 21:2682-2691(2002) SUMO-1 modification of histone deacetylase 1 (HDAC1) modulates its biological activities.David G., Neptune M.A., DePinho R.A.J. Biol. Chem. 277:23658-23663(2002) Role of acetylated human AP-endonuclease (APE1/Ref-1) in regulation of the parathyroid hormone gene.Bhakat K.K., Izumi T., Yang S.H., Hazra T.K., Mitra S.EMBO J. 22:6299-6309(2003) Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1.Wysocka J., Myers M.P., Laherty C.D., Eisenman R.N., Herr W.Genes Dev. 17:896-911(2003) A candidate X-linked mental retardation gene is a component of a new family of histone deacetylase-containing complexes.Hakimi M.-A., Dong Y., Lane W.S., Speicher D.W., Shiekhattar R.J. Biol. Chem. 278:7234-7239(2003) Acetylated SP3 is a transcriptional activator.Ammanamanchi S., Freeman J.W., Brattain M.G.J. Biol. Chem. 278:35775-35780(2003) Human MI-ER1 alpha and beta function as transcriptional repressors by recruitment of histone deacetylase 1 to their conserved ELM2 domain.Ding Z., Gillespie L.L., Paterno G.D.Mol. Cell. Biol. 23:250-258(2003) Identification and characterization of three new components of the mSin3A corepressor complex.Fleischer T.C., Yun U.J., Ayer D.E.Mol. Cell. Biol. 23:3456-3467(2003) Modulation of p120E4F transcriptional activity by the Gam1 adenoviral early protein.Colombo R., Draetta G.F., Chiocca S.Oncogene 22:2541-2547(2003) Identification of a novel BRMS1-homologue protein p40 as a component of the mSin3A/p33(ING1b) /HDAC1 deacetylase complex.Nikolaev A.Y., Papanikolaou N.A., Li M., Qin J., Gu W.Biochem. Biophys. Res. Commun. 323:1216-1222(2004) MTA3 and the Mi-2/NuRD complex regulate cell fate during B lymphocyte differentiation.Fujita N., Jaye D.L., Geigerman C., Akyildiz A., Mooney M.R., Boss J.M., Wade P.A.Cell 119:75-86(2004) Site-specific acetylation of the fetal globin activator NF-E4 prevents its ubiquitination and regulates its interaction with the histone deacetylase, HDAC1.Zhao Q., Cumming H., Cerruti L., Cunningham J.M., Jane S.M.J. Biol. Chem. 279:41477-41486(2004) SENP1 enhances androgen receptor-dependent transcription through desumoylation of histone deacetylase 1.Cheng J., Wang D., Wang Z., Yeh E.T.H.Mol. Cell. Biol. 24:6021-6028(2004) ICBP90, an E2F-1 target, recruits HDAC1 and binds to methyl-CpG through its SRA domain.Unoki M., Nishidate T., Nakamura Y.Oncogene 23:7601-7610(2004) NuRD and SIN3 histone deacetylase complexes in development.Ahringer J.Trends Genet. 16:351-356(2000) Functional characterization of JMJD2A, a histone deacetylase- and retinoblastoma-binding protein.Gray S.G., Iglesias A.H., Lizcano F., Villanueva R., Camelo S., Jingu H., Teh B.T., Koibuchi N., Chin W.W., Kokkotou E., Dangond F.J. Biol. Chem. 280:28507-28518(2005) Tumor suppressor SMAR1 mediates cyclin D1 repression by recruitment of the SIN3/histone deacetylase 1 complex.Rampalli S., Pavithra L., Bhatt A., Kundu T.K., Chattopadhyay S.Mol. Cell. Biol. 25:8415-8429(2005) INSM1 functions as a transcriptional repressor of the neuroD/beta2 gene through the recruitment of cyclin D1 and histone deacetylases.Liu W.D., Wang H.W., Muguira M., Breslin M.B., Lan M.S.Biochem. J. 397:169-177(2006) Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.Cell 127:635-648(2006) Sp1 deacetylation induced by phorbol ester recruits p300 to activate 12(S) -lipoxygenase gene transcription.Hung J.J., Wang Y.T., Chang W.C.Mol. Cell. Biol. 26:1770-1785(2006) Breast cancer metastasis suppressor 1 functions as a corepressor by enhancing histone deacetylase 1-mediated deacetylation of RelA/p65 and promoting apoptosis.Liu Y., Smith P.W., Jones D.R.Mol. Cell. Biol. 26:8683-8696(2006) SAP30L interacts with members of the Sin3A corepressor complex and targets Sin3A to the nucleolus.Viiri K.M., Korkeamaeki H., Kukkonen M.K., Nieminen L.K., Lindfors K., Peterson P., Maeki M., Kainulainen H., Lohi O.Nucleic Acids Res. 34:3288-3298(2006) Toward a global characterization of the phosphoproteome in prostate cancer cells identification of phosphoproteins in the LNCaP cell line.Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.Electrophoresis 28:2027-2034(2007) Mechanisms of ceramide-mediated repression of the human telomerase reverse transcriptase promoter via deacetylation of Sp3 by histone deacetylase 1.Wooten-Blanks L.G., Song P., Senkal C.E., Ogretmen B.FASEB J. 21:3386-3397(2007) Breast cancer associated transcriptional repressor PLU-1/JARID1B interacts directly with histone deacetylases.Barrett A., Santangelo S., Tan K., Catchpole S., Roberts K., Spencer-Dene B., Hall D., Scibetta A., Burchell J., Verdin E., Freemont P., Taylor-Papadimitriou J.Int. J. Cancer 121:265-275(2007) Regulation of E2F1 function by the nuclear corepressor KAP1.Wang C., Rauscher F.J. III, Cress W.D., Chen J.J. Biol. Chem. 282:29902-29909(2007) Critical and functional regulation of CHOP (C/EBP homologous protein) through the N-terminal portion.Ohoka N., Hattori T., Kitagawa M., Onozaki K., Hayashi H.J. Biol. Chem. 282:35687-35694(2007) Involvement of chromatin and histone deacetylation in SV40 T antigen transcription regulation.Valls E., Blanco-Garcia N., Aquizu N., Piedra D., Estaras C., de la Cruz X., Martinez-Balbas M.A.Nucleic Acids Res. 35:1958-1968(2007) SUMO modification of the DEAD box protein p68 modulates its transcriptional activity and promotes its interaction with HDAC1.Jacobs A.M., Nicol S.M., Hislop R.G., Jaffray E.G., Hay R.T., Fuller-Pace F.V.Oncogene 26:5866-5876(2007) The orphan nuclear receptor Rev-erbbeta recruits Tip60 and HDAC1 to regulate apolipoprotein CIII promoter.Wang J., Liu N., Liu Z., Li Y., Song C., Yuan H., Li Y.Y., Zhao X., Lu H.Biochim. Biophys. Acta 1783:224-236(2008) Nuclear tumor necrosis factor receptor-associated factor 6 in lymphoid cells negatively regulates c-Myb-mediated transactivation through small ubiquitin-related modifier-1 modification.Pham L.V., Zhou H.J., Lin-Lee Y.C., Tamayo A.T., Yoshimura L.C., Fu L., Darnay B.G., Ford R.J.J. Biol. Chem. 283:5081-5089(2008) Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.Mol. Cell 31:438-448(2008) CDYL bridges REST and histone methyltransferases for gene repression and suppression of cellular transformation.Mulligan P., Westbrook T.F., Ottinger M., Pavlova N., Chang B., Macia E., Shi Y.J., Barretina J., Liu J., Howley P.M., Elledge S.J., Shi Y.Mol. Cell 32:718-726(2008) Protein lysine methyltransferase G9a acts on non-histone targets.Rathert P., Dhayalan A., Murakami M., Zhang X., Tamas R., Jurkowska R., Komatsu Y., Shinkai Y., Cheng X., Jeltsch A.Nat. Chem. Biol. 4:344-346(2008) A calcium-dependent switch in a CREST-BRG1 complex regulates activity-dependent gene expression.Qiu Z., Ghosh A.Neuron 60:775-787(2008) A quantitative atlas of mitotic phosphorylation.Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography.Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.Proteomics 8:1346-1361(2008) Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.Anal. Chem. 81:4493-4501(2009) SKI and MEL1 cooperate to inhibit transforming growth factor-beta signal in gastric cancer cells.Takahata M., Inoue Y., Tsuda H., Imoto I., Koinuma D., Hayashi M., Ichikura T., Yamori T., Nagasaki K., Yoshida M., Matsuoka M., Morishita K., Yuki K., Hanyu A., Miyazawa K., Inazawa J., Miyazono K., Imamura T.J. Biol. Chem. 284:3334-3344(2009) FE65 binds Teashirt, inhibiting expression of the primate-specific caspase-4.Kajiwara Y., Akram A., Katsel P., Haroutunian V., Schmeidler J., Beecham G., Haines J.L., Pericak-Vance M.A., Buxbaum J.D.PLoS ONE 4:E5071-E5071(2009) Chfr is linked to tumour metastasis through the downregulation of HDAC1.Oh Y.M., Kwon Y.E., Kim J.M., Bae S.J., Lee B.K., Yoo S.J., Chung C.H., Deshaies R.J., Seol J.H.Nat. Cell Biol. 11:295-302(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) Histone deacetylase and Cullin3-REN(KCTD11) ubiquitin ligase interplay regulates Hedgehog signalling through Gli acetylation.Canettieri G., Di Marcotullio L., Greco A., Coni S., Antonucci L., Infante P., Pietrosanti L., De Smaele E., Ferretti E., Miele E., Pelloni M., De Simone G., Pedone E.M., Gallinari P., Giorgi A., Steinkuhler C., Vitagliano L., Pedone C. , Schinin M.E., Screpanti I., Gulino A.Nat. Cell Biol. 12:132-142(2010) Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.Sci. Signal. 3:RA3-RA3(2010) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011) Maintenance of silent chromatin through replication requires SWI/SNF-like chromatin remodeler SMARCAD1.Rowbotham S.P., Barki L., Neves-Costa A., Santos F., Dean W., Hawkes N., Choudhary P., Will W.R., Webster J., Oxley D., Green C.M., Varga-Weisz P., Mermoud J.E.Mol. Cell 42:285-296(2011) SUMOylation of DEC1 protein regulates its transcriptional activity and enhances its stability.Hong Y., Xing X., Li S., Bi H., Yang C., Zhao F., Liu Y., Ao X., Chang A.K., Wu H.PLoS ONE 6:E23046-E23046(2011) System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.Sci. Signal. 4:RS3-RS3(2011) 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) Structural and functional characterization of a cell cycle associated HDAC1/2 complex reveals the structural basis for complex assembly and nucleosome targeting.Itoh T., Fairall L., Muskett F.W., Milano C.P., Watson P.J., Arnaudo N., Saleh A., Millard C.J., El-Mezgueldi M., Martino F., Schwabe J.W.Nucleic Acids Res. 43:2033-2044(2015) +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
71.1 kDa
NCBI Official Full Name
histone deacetylase 1
NCBI Official Synonym Full Names
histone deacetylase 1
NCBI Official Symbol
HDAC1
NCBI Official Synonym Symbols
HD1; RPD3; GON-10; RPD3L1
NCBI Protein Information
histone deacetylase 1
UniProt Protein Name
Histone deacetylase 1
Protein Family
UniProt Gene Name
HDAC1
UniProt Synonym Gene Names
RPD3L1; HD1
UniProt Entry Name
HDAC1_HUMAN

NCBI Description

Histone acetylation and deacetylation, catalyzed by multisubunit complexes, play a key role in the regulation of eukaryotic gene expression. The protein encoded by this gene belongs to the histone deacetylase/acuc/apha family and is a component of the histone deacetylase complex. It also interacts with retinoblastoma tumor-suppressor protein and this complex is a key element in the control of cell proliferation and differentiation. Together with metastasis-associated protein-2, it deacetylates p53 and modulates its effect on cell growth and apoptosis. [provided by RefSeq, Jul 2008]

Uniprot Description

HDAC1: a transcriptional regulator of the histone deacetylase family, subfamily 1. Deacetylates lysine residues on the N-terminal part of the core histones H2A, H2B, H3 AND H4. Plays an important role in transcriptional regulation, cell cycle progression and developmental events.

Protein type: Hydrolase; EC 3.5.1.98; Nuclear receptor co-regulator

Chromosomal Location of Human Ortholog: 1p34

Cellular Component: chromatin; cytoplasm; cytosol; histone deacetylase complex; nuclear chromatin; nucleoplasm; nucleus; NuRD complex; protein complex; Sin3 complex

Molecular Function: deacetylase activity; enzyme binding; histone deacetylase activity; histone deacetylase binding; NAD-dependent histone deacetylase activity (H3-K14 specific); NF-kappaB binding; nucleosomal DNA binding; protein binding; protein deacetylase activity; protein N-terminus binding; transcription activator binding; transcription factor activity; transcription factor binding

Biological Process: ATP-dependent chromatin remodeling; blood coagulation; chromatin modification; chromatin remodeling; circadian regulation of gene expression; embryonic digit morphogenesis; epidermal cell differentiation; establishment and/or maintenance of chromatin architecture; gene expression; histone deacetylation; mitotic cell cycle; negative regulation of apoptosis; negative regulation of cell cycle; negative regulation of gene expression, epigenetic; negative regulation of transcription from RNA polymerase II promoter; negative regulation of transcription, DNA-dependent; nerve growth factor receptor signaling pathway; Notch signaling pathway; odontogenesis of dentine-containing teeth; positive regulation of cell proliferation; positive regulation of transcription from RNA polymerase II promoter; positive regulation of transcription, DNA-dependent; protein amino acid deacetylation; regulation of gene expression, epigenetic; transcription initiation from RNA polymerase II promoter; transcription, DNA-dependent; transforming growth factor beta receptor signaling pathway; viral reproduction

Research Articles on HDAC1

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Product Notes

The HDAC1 hdac1 (Catalog #AAA1426580) is a Recombinant Protein produced from E Coli or Yeast or Baculovirus or Mammalian Cell and is intended for research purposes only. The product is available for immediate purchase. The immunogen sequence is 1-482aa; Full Length. The amino acid sequence is listed below: MAQTQGTRRK VCYYYDGDVG NYYYGQGHPM KPHRIRMTHN LLLNYGLYRK MEIYRPHKAN AEEMTKYHSD DYIKFLRSIR PDNMSEYSKQ MQRFNVGEDC PVFDGLFEFC QLSTGGSVAS AVKLNKQQTD IAVNWAGGLH HAKKSEASGF CYVNDIVLAI LELLKYHQRV LYIDIDIHHG DGVEEAFYTT DRVMTVSFHK YGEYFPGTGD LRDIGAGKGK YYAVNYPLRD GIDDESYEAI FKPVMSKVME MFQPSAVVLQ CGSDSLSGDR LGCFNLTIKG HAKCVEFVKS FNLPMLMLGG GGYTIRNVAR CWTYETAVAL DTEIPNELPY NDYFEYFGPD FKLHISPSNM TNQNTNEYLE KIKQRLFENL RMLPHAPGVQ MQAIPEDAIP EESGDEDEDD PDKRISICSS DKRIACEEEF SDSEEEGEGG RKNSSNFKKA KRVKTEDEKE KDPEEKKEVT EEEKTKEEKP EAKGVKEEVK LA . It is sometimes possible for the material contained within the vial of "Histone deacetylase 1, 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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