protein

Recombinant Human Alcohol dehydrogenase 1B

MBS952645

0.05 mg (E-Coli)

190 USD

Recombinant Protein

Recombinant Human Alcohol dehydrogenase 1B

Alcohol dehydrogenase 1B

Alcohol dehydrogenase subunit beta

alcohol dehydrogenase 1B isoform 1; Alcohol dehydrogenase 1B; alcohol dehydrogenase 1B; alcohol dehydrogenase 1B (class I), beta polypeptide; Alcohol dehydrogenase subunit beta

ADH1B

ADH1B; ADH1B; ADH2; HEL-S-117; ADH2

ADH1B_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

2-375

335

STAGKVIKCKAAVLWEVKKPFSIEDVEVAPPKAYEVRIK
MVAVGICRTDDHVVSGNLVTPLPVILGHEAAGIVESVGE
GVTTVKPGDKVIPLFTPQCGKCRVCKNPESNYCLKNDLG
NPRGTLQDGTRRFTCRGKPIHHFLGTSTFSQYTVVDENA
VAKIDAASPLEKVCLIGCGFSTGYGSAVNVAKVTPGSTC
AVFGLGGVGLSAVMGCKAAGAARIIAVDINKDKFAKAKE
LGATECINPQDYKKPIQEVLK

Greater than 90% as determined by SDS-PAGE.

Liquid containing glycerol; lyophilization may be available upon request.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Metabolism

Molecular cloning of a full-length cDNA for human alcohol dehydrogenase.Ikuta T., Fujiyoshi T., Kurachi K., Yoshida A.Proc. Natl. Acad. Sci. U.S.A. 82:2703-2707(1985) ErratumIkuta T., Fujiyoshi T., Kurachi K., Yoshida A.Proc. Natl. Acad. Sci. U.S.A. 82:5578-5578(1985) cDNA clones coding for the beta-subunit of human liver alcohol dehydrogenase have differently sized 3'-non-coding regions.Heden L.-O., Hoeoeg J.-O., Larsson K., Lake M., Lagerholm E., Holmgren A., Vallee B.L., Joernvall H., von Bahr-Lindstroem H.FEBS Lett. 194:327-332(1986) Molecular analysis of the human class I alcohol dehydrogenase gene family and nucleotide sequence of the gene encoding the beta subunit.Duester G., Smith M., Bilanchone V., Hatfield G.W.J. Biol. Chem. 261:2027-2033(1986) Three human alcohol dehydrogenase subunits cDNA structure and molecular and evolutionary divergence.Ikuta T., Szeto S., Yoshida A.Proc. Natl. Acad. Sci. U.S.A. 83:634-638(1986) Molecular characterization of cDNA clones encoding the human alcohol dehydrogenase beta 1 and the evolutionary relationship to the other class I subunits alpha and gamma.Yokoyama S., Yokoyama R., Rotwein P.Jpn. J. Genet. 62:241-256(1987) Nucleotide sequence of the ADH2(3) gene encoding the human alcohol dehydrogenase beta 3 subunit.Carr L.G., Xu Y., Ho W.H., Edenberg H.J.Alcohol. Clin. Exp. Res. 13:594-596(1989) The genes for human alcohol dehydrogenases beta 1 and beta 2 differ by only one nucleotide.Matsuo Y., Yokoyama R., Yokoyama S.Eur. J. Biochem. 183:317-320(1989) Polin L., Hey-Chi H. NIEHS SNPs programComplete 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) Generation and annotation of the DNA sequences of human chromosomes 2 and 4.Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.Nature 434:724-731(2005) Human liver alcohol dehydrogenase. 1. The primary structure of the beta 1 beta 1 isoenzyme.Hempel J., Buhler R., Kaiser R., Holmquist B., de Zalenski C., von Wartburg J.-P., Vallee B.L., Joernvall H.Eur. J. Biochem. 145:437-445(1984) Genotyping of human alcohol dehydrogenases at the ADH2 and ADH3 loci following DNA sequence amplification.Xu Y.L., Carr L.G., Bosron W.F., Li T.K., Edenberg H.J.Genomics 2:209-214(1988) Osier M., Speed W.C., Seaman M.I., Kidd K.K.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) Human liver alcohol dehydrogenase amino acid substitution in the beta 2 beta 2 Oriental isozyme explains functional properties, establishes an active site structure, and parallels mutational exchanges in the yeast enzyme.Joernvall H., Hempel J., Vallee B.L., Bosron W.F., Li T.-K.Proc. Natl. Acad. Sci. U.S.A. 81:3024-3028(1984) The human beta 3 alcohol dehydrogenase subunit differs from beta 1 by a Cys for Arg-369 substitution which decreases NAD(H) binding.Burnell J.C., Carr L.G., Dwulet F.E., Edenberg H.J., Li T.-K., Bosron W.F.Biochem. Biophys. Res. Commun. 146:1127-1133(1987) Structure of human beta 1 beta 1 alcohol dehydrogenase catalytic effects of non-active-site substitutions.Hurley T.D., Bosron W.F., Hamilton J.A., Amzel L.M.Proc. Natl. Acad. Sci. U.S.A. 88:8149-8153(1991) Structures of three human beta alcohol dehydrogenase variants. Correlations with their functional differences.Hurley T.D., Bosron W.F., Stone C.L., Amzel L.M.J. Mol. Biol. 239:415-429(1994) X-ray structure of human beta3beta3 alcohol dehydrogenase. The contribution of ionic interactions to coenzyme binding.Davis G.J., Bosron W.F., Stone C.L., Owusu-Dekyi K., Hurley T.D.J. Biol. Chem. 271:17057-17061(1996) Three-dimensional structures of the three human class I alcohol dehydrogenases.Niederhut M.S., Gibbons B.J., Perez-Miller S., Hurley T.D.Protein Sci. 10:697-706(2001) Genetic polymorphism of alcohol dehydrogenase in Europeans the ADH2*2 allele decreases the risk for alcoholism and is associated with ADH3*1.Borras E., Coutelle C., Rosell A., Fernandez-Muixi F., Broch M., Crosas B., Hjelmqvist L., Lorenzo A., Gutierrez C., Santos M., Szczepanek M., Heilig M., Quattrocchi P., Farres J., Vidal F., Richart C., Mach T., Bogdal J., Joernvall H., Seitz H.K., Couzigou P., Pares X.Hepatology 31:984-989(2000)

34577061

NP_000659.2

NM_000668.5

P00325

55.7kD

Biological Oxidations Pathway (1270189); Chemical Carcinogenesis Pathway (673221); Chemical Carcinogenesis Pathway (673237); Drug Metabolism - Cytochrome P450 Pathway (83032); Drug Metabolism - Cytochrome P450 Pathway (427); Ethanol Oxidation Pathway (1270206); Fatty Acid Omega Oxidation Pathway (198915); Fatty Acid Degradation Pathway (82935); Fatty Acid Degradation Pathway (296); Glycolysis / Gluconeogenesis Pathway (82926)

The protein encoded by this gene is a member of the alcohol dehydrogenase family. Members of this enzyme family metabolize a wide variety of substrates, including ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. This encoded protein, consisting of several homo- and heterodimers of alpha, beta, and gamma subunits, exhibits high activity for ethanol oxidation and plays a major role in ethanol catabolism. Three genes encoding alpha, beta and gamma subunits are tandemly organized in a genomic segment as a gene cluster. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Nov 2013]

0.05 mg (E-Coli)

190 USD

0.2 mg (E-Coli)

460

0.5 mg (E-Coli)

750

0.05 mg (Baculovirus)

1140

1 mg (E-Coli)

1180