All-trans-retinol dehydrogenase [NAD(+)] ADH1B (ADH1B) Recombinant Protein | ADH1B recombinant protein

Recombinant Human All-trans-retinol dehydrogenase [NAD(+)] ADH1B (ADH1B)

Cat. Num. AAA952645

• Gene Names: ADH1B; ADH2; HEL-S-117
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: All-trans-retinol dehydrogenase [NAD(+)] ADH1B (ADH1B); Recombinant Human All-trans-retinol dehydrogenase [NAD(+)] ADH1B (ADH1B); Alcohol dehydrogenase subunit beta; ADH1B recombinant protein

• 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: 2-375aa; Full Length of Mature Protein
• Sequence: STAGKVIKCKAAVLWEVKKPFSIEDVEVAPPKAYEVRIKMVAVGICRTDDHVVSGNLVTPLPVILGHEAAGIVESVGEGVTTVKPGDKVIPLFTPQCGKCRVCKNPESNYCLKNDLGNPRGTLQDGTRRFTCRGKPIHHFLGTSTFSQYTVVDENAVAKIDAASPLEKVCLIGCGFSTGYGSAVNVAKVTPGSTCAVFGLGGVGLSAVMGCKAAGAARIIAVDINKDKFAKAKELGATECINPQDYKKPIQEVLKEMTDGGVDFSFEVIGRLDTMMASLLCCHEACGTSVIVGVPPASQNLSINPMLLLTGRTWKGAVYGGFKSKEGIPKLVADFMAKKFSLDALITHVLPFEKINEGFDLLHSGKSIRTVLTF

• Production Note: Special Offer: The E Coli host-expressed protein is manufactured from a stock plasmid containing the protein gene. E Colihost-expressed protein is stocked in different unit sizes ranging from as small as 10 ug to as large as 1 mg. Bulk inventory is also available. The E Coli host-expressed protein has been ordered over and over again by researchers and has stood the test of time as both a robust protein and important target for the research community. It is part of our new program to make our most popular protein targets and corresponding hosts available in expanded unit sizes and with a quick processing time. Select E Coli host-expressed protein for the fastest delivery among all hosts. Please contact our technical support team or email to [email protected] for more details.
• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Product Categories/Family for ADH1B recombinant protein

Metabolism

References

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. 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NCBI and Uniprot Product Information

• NCBI GI #: 34577061
• NCBI GeneID: 125
• NCBI Accession #: NP_000659.2
• NCBI GenBank Nucleotide #: NM_000668.5
• UniProt Accession #: P00325; Q13711; Q4ZGI9; Q96KI7; A8MYN5; B4DRS9; B4DVC3
• Molecular Weight: 55.7 kDa
• NCBI Official Full Name: alcohol dehydrogenase 1B isoform 1
• NCBI Official Synonym Full Names: alcohol dehydrogenase 1B (class I), beta polypeptide
• NCBI Official Symbol: ADH1B
• NCBI Official Synonym Symbols: ADH2; HEL-S-117
• NCBI Protein Information: alcohol dehydrogenase 1B
• UniProt Protein Name: Alcohol dehydrogenase 1B
• UniProt Gene Name: ADH1B
• UniProt Synonym Gene Names: ADH2
• UniProt Entry Name: ADH1B_HUMAN

NCBI Description

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]

Uniprot Description

MiscellaneousThere are 7 different ADH's isozymes in human: three belongs to class-I: alpha, beta, and gamma, one to class-II: pi, one to class-III: chi, one to class-IV: ADH7 and one to class-V: ADH6.