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company name :
MyBioSource
product type :
protein
product name :
Recombinant Human UDP-glucuronosyltransferase 1-1
catalog :
MBS965441
quantity :
0.05 mg (Yeast)
price :
190 USD
more info or order :
product information
catalog number :
MBS965441
products type :
Recombinant Protein
products full name :
Recombinant Human UDP-glucuronosyltransferase 1-1
products short name :
UDP-glucuronosyltransferase 1-1
products name syn :
Bilirubin-specific UDPGT isozyme 1; hUG-BR1; UDP-glucuronosyltransferase 1-A; UGT-1A; UGT1A; UDP-glucuronosyltransferase 1A1
other names :
UDP-glucuronosyltransferase 1-1; UDP-glucuronosyltransferase 1-1; UDP-glucuronosyltransferase 1-1; UDP glucuronosyltransferase 1 family, polypeptide A1; Bilirubin-specific UDPGT isozyme 1; hUG-BR1; UDP-glucuronosyltransferase 1-A; UGT-1A; UGT1A; UDP-glucuronosyltransferase 1A1
products gene name :
UGT1A1
other gene names :
UGT1A1; UGT1A1; GNT1; UGT1; UDPGT; UGT1A; HUG-BR1; BILIQTL1; UDPGT 1-1; GNT1; UGT1; UDPGT 1-1; UGT1*1; UGT1-01; UGT1.1; hUG-BR1; UGT-1A; UGT1A
uniprot entry name :
UD11_HUMAN
host :
E Coli or Yeast or Baculovirus or Mammalian Cell
sequence positions :
26-533, The mature full length of Isoform 1.
sequence length :
533
sequence :
HAGKILLIPVDGSHWLSMLGAIQQLQQRGHEIVVLAPDA
SLYIRDGAFYTLKTYPVPFQREDVKESFVSLGHNVFEND
SFLQRVIKTYKKIKKDSAMLLSGCSHLLHNKELMASLAE
SSFDVMLTDPFLPCSPIVAQYLSLPTVFFLHALPCSLEF
EATQCPNPFSYVPRPLSSHSDHMTFLQRVKNMLIAFSQN
FLCDVVYSPYATLASEFLQREVTVQDLLSSASVWLFRSD
FVKDYPRPIMPNMVFVGGINCLHQNPLSQEFEAYINASG
EHGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRY
TGTRPSNLANNTILVKWLPQNDLLGHPMTRAFITHAGSH
GVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNV
LEMTSEDLENALKAVINDKSYKENIMRLSSLHKDRPVEP
LDLAVFWVEFVMRHKGAPHLRPAAHDLTWYQYHSLDVIG
FLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKT
H
purity :
Greater than 90% as determined by SDS-PAGE.
form :
Liquid containing glycerol; lyophilization may be available upon request.
storage stability :
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
products categories :
Metabolism
products description :
UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isoform glucuronidates bilirubin IX-alpha to form both the IX-alpha-C8 and IX-alpha-C12 monoconjugates and diconjugate. Is also able to catalyze the glucuronidation of 17beta-estradiol, 17alpha-ethinylestradiol, 1-hydroxypyrene, 4-methylumbelliferone, 1-naphthol, paranitrophenol, scopoletin, and umbelliferone. Isoform 2 lacks transferase activity but acts as a negative regulator of isoform 1.
products references :
Cloning of two human liver bilirubin UDP-glucuronosyltransferase cDNAs with expression in COS-1 cells.Ritter J.K., Crawford J.M., Owens I.S.J. Biol. Chem. 266:1043-1047(1991) A novel complex locus UGT1 encodes human bilirubin, phenol, and other UDP-glucuronosyltransferase isozymes with identical carboxyl termini.Ritter J.K., Chen F., Sheen Y.Y., Tran H.M., Kimura S., Yeatman M.T., Owens I.S.J. Biol. Chem. 267:3257-3261(1992) Thirteen UDP-glucuronosyltransferase genes are encoded at the human UGT1 gene complex locus.Gong Q.H., Cho J.W., Huang T., Potter C., Gholami N., Basu N.K., Kubota S., Carvalho S., Pennington M.W., Owens I.S., Popescu N.C.Pharmacogenetics 11:357-368(2001) Guillemette C., Levesque E., Girard H., Bernard O.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) Analysis of the promoter of human bilirubin UDP-glucuronosyltransferase gene (UGT1*1) in relevance to Gilbert's syndrome.Ueyama H., Koiwai O., Soeda Y., Sato H., Satoh Y., Ohkubo I., Doida Y.Hepatol. Res. 9:152-163(1997) A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins.Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.Mol. Biol. Cell 13:4456-4469(2002) Regulation of the UGT1A1 bilirubin-conjugating pathway role of a new splicing event at the UGT1A locus.Levesque E., Girard H., Journault K., Lepine J., Guillemette C.Hepatology 45:128-138(2007) Influence of mutations associated with Gilbert and Crigler-Najjar type II syndromes on the glucuronidation kinetics of bilirubin and other UDP-glucuronosyltransferase 1A substrates.Udomuksorn W., Elliot D.J., Lewis B.C., Mackenzie P.I., Yoovathaworn K., Miners J.O.Pharmacogenet. Genomics 17:1017-1029(2007) Genetic diversity at the UGT1 locus is amplified by a novel 3' alternative splicing mechanism leading to nine additional UGT1A proteins that act as regulators of glucuronidation activity.Girard H., Levesque E., Bellemare J., Journault K., Caillier B., Guillemette C.Pharmacogenet. Genomics 17:1077-1089(2007) Structure and concentration changes affect characterization of UGT isoform-specific metabolism of isoflavones.Tang L., Singh R., Liu Z., Hu M.Mol. Pharm. 6:1466-1482(2009) Crigler-Najjar syndrome in The Netherlands identification of four novel UGT1A1 alleles, genotype-phenotype correlation, and functional analysis of 10 missense mutants.Sneitz N., Bakker C.T., de Knegt R.J., Halley D.J., Finel M., Bosma P.J.Hum. Mutat. 31:52-59(2010) Genome-wide association meta-analysis for total serum bilirubin levels.Johnson A.D., Kavousi M., Smith A.V., Chen M.H., Dehghan A., Aspelund T., Lin J.P., van Duijn C.M., Harris T.B., Cupples L.A., Uitterlinden A.G., Launer L., Hofman A., Rivadeneira F., Stricker B., Yang Q., O'Donnell C.J., Gudnason V., Witteman J.C.Hum. Mol. Genet. 18:2700-2710(2009) Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.J. Proteome Res. 8:651-661(2009) Alternatively spliced products of the UGT1A gene interact with the enzymatically active proteins to inhibit glucuronosyltransferase activity in vitro.Bellemare J., Rouleau M., Girard H., Harvey M., Guillemette C.Drug Metab. Dispos. 38:1785-1789(2010) 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) Mechanisms of inherited deficiencies of multiple UDP-glucuronosyltransferase isoforms in two patients with Crigler-Najjar syndrome, type I.Bosma P.J., Chowdhury J.R., Huang T.-J., Lahiri P., Elferink R.P.J.O., van Es H.H.G., Lederstein M., Whitington P.F., Jansen P.L.M., Chowdhury N.R.FASEB J. 6:2859-2863(1992) Identification of defect in the genes for bilirubin UDP-glucuronosyl-transferase in a patient with Crigler-Najjar syndrome type II.Aono S., Yamada Y., Keino H., Hanada N., Nakagawa T., Sasaoka Y., Yazawa T., Sato H., Koiwai O.Biochem. Biophys. Res. Commun. 197:1239-1244(1993) Identification of an A-to-G missense mutation in exon 2 of the UGT1 gene complex that causes Crigler-Najjar syndrome type 2.Moghrabi N., Clarke D.J., Boxer M., Burchell B.Genomics 18:171-173(1993) A phenylalanine codon deletion at the UGT1 gene complex locus of a Crigler-Najjar type I patient generates a pH-sensitive bilirubin UDP-glucuronosyltransferase.Ritter J.K., Yeatman M.T., Kaiser C., Gridelli B., Owens I.S.J. Biol. Chem. 268:23573-23579(1993) Genetic heterogeneity of Crigler-Najjar syndrome type I a study of 14 cases.Labrune P., Myara A., Hadchouel M., Ronchi F., Bernard O., Trivin F., Roy Chowdhury N., Roy Chowdhury J., Munnich A., Odievre M.Hum. Genet. 94:693-697(1994) Identification of two single base substitutions in the UGT1 gene locus which abolish bilirubin uridine diphosphate glucuronosyltransferase activity in vitro.Erps L.T., Ritter J.K., Hersh J.H., Blossom D., Martin N.C., Owens I.S.J. Clin. Invest. 93:564-570(1994) Discrimination between Crigler-Najjar type I and II by expression of mutant bilirubin uridine diphosphate-glucuronosyltransferase.Seppen J., Bosma P.J., Goldhoorn B.G., Bakker C.T.M., Roy Chowdhury J., Roy Chowdhury N., Jansen P.L.M., Oude Elferink R.P.J.J. Clin. Invest. 94:2385-2391(1994) Analysis of genes for bilirubin UDP-glucuronosyltransferase in Gilbert's syndrome.Aono S., Adachi Y., Uyama E., Yamada Y., Keino H., Nanno T., Koiwai O., Sato H.Lancet 345:958-959(1995) A mutation which disrupts the hydrophobic core of the signal peptide of bilirubin UDP-glucuronosyltransferase, an endoplasmic reticulum membrane protein, causes Crigler-Najjar type II.Seppen J., Steenken E., Lindhout D., Bosma P.J., Oude Elferink R.P.J.FEBS Lett. 390:294-298(1996) Coding defect and a TATA box mutation at the bilirubin UDP-glucuronosyltransferase gene cause Crigler-Najjar type I disease.Ciotti M., Chen F., Rubaltelli F.F., Owens I.S.Biochim. Biophys. Acta 1407:40-50(1998) Analysis of bilirubin uridine 5'-diphosphate (UDP) -glucuronosyltransferase gene mutations in seven patients with Crigler-Najjar syndrome type II.Yamamoto K., Soeda Y., Kamisako T., Hosaka H., Fukano M., Sato H., Fujiyama Y., Dachi Y., Satoh Y., Bamba T.J. Hum. Genet. 43:111-114(1998) Gilbert syndrome caused by a homozygous missense mutation (Tyr486Asp) of bilirubin UDP-glucuronosyltransferase gene.Maruo Y., Sato H., Yamano T., Doida Y., Shimada M.J. Pediatr. 132:1045-1047(1998) Genetic lesions of bilirubin uridine-diphosphoglucuronate glucuronosyltransferase (UGT1A1) causing Crigler-Najjar and Gilbert syndromes correlation of genotype to phenotype.Kadakol A., Ghosh S.S., Sappal B.S., Sharma G., Chowdhury J.R., Chowdhury N.R.3.0.CO;2-Z>Hum. Mutat. 16:297-306(2000) Prolonged unconjugated hyperbilirubinemia associated with breast milk and mutations of the bilirubin uridine diphosphate-glucuronosyltransferase gene.Maruo Y., Nishizawa K., Sato H., Sawa H., Shimada M.Pediatrics 106:E59-E59(2000) Interaction of coding region mutations and the Gilbert-type promoter abnormality of the UGT1A1 gene causes moderate degrees of unconjugated hyperbilirubinaemia and may lead to neonatal kernicterus.Kadakol A., Sappal B.S., Ghosh S.S., Lowenheim M., Chowdhury A., Chowdhury S., Santra A., Arias I.M., Chowdhury J.R., Chowdhury N.R.J. Med. Genet. 38:244-249(2001) Association of a homozygous (TA) 8 promoter polymorphism and a N400D mutation of UGT1A1 in a child with Crigler-Najjar type II syndrome.Labrune P., Myara A., Chalas J., Le Bihan B., Capel L., Francoual J.Hum. Mutat. 20:399-401(2002) Novel missense mutation of the UGT1A1 gene in Thai siblings with Gilbert's syndrome.Sutomo R., Laosombat V., Sadewa A.H., Yokoyama N., Nakamura H., Matsuo M., Nishio H.Pediatr. Int. 44:427-432(2002) Rapid proteasomal degradation of translocation-deficient UDP-glucuronosyltransferase 1A1 proteins in patients with Crigler-Najjar type II.Ohnishi A., Emi Y.Biochem. Biophys. Res. Commun. 310:735-741(2003) Spectrum of UGT1A1 mutations in Crigler-Najjar (CN) syndrome patients identification of twelve novel alleles and genotype-phenotype correlation.Servedio V., d'Apolito M., Maiorano N., Minuti B., Torricelli F., Ronchi F., Zancan L., Perrotta S., Vajro P., Boschetto L., Iolascon A.Hum. Mutat. 25:325-325(2005) Seven novel mutations of the UGT1A1 gene in patients with unconjugated hyperbilirubinemia.D'Apolito M., Marrone A., Servedio V., Vajro P., De Falco L., Iolascon A.Haematologica 92:133-134(2007) UGT1A1 gene mutations in Pakistani children suffering from inherited nonhemolytic unconjugated hyperbilirubinemias.Khan S., Irfan M., Sher G., Zubaida B., Alvi M.A., Yasinzai M., Naeem M.Ann. Hum. Genet. 77:482-487(2013) Identification of a novel mutation in UDP-glucuronosyltransferase (UGT1A1) gene in a child with neonatal unconjugated hyperbilirubinemia.Minucci A., Canu G., Gentile L., Cimino V., Giardina B., Zuppi C., Capoluongo E.Clin. Biochem. 46:170-172(2013) +Additional computationally mapped references. p>Provides general information on the entry.
ncbi gi num :
8850236
ncbi acc num :
NP_000454.1
ncbi gb acc num :
NM_000463.2
uniprot acc num :
P22309
ncbi mol weight :
59.1kD
ncbi pathways :
AhR Pathway (755436); Ascorbate And Aldarate Metabolism Pathway (82932); Ascorbate And Aldarate Metabolism Pathway (293); Biological Oxidations Pathway (1270189); Chemical Carcinogenesis Pathway (673221); Chemical Carcinogenesis Pathway (673237); Codeine And Morphine Metabolism Pathway (198831); Drug Metabolism - Cytochrome P450 Pathway (83032); Drug Metabolism - Cytochrome P450 Pathway (427); Drug Metabolism - Other Enzymes Pathway (83033)
ncbi summary :
This gene encodes a UDP-glucuronosyltransferase, an enzyme of the glucuronidation pathway that transforms small lipophilic molecules, such as steroids, bilirubin, hormones, and drugs, into water-soluble, excretable metabolites. This gene is part of a complex locus that encodes several UDP-glucuronosyltransferases. The locus includes thirteen unique alternate first exons followed by four common exons. Four of the alternate first exons are considered pseudogenes. Each of the remaining nine 5' exons may be spliced to the four common exons, resulting in nine proteins with different N-termini and identical C-termini. Each first exon encodes the substrate binding site, and is regulated by its own promoter. The preferred substrate of this enzyme is bilirubin, although it also has moderate activity with simple phenols, flavones, and C18 steroids. Mutations in this gene result in Crigler-Najjar syndromes types I and II and in Gilbert syndrome. [provided by RefSeq, Jul 2008]
uniprot summary :
UGT1A1: UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isoform glucuronidates bilirubin IX- alpha to form both the IX-alpha-C8 and IX-alpha-C12 monoconjugates and diconjugate. Is also able to catalyze the glucuronidation of 17beta-estradiol, 17alpha-ethinylestradiol, 1-hydroxypyrene, 4- methylumbelliferone, 1-naphthol, paranitrophenol, scopoletin, and umbelliferone. Part a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX. Expressed in liver. Not expressed in skin or kidney. Belongs to the UDP-glycosyltransferase family. 1 isoforms of the human protein are produced by alternative splicing. Protein type: EC 2.4.1.17; Xenobiotic Metabolism - drug metabolism - cytochrome P450; Cofactor and Vitamin Metabolism - porphyrin and chlorophyll; Carbohydrate Metabolism - pentose and glucuronate interconversions; Carbohydrate Metabolism - ascorbate and aldarate; Transferase; Lipid Metabolism - androgen and estrogen; Cofactor and Vitamin Metabolism - retinol; Xenobiotic Metabolism - metabolism by cytochrome P450; Carbohydrate Metabolism - starch and sucrose; Xenobiotic Metabolism - drug metabolism - other enzymes; Membrane protein, integral. Chromosomal Location of Human Ortholog: 2q37. Cellular Component: endoplasmic reticulum; endoplasmic reticulum membrane; integral to plasma membrane. Molecular Function: enzyme binding; enzyme inhibitor activity; glucuronosyltransferase activity; protein heterodimerization activity; protein homodimerization activity; retinoic acid binding; steroid binding. Biological Process: acute-phase response; bilirubin conjugation; digestion; drug metabolic process; estrogen metabolic process; flavone metabolic process; flavonoid biosynthetic process; heme catabolic process; heterocycle metabolic process; liver development; negative regulation of catalytic activity; negative regulation of fatty acid metabolic process; negative regulation of steroid metabolic process; organ regeneration; porphyrin metabolic process; response to drug; response to lipopolysaccharide; response to nutrient; response to starvation; retinoic acid metabolic process; steroid metabolic process; xenobiotic metabolic process. Disease: Bilirubin, Serum Level Of, Quantitative Trait Locus 1; Crigler-najjar Syndrome, Type I; Crigler-najjar Syndrome, Type Ii; Gilbert Syndrome; Hyperbilirubinemia, Transient Familial Neonatal
size1 :
0.05 mg (Yeast)
price1 :
190 USD
size2 :
0.05 mg (E-Coli)
price2 :
305
size3 :
0.2 mg (Yeast)
price3 :
460
size4 :
0.2 mg (E-Coli)
price4 :
580
size5 :
0.5 mg (Yeast)
price5 :
750
more info or order :
company information
MyBioSource
P.O. Box 153308
San Diego, CA 92195-3308
sales@mybiosource.com
https://www.mybiosource.com
1-888-627-0165
headquarters: USA
MyBioSource, LLC was orginally founded in Vancouver by three enthusiastic scientists who are passionate about providing the world with the best reagents available. Together, they form a company with a big vision known as MyBioSource. MyBioSource is now located in San Diego, California, USA.

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