Recombinant Human Epoxide hydrolase 1 | MyBioSource MBS955361 product information

product summary

company name :

MyBioSource

product type :

protein

product name :

Recombinant Human Epoxide hydrolase 1

catalog :

MBS955361

quantity :

0.05 mg (E-Coli)

price :

180 USD

more info or order :

MyBioSource product webpage

product information

catalog number :

MBS955361

products type :

Recombinant Protein

products full name :

Recombinant Human Epoxide hydrolase 1

products short name :

Epoxide hydrolase 1

products name syn :

Epoxide hydratase; Microsomal epoxide hydrolase

other names :

epoxide hydrolase 1; Epoxide hydrolase 1; epoxide hydrolase 1; epoxide hydrolase 1; Epoxide hydratase; Microsomal epoxide hydrolase

products gene name :

EPHX1

other gene names :

EPHX1; EPHX1; MEH; EPHX; EPOX; HYL1; EPHX; EPOX

uniprot entry name :

HYEP_HUMAN

host :

E Coli or Yeast or Baculovirus or Mammalian Cell

sequence positions :

1-455; Full length

sequence length :

455

sequence :

MWLEILLTSVLGFAIYWFISRDKEETLPLEDGWWGPGTR
SAAREDDSIRPFKVETSDEEIHDLHQRIDKFRFTPPLED
SCFHYGFNSNYLKKVISYWRNEFDWKKQVEILNRYPHFK
TKIEGLDIHFIHVKPPQLPAGHTPKPLLMVHGWPGSFYE
FYKIIPLLTDPKNHGLSDEHVFEVICPSIPGYGFSEASS
KKGFNSVATARIFYKLMLRLGFQEFYIQGGDWGSLICTN
MAQLVPSHVKGLHLNMALVLSNFSTLTLLLGQRFGRFLG
LTERDVELLYPVKEKVFYSLMRESGYMHIQCTKPDTVGS
ALNDSPVGLAAYILEKFSTWTNTEFRYLEDGGLERKFSL
DDLLTNVMLYWTTGTIISSQRFYKENLGQGWMTQKHERM
KVYVPTGFSAFPFELLHTPEKWVRFKYPKLISYSYMVRG
GHFAAFEEPELLAQDIRKFLSVLERQ

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 :

Biotransformation enzyme that catalyzes the hydrolysis of arene and aliphatic epoxides to less reactive and more water soluble dihydrodiols by the trans addition of water.

products references :

Human microsomal xenobiotic epoxide hydrolase. Complementary DNA sequence, complementary DNA-directed expression in COS-1 cells, and chromosomal localization.Skoda R.C., Demierre A., McBride O.W., Gonzalez F.J., Meyer U.A.J. Biol. Chem. 263:1549-1554(1988) Nucleotide sequence of a human microsomal epoxide hydrolase cDNA clone.Wilson N.M., Omiecinski C.J. Nucleotide and deduced amino acid sequence of human liver microsomal epoxide hydrolase.Jackson M.R., Craft J.A., Burchell B.Nucleic Acids Res. 15:7188-7188(1987) Human microsomal epoxide hydrolase genetic polymorphism and functional expression in vitro of amino acid variants.Hassett C., Aicher L., Sidhu J.S., Omiecinski C.J.Hum. Mol. Genet. 3:421-428(1994) ErratumHassett C., Aicher L., Sidhu J.S., Omiecinski C.J.Hum. Mol. Genet. 3:1214-1214(1994) The human microsomal epoxide hydrolase gene (EPHX1) complete nucleotide sequence and structural characterization.Hassett C., Robinson K.B., Beck N.B., Omiecinski C.J.Genomics 23:433-442(1994) 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) NIEHS SNPs programThe DNA sequence and biological annotation of human chromosome 1.Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.Nature 441:315-321(2006) Partial nucleotide sequence of a cloned cDNA for human liver microsomal epoxide hydrolase.Craft J.A., Jackson M.R., Burchell B.Biochem. Soc. Trans. 15:708-709(1987) Identification of 6 new polymorphisms, g.11177G>A, g.14622C>T (R49C) , g.17540T>C, g.17639T>C, g.30929T>C, g.31074G>A (R454Q) , in the human microsomal epoxide hydrolase gene (EPHX1) in a French population.Belmahdi F., Chevalier D., Lo-Guidice J.-M., Allorge D., Cauffiez C., Lafitte J.-J., Broly F.3.0.CO;2-1>Hum. Mutat. 16:450-450(2000) Inhibition of human m-epoxide hydrolase gene expression in a case of hypercholanemia.Zhu Q.S., Xing W., Qian B., von Dippe P., Shneider B.L., Fox V.L., Levy D.Biochim. Biophys. Acta 1638:208-216(2003) 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) 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) Two exonic single nucleotide polymorphisms in the microsomal epoxide hydrolase gene are jointly associated with preeclampsia.Laasanen J., Romppanen E.-L., Hiltunen M., Helisalmi S., Mannermaa A., Punnonen K., Heinonen S.Eur. J. Hum. Genet. 10:569-573(2002) Five novel single nucleotide polymorphisms in the EPHX1 gene encoding microsomal epoxide hydrolase.Shiseki K., Itoda M., Saito Y., Nakajima Y., Maekawa K., Kimura H., Goto Y., Saitoh O., Katoh M., Ohnuma T., Kawai M., Sugai K., Ohtsuki T., Suzuki C., Minami N., Ozawa S., Sawada J.Drug Metab. Pharmacokinet. 18:150-153(2003) Functional analysis of human microsomal epoxide hydrolase genetic variants.Hosagrahara V.P., Rettie A.E., Hassett C., Omiecinski C.J.Chem. Biol. Interact. 150:149-159(2004)

ncbi gi num :

4503583

ncbi acc num :

NP_000111.1

ncbi gb acc num :

NM_000120.3

uniprot acc num :

P07099

ncbi mol weight :

68.9kD

ncbi pathways :

Aflatoxin B1 Metabolism Pathway (198808); Benzo(a)pyrene Metabolism Pathway (198911); Bile Secretion Pathway (193146); Bile Secretion Pathway (193095); Biological Oxidations Pathway (1270189); Chemical Carcinogenesis Pathway (673221); Chemical Carcinogenesis Pathway (673237); Metabolism Pathway (1269956); Metabolism Of Xenobiotics By Cytochrome P450 Pathway (83031); Metabolism Of Xenobiotics By Cytochrome P450 Pathway (425)

ncbi summary :

Epoxide hydrolase is a critical biotransformation enzyme that converts epoxides from the degradation of aromatic compounds to trans-dihydrodiols which can be conjugated and excreted from the body. Epoxide hydrolase functions in both the activation and detoxification of epoxides. Mutations in this gene cause preeclampsia, epoxide hydrolase deficiency or increased epoxide hydrolase activity. Alternatively spliced transcript variants encoding the same protein have been found for this gene.[provided by RefSeq, Dec 2008]

uniprot summary :

Ephx1: Biotransformation enzyme that catalyzes the hydrolysis of arene and aliphatic epoxides to less reactive and more water soluble dihydrodiols by the trans addition of water. In some populations, the high activity haplotype tyr113/his139 is overrepresented among women suffering from pregnancy-induced hypertension (pre-eclampsia) when compared with healthy controls. Defects in EPHX1 are a cause of familial hypercholanemia (FHCA). FHCA is a disorder characterized by elevated serum bile acid concentrations, itching, and fat malabsorption. Belongs to the peptidase S33 family. Protein type: Hydrolase; Membrane protein, integral; Xenobiotic Metabolism - metabolism by cytochrome P450; EC 3.3.2.9. Chromosomal Location of Human Ortholog: 1q42.1. Cellular Component: endoplasmic reticulum membrane; integral to membrane. Molecular Function: cis-stilbene-oxide hydrolase activity; epoxide hydrolase activity. Biological Process: aromatic compound catabolic process; response to organic cyclic substance; response to toxin; xenobiotic metabolic process. Disease: Hypercholanemia, Familial; Preeclampsia/eclampsia 1

size1 :

0.05 mg (E-Coli)

price1 :

180 USD

size2 :

0.2 mg (E-Coli)

price2 :

490

size3 :

0.5 mg (E-Coli)

price3 :

715

size4 :

1 mg (E-Coli)

price4 :

1170

size5 :

0.05 mg (Mammalian-Cell)

price5 :

1170

more info or order :

MyBioSource product webpage