Lycopene beta cyclase, chloroplastic Recombinant Protein | LCY1 recombinant protein

Recombinant Arabidopsis thaliana Lycopene beta cyclase, chloroplastic

Cat. Num. AAA1325054

• Gene Names: LYC; LYCOPENE BETA-CYCLASE; lycopene cyclase
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Lycopene beta cyclase; chloroplastic; Recombinant Arabidopsis thaliana Lycopene beta cyclase; LCY1 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: 81-501aa; Full Length
• Sequence: QVVDLAIVGGGPAGLAVAQQVSEAGLSVCSIDPSPKLIWPNNYGVWVDEFEAMDLLDCLDTTWSGAVVYVDEGVKKDLSRPYGRVNRKQLKSKMLQKCITNGVKFHQSKVTNVVHEEANSTVVCSDGVKIQASVVLDATGFSRCLVQYDKPYNPGYQVAYGIVAEVDGHPFDVDKMVFMDWRDKHLDSYPELKERNSKIPTFLYAMPFSSNRIFLEETSLVARPGLRMEDIQERMAARLKHLGINVKRIEEDERCVIPMGGPLPVLPQRVVGIGGTAGMVHPSTGYMVARTLAAAPIVANAIVRYLGSPSSNSLRGDQLSAEVWRDLWPIERRRQREFFCFGMDILLKLDLDATRRFFDAFFDLQPHYWHGFLSSRLFLPELLVFGLSLFSHASNTSRLEIMTKGTVPLAKMINNLVQDRD
• Sequence Length: 369

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for LCY1 recombinant protein

Catalyzes the double cyclization reaction which converts lycopene to beta-carotene and neurosporene to beta-zeacarotene.

References

Functional analysis of the beta and epsilon lycopene cyclase enzymes of Arabidopsis reveals a mechanism for control of cyclic carotenoid formation.Cunningham F.X. Jr., Pogson B., Sun Z., McDonald K.A., Dellapenna D., Gantt E.Plant Cell 8:1613-1626(1996) Gene structure and regulation of the carotenoid biosynthesis pathway in Arabidopsis thaliana.Giuliano G., Rosati C., Santangelo G.Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.Nature 408:820-822(2000) Empirical analysis of transcriptional activity in the Arabidopsis genome.Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.Science 302:842-846(2003)

NCBI and Uniprot Product Information

• NCBI GI #: 145332018
• NCBI GeneID: 820185
• NCBI Accession #: NP_001078131.1
• NCBI GenBank Nucleotide #: NM_001084662.1
• UniProt Accession #: Q38933; Q39145; A8MR53
• Molecular Weight: 49.1 kDa
• NCBI Official Full Name: lycopene beta cyclase
• NCBI Official Symbol: LYC
• NCBI Official Synonym Symbols: LYCOPENE BETA-CYCLASE; lycopene cyclase
• NCBI Protein Information: lycopene beta cyclase
• UniProt Protein Name: Lycopene beta cyclase, chloroplastic
• UniProt Gene Name: LCY1
• UniProt Synonym Gene Names: LYC
• UniProt Entry Name: LCYB_ARATH

NCBI Description

Encodes a protein with lycopene β-cyclase activity. This enzyme uses the linear, symmetrical lycopene as substrate. However, unlike the ε-cyclase which adds only one ring, the β-cyclase introduces a ring at both ends of lycopene to form the bicyclic β-carotene.

Uniprot Description

Catalyzes the double cyclization reaction which converts lycopene to beta-carotene and neurosporene to beta-zeacarotene.