protein

Recombinant Human Geranylgeranyl pyrophosphate synthase

MBS1175303

0.05 mg (E-Coli)

190 USD

Recombinant Protein

Recombinant Human Geranylgeranyl pyrophosphate synthase

Geranylgeranyl pyrophosphate synthase

(2E,6E)-farnesyl diphosphate synthase; Dimethylallyltranstransferase (EC:2.5.1.1); Farnesyl diphosphate synthase; Farnesyltranstransferase (EC:2.5.1.29); Geranylgeranyl diphosphate synthase; Geranyltranstransferase (EC:2.5.1.10)

geranylgeranyl pyrophosphate synthase; Geranylgeranyl pyrophosphate synthase; geranylgeranyl pyrophosphate synthase; geranylgeranyl diphosphate synthase 1; (2E,6E)-farnesyl diphosphate synthase; Dimethylallyltranstransferase (EC:2.5.1.1); Farnesyl diphosphate synthase; Farnesyltranstransferase (EC:2.5.1.29); Geranylgeranyl diphosphate synthase; Geranyltranstransferase (EC:2.5.1.10)

GGPS1

GGPS1; GGPS1; GGPPS; GGPPS1; GGPP synthase; GGPPSase

GGPPS_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

1-300; Full length;

300

MEKTQETVQRILLEPYKYLLQLPGKQVRTKLSQAFNHWL
KVPEDKLQIIIEVTEMLHNASLLIDDIEDNSKLRRGFPV
AHSIYGIPSVINSANYVYFLGLEKVLTLDHPDAVKLFTR
QLLELHQGQGLDIYWRDNYTCPTEEEYKAMVLQKTGGLF
GLAVGLMQLFSDYKEDLKPLLNTLGLFFQIRDDYANLHS
KEYSENKSFCEDLTEGKFSFPTIHAIWSRPESTQVQNIL
RQRTENIDIKKYCVHYLEDVGSFEYTRNTLKELEAKAYK
QIDARGGNPELVALVKHLSKMFKEENE

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.

Cancer

Catalyzes the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate, an important precursor of carotenoids and geranylated proteins.

Human geranylgeranyl diphosphate synthase isolation of the cDNA, chromosomal mapping and tissue expression.Ericsson J., Greene J.M., Carter K.C., Shell B.K., Duan D.R., Florence C., Edwards P.A.J. Lipid Res. 39:1731-1739(1998) Human geranylgeranyl diphosphate synthase. cDNA cloning and expression.Kuzuguchi T., Morita Y., Sagami I., Sagami H., Ogura K.J. Biol. Chem. 274:5888-5894(1999) Study on isolation of a geranylgeranyl pyrophosphate (GGPP) synthase cDNA and its expression -- development of a new assay system of gene functions.Misawa N., Okazaki H., Noguchi Y., Tatsuno I., Saito Y., Yasuda T., Hirai A.Proc. Jpn. Conf. Biochem. Lipids 41:293-296(1999) Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning.Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) Identification of the GGPS1 genes encoding geranylgeranyl diphosphate synthases from mouse and human.Kainou T., Kawamura K., Tanaka K., Matsuda H., Kawamukai M.Biochim. Biophys. Acta 1437:333-340(1999) Molecular cloning and expression analysis of a novel human cDNA encoding a protein homologous to Neurospora crassa geranylgeranyl pyrophosphate synthetase.Zhang M., Yu L., Hu P., Bi A., Zhang Q., Xu M., Zhao S.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) The 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) Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. 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) N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) The crystal structure of human geranylgeranyl pyrophosphate synthase reveals a novel hexameric arrangement and inhibitory product binding.Kavanagh K.L., Dunford J.E., Bunkoczi G., Russell R.G., Oppermann U.J. Biol. Chem. 281:22004-22012(2006)

83700220

NP_001032354.1

NM_001037277.1

O95749

50.85kD

Activation Of Gene Expression By SREBF (SREBP) Pathway (1270039); Cholesterol Biosynthesis Pathway (1270037); Metabolic Pathways (132956); Metabolism Pathway (1269956); Metabolism Of Lipids And Lipoproteins Pathway (1270001); Regulation Of Cholesterol Biosynthesis By SREBP (SREBF) Pathway (1270038); Terpenoid Backbone Biosynthesis Pathway (83022); Terpenoid Backbone Biosynthesis Pathway (408); Geranylgeranyl Diphosphate Biosynthesis Pathway (138387); Geranylgeranyldiphosphate Biosynthesis Pathway (545287)

This gene is a member of the prenyltransferase family and encodes a protein with geranylgeranyl diphosphate (GGPP) synthase activity. The enzyme catalyzes the synthesis of GGPP from farnesyl diphosphate and isopentenyl diphosphate. GGPP is an important molecule responsible for the C20-prenylation of proteins and for the regulation of a nuclear hormone receptor. Alternate transcriptional splice variants, both protein-coding and non-protein-coding, have been found for this gene. [provided by RefSeq, Sep 2010]

GGPS1: Catalyzes the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate, an important precursor of carotenoids and geranylated proteins. Belongs to the FPP/GGPP synthase family. Protein type: EC 2.5.1.29; Motility/polarity/chemotaxis; Secondary Metabolites Metabolism - terpenoid backbone biosynthesis; Transferase; EC 2.5.1.10; EC 2.5.1.1. Chromosomal Location of Human Ortholog: 1q43. Cellular Component: cytosol. Molecular Function: dimethylallyltranstransferase activity; farnesyltranstransferase activity; geranyltranstransferase activity; metal ion binding; protein binding. Biological Process: cholesterol biosynthetic process; farnesyl diphosphate biosynthetic process; geranyl diphosphate biosynthetic process; geranylgeranyl diphosphate biosynthetic process; isoprenoid metabolic process

0.05 mg (E-Coli)

190 USD

0.2 mg (E-Coli)

460

0.5 mg (E-Coli)

750

0.05 mg (Baculovirus)

950

0.1 mg (Mammalian-Cell)

1000