Recombinant Human Fucose-1-phosphate guanylyltransferase | MyBioSource MBS1033389 product information

product summary

company name :

MyBioSource

product type :

protein

product name :

Recombinant Human Fucose-1-phosphate guanylyltransferase

catalog :

MBS1033389

quantity :

0.05 mg (E-Coli)

price :

190 USD

more info or order :

MyBioSource product webpage

product information

catalog number :

MBS1033389

products type :

Recombinant Protein

products full name :

Recombinant Human Fucose-1-phosphate guanylyltransferase

products short name :

Fucose-1-phosphate guanylyltransferase

products name syn :

GDP-L-fucose diphosphorylase; GDP-L-fucose pyrophosphorylase

other names :

fucose-1-phosphate guanylyltransferase isoform 3; Fucose-1-phosphate guanylyltransferase; fucose-1-phosphate guanylyltransferase; fucose-1-phosphate guanylyltransferase; GDP-L-fucose diphosphorylase; GDP-L-fucose pyrophosphorylase

products gene name :

FPGT

other gene names :

FPGT; FPGT; GFPP; GFPP

uniprot entry name :

FPGT_HUMAN

host :

E Coli or Yeast or Baculovirus or Mammalian Cell

sequence positions :

1-594

sequence length :

353

sequence :

MAAARDPPEVSLREATQRKLRRFSELRGKLVARGEFWDI
VAITAADEKQELAYNQQLSEKLKRKELPLGVQYHVFVDP
AGAKIGNGGSTLCALQCLEKLYGDKWNSFTILLIHSGGY
SQRLPNASALGKIFTALPLGNPIYQMLELKLAMYIDFPL
NMNPGILVTCADDIELYSIGEFEFIRFDKPGFTALAHPS
SLTIGTTHGVFVLDPFDDLKHRDLEYRSCHRFLHKPSIE
KMYQFNAVCRPGNFCQQDFAG

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 :

Catalyzes the formation of GDP-L-fucose from GTP and L-fucose-1-phosphate. Functions as a salvage pathway to reutilize L-fucose arising from the turnover of glycoproteins and glycolipids.

products references :

GDP-L-fucose pyrophosphorylase purification, cDNA cloning, and properties of the enzyme.Pastuszak I., Ketchum C., Hermanson G., Sjoberg E.J., Drake R., Elbein A.D.J. Biol. Chem. 273:30165-30174(1998) 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)

ncbi gi num :

510025472

ncbi acc num :

NP_001186257.2

ncbi gb acc num :

NM_001199328.2

uniprot acc num :

O14772

ncbi mol weight :

68.6kD

ncbi pathways :

Amino Sugar And Nucleotide Sugar Metabolism Pathway (82979); Amino Sugar And Nucleotide Sugar Metabolism Pathway (350); Asparagine N-linked Glycosylation Pathway (1268714); Biosynthesis Of The N-glycan Precursor (dolichol Lipid-linked Oligosaccharide, LLO) And Transfer To A Nascent Protein Pathway (1268715); Fructose And Mannose Metabolism Pathway (82930); Fructose And Mannose Metabolism Pathway (291); GDP-L-fucose Biosynthesis II (from L-fucose) Pathway (142191); GDP-fucose Biosynthesis Pathway (1339108); Metabolic Pathways (132956); Metabolism Of Proteins Pathway (1268677)

ncbi summary :

L-fucose is a key sugar in glycoproteins and other complex carbohydrates since it may be involved in many of the functional roles of these macromolecules, such as in cell-cell recognition. The fucosyl donor for these fucosylated oligosaccharides is GDP-beta-L-fucose. There are two alternate pathways for the biosynthesis of GDP-fucose; the major pathway converts GDP-alpha-D-mannose to GDP-beta-L-fucose. The protein encoded by this gene participates in an alternate pathway that is present in certain mammalian tissues, such as liver and kidney, and appears to function as a salvage pathway to reutilize L-fucose arising from the turnover of glycoproteins and glycolipids. This pathway involves the phosphorylation of L-fucose to form beta-L-fucose-1-phosphate, and then condensation of the beta-L-fucose-1-phosphate with GTP by fucose-1-phosphate guanylyltransferase to form GDP-beta-L-fucose. Alternative splicing results in multiple transcript variants. Read-through transcription also exists between this gene and the neighboring downstream TNNI3 interacting kinase (TNNI3K) gene. [provided by RefSeq, Dec 2010]

uniprot summary :

FPGT: Catalyzes the formation of GDP-L-fucose from GTP and L- fucose-1-phosphate. Functions as a salvage pathway to reutilize L- fucose arising from the turnover of glycoproteins and glycolipids. 4 isoforms of the human protein are produced by alternative splicing. Protein type: EC 2.7.7.30; Carbohydrate Metabolism - fructose and mannose; Carbohydrate Metabolism - amino sugar and nucleotide sugar; Transferase. Chromosomal Location of Human Ortholog: 1p31.1. Cellular Component: cytoplasm; cytosol. Molecular Function: catalytic activity; fucose-1-phosphate guanylyltransferase activity; GTP binding. Biological Process: cellular protein metabolic process; dolichol-linked oligosaccharide biosynthetic process; fucose metabolic process; post-translational protein modification; protein amino acid N-linked glycosylation via asparagine

size1 :

0.05 mg (E-Coli)

price1 :

190 USD

size2 :

0.2 mg (E-Coli)

price2 :

460

size3 :

0.5 mg (E-Coli)

price3 :

750

size4 :

1 mg (E-Coli)

price4 :

1180

size5 :

0.05 mg (Baculovirus)

price5 :

1395

more info or order :

MyBioSource product webpage