protein

Recombinant Human Serine--pyruvate aminotransferase

MBS962305

0.05 mg (E-Coli)

190 USD

Recombinant Protein

Recombinant Human Serine--pyruvate aminotransferase

Serine--pyruvate aminotransferase

Alanine-glyoxylate aminotransferase (EC:2.6.1.44); AGT

serine--pyruvate aminotransferase; Serine--pyruvate aminotransferase; serine--pyruvate aminotransferase; alanine-glyoxylate aminotransferase; Alanine--glyoxylate aminotransferase (EC:2.6.1.44); AGT

AGXT

AGXT; AGXT; AGT; PH1; SPT; AGT1; SPAT; TLH6; AGXT1; AGT1; SPAT; SPT; AGT

SPYA_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

1-392

392

MASHKLLVTPPKALLKPLSIPNQLLLGPGPSNLPPRIMA
AGGLQMIGSMSKDMYQIMDEIKEGIQYVFQTRNPLTLVI
SGSGHCALEAALVNVLEPGDSFLVGANGIWGQRAVDIGE
RIGARVHPMTKDPGGHYTLQEVEEGLAQHKPVLLFLTHG
ESSTGVLQPLDGFGELCHRYKCLLLVDSVASLGGTPLYM
DRQGIDILYSGSQKALNAPPGTSLISFSDKAKKKMYSRK
TKPFSFYLDIKWLANFWGCDD

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.

Signal Transduction

Cloning and nucleotide sequence of cDNA encoding human liver serine-pyruvate aminotransferase.Nishiyama K., Berstein G., Oda T., Ichiyama A.Eur. J. Biochem. 194:9-18(1990) Identification of mutations associated with peroxisome-to-mitochondrion mistargeting of alanine/glyoxylate aminotransferase in primary hyperoxaluria type 1.Purdue P.E., Takada Y., Danpure C.J.J. Cell Biol. 111:2341-2351(1990) Human peroxisomal L-alanine glyoxylate aminotransferase. Evolutionary loss of a mitochondrial targeting signal by point mutation of the initiation codon.Takada Y., Kaneko N., Esumi H., Purdue P.E., Danpure C.J.Biochem. J. 268:517-520(1990) Characterization and chromosomal mapping of a genomic clone encoding human alanine:glyoxylate aminotransferase.Purdue P.E., Lumb M.J., Fox M., Griffo G., Hamon-Benais C., Povey S., Danpure C.J.Genomics 10:34-42(1991) 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) 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)

4557289

NP_000021.1

NM_000030.2

P21549

47.08kD

Alanine And Aspartate Metabolism Pathway (198783); Alanine, Aspartate And Glutamate Metabolism Pathway (101142); Alanine, Aspartate And Glutamate Metabolism Pathway (100063); Carbon Metabolism Pathway (814926); Carbon Metabolism Pathway (817567); Glycine, Serine And Threonine Metabolism Pathway (82949); Glycine, Serine And Threonine Metabolism Pathway (313); Glyoxylate And Dicarboxylate Metabolism Pathway (83002); Glyoxylate And Dicarboxylate Metabolism Pathway (383); Glyoxylate Metabolism And Glycine Degradation Pathway (1270180)

This gene is expressed only in the liver and the encoded protein is localized mostly in the peroxisomes, where it is involved in glyoxylate detoxification. Mutations in this gene, some of which alter subcellular targetting, have been associated with type I primary hyperoxaluria. [provided by RefSeq, Jul 2008]

AGXT: Defects in AGXT are the cause of hyperoxaluria primary type 1 (HP1); also known as primary hyperoxaluria type I (PH1) and oxalosis I. HP1 is a rare autosomal recessive inborn error of glyoxylate metabolism characterized by increased excretion of oxalate and glycolate, and the progressive accumulation of insoluble calcium oxalate in the kidney and urinary tract. Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. Protein type: EC 2.6.1.44; Motility/polarity/chemotaxis; Transferase; EC 2.6.1.51; Amino Acid Metabolism - alanine, aspartate and glutamate; Amino Acid Metabolism - glycine, serine and threonine; Mitochondrial. Chromosomal Location of Human Ortholog: 2q37.3. Cellular Component: mitochondrial matrix; peroxisomal matrix; peroxisome. Molecular Function: alanine-glyoxylate transaminase activity; amino acid binding; protein binding; protein homodimerization activity; protein self-association; pyridoxal phosphate binding; receptor binding; serine-pyruvate transaminase activity; transaminase activity. Biological Process: glycine biosynthetic process, by transamination of glyoxylate; glyoxylate catabolic process; glyoxylate metabolic process; L-alanine catabolic process; L-cysteine catabolic process; Notch signaling pathway; oxalic acid secretion; proteasomal protein catabolic process; pyruvate biosynthetic process; response to cAMP; response to glucocorticoid stimulus. Disease: Hyperoxaluria, Primary, Type I

0.05 mg (E-Coli)

190 USD

0.2 mg (E-Coli)

460

0.5 mg (E-Coli)

750

0.05 mg (Baculovirus)

1160

1 mg (E-Coli)

1180