Serine--pyruvate aminotransferase Recombinant Protein | AGXT recombinant protein

Recombinant Human Serine--pyruvate aminotransferase

Cat. Num. AAA962305

• Gene Names: AGXT; AGT; PH1; SPT; AGT1; SPAT; TLH6; AGXT1
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Serine--pyruvate aminotransferase; Recombinant Human Serine--pyruvate aminotransferase; Alanine-glyoxylate aminotransferase (EC:2.6.1.44); AGT; AGXT 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: 1-392aa; Full Length
• Sequence: MASHKLLVTPPKALLKPLSIPNQLLLGPGPSNLPPRIMAAGGLQMIGSMSKDMYQIMDEIKEGIQYVFQTRNPLTLVISGSGHCALEAALVNVLEPGDSFLVGANGIWGQRAVDIGERIGARVHPMTKDPGGHYTLQEVEEGLAQHKPVLLFLTHGESSTGVLQPLDGFGELCHRYKCLLLVDSVASLGGTPLYMDRQGIDILYSGSQKALNAPPGTSLISFSDKAKKKMYSRKTKPFSFYLDIKWLANFWGCDDQPRMYHHTIPVISLYSLRESLALIAEQGLENSWRQHREAAAYLHGRLQALGLQLFVKDPALRLPTVTTVAVPAGYDWRDIVSYVIDHFDIEIMGGLGPSTGKVLRIGLLGCNATRENVDRVTEALRAALQHCPKKKL
• Sequence Length: 392

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

SDS-PAGE

Product Categories/Family for AGXT recombinant protein

Signal Transduction

References

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)

NCBI and Uniprot Product Information

• NCBI GI #: 4557289
• NCBI GeneID: 189
• NCBI Accession #: NP_000021.1
• NCBI GenBank Nucleotide #: NM_000030.2
• UniProt Accession #: P21549; Q53QU6
• Molecular Weight: 44.3 kDa
• NCBI Official Full Name: serine--pyruvate aminotransferase
• NCBI Official Synonym Full Names: alanine-glyoxylate aminotransferase
• NCBI Official Symbol: AGXT
• NCBI Official Synonym Symbols: AGT; PH1; SPT; AGT1; SPAT; TLH6; AGXT1
• NCBI Protein Information: serine--pyruvate aminotransferase
• UniProt Protein Name: Serine--pyruvate aminotransferase
• Protein Family: Serine--pyruvate aminotransferase
• UniProt Gene Name: AGXT
• UniProt Synonym Gene Names: AGT1; SPAT; SPT; AGT
• UniProt Entry Name: SPYA_HUMAN

NCBI Description

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]

Uniprot Description

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