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AGXT recombinant protein :: Serine--pyruvate aminotransferase Recombinant Protein

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Catalog # MBS962305
Unit / Price
  0.01 mg (E-Coli)  /  $160 +1 FREE 8GB USB
  0.01 mg (Yeast)  /  $175 +1 FREE 8GB USB
  0.05 mg (E-Coli)  /  $200 +1 FREE 8GB USB
  0.05 mg (Yeast)  /  $225 +1 FREE 8GB USB
  0.1 mg (E-Coli)  /  $295 +1 FREE 8GB USB
  0.1 mg (Yeast)  /  $355 +1 FREE 8GB USB
  0.2 mg (E-Coli)  /  $480 +1 FREE 8GB USB
  0.2 mg (Yeast)  /  $565 +1 FREE 8GB USB
  0.5 mg (E-Coli)  /  $790 +1 FREE 8GB USB
  0.5 mg (Yeast)  /  $925 +1 FREE 8GB USB
  1 mg (E-Coli)  /  $1,215 +1 FREE 8GB USB
  1 mg (Yeast)  /  $1,410 +1 FREE 8GB USB
SDS-PAGE
Product Name

Serine--pyruvate aminotransferase (AGXT), Recombinant Protein

Popular Item
Full Product Name

Recombinant Human Serine--pyruvate aminotransferase

Product Synonym Names
Alanine-glyoxylate aminotransferase (EC:2.6.1.44); AGT
Research Use Only
For Research Use Only. Not for use in diagnostic procedures.
Sequence Positions
1-392aa; Full Length
Sequence
MASHKLLVTP PKALLKPLSI PNQLLLGPGP SNLPPRIMAA GGLQMIGSMS KDMYQIMDEI KEGIQYVFQT RNPLTLVISG SGHCALEAAL VNVLEPGDSF LVGANGIWGQ RAVDIGERIG ARVHPMTKDP GGHYTLQEVE EGLAQHKPVL LFLTHGESST GVLQPLDGFG ELCHRYKCLL LVDSVASLGG TPLYMDRQGI DILYSGSQKA LNAPPGTSLI SFSDKAKKKM YSRKTKPFSF YLDIKWLANF WGCDDQPRMY HHTIPVISLY SLRESLALIA EQGLENSWRQ HREAAAYLHG RLQALGLQLF VKDPALRLPT VTTVAVPAGY DWRDIVSYVI DHFDIEIMGG LGPSTGKVLR IGLLGCNATR ENVDRVTEAL RAALQHCPKK KL
OMIM
259900
3D Structure
ModBase 3D Structure for P21549
Host
E Coli or Yeast or Baculovirus or Mammalian Cell
Purity/Purification
Greater than 90% as determined by SDS-PAGE. (lot specific)
Form/Format
Liquid containing glycerol
Tag Information
This protein contains an N-terminal tag and may also contain a C-terminal tag. Tag types are determined by various factors including tag-protein stability, please inquire for tag information.
Sterility
Sterile filter available upon request.
Endotoxin
Low endotoxin available upon request.
Preparation and Storage
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
ISO Certification
Manufactured in an ISO 9001:2008 Certified Laboratory.
Other Notes
Small volumes of AGXT recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.
Searchable Terms forAGXTpurchase
Serine pyruvate aminotransferase AGXT or SPT has tissue restricted expression. This enzyme and gene expression pattern is localized specifically to peroxisomes where it detoxifies byproducts of oxidative phosphorylation metabolism like glyoxylate by removing alanine. To further understand liver detoxification or to use in cell assay types, MyBiosource offers a human AGXT alanine glyoxylate aminotransferase in multiple tagged recombinant protein forms. Like all our recombinant proteins from Creative Biomart, you can chose your expression vector with confidence. All are genome sequence verified from conserved domain plasmids and highly purified after protein production. Our recombinant human protein resources take the guesswork out of your lab. AGT pyruvate alanine DNA is confirmed with genome workbench alignment tool BLAST, so you know any antibody generated will be robust and ready to validate. To find out about additional applications such as data generation with chemical AMP bioassays, go to MyBiosource.com today.
Product Categories/Family for AGXT recombinant protein

AGXT recombinant protein SDS-PAGE image
(Note: Representative image, actual molecular weight may vary depending on Tag type and expression host)
NCBI/Uniprot data below describe general gene information for AGXT. It may not necessarily be applicable to this product.
NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Primary Accession #
UniProt Secondary Accession #
UniProt Related Accession #
Molecular Weight
47.08kD
NCBI Official Full Name
serine--pyruvate aminotransferase
NCBI Official Synonym Full Names
alanine-glyoxylate aminotransferase
NCBI Official Symbol
NCBI Official Synonym Symbols
AGT; PH1; SPT; AGT1; SPAT; TLH6; AGXT1
  [Similar Products]
NCBI Protein Information
serine--pyruvate aminotransferase
UniProt Protein Name
Serine--pyruvate aminotransferase
UniProt Synonym Protein Names
Alanine--glyoxylate aminotransferase (EC:2.6.1.44); AGT
UniProt Gene Name
UniProt Synonym Gene Names
AGT1; SPAT; SPT; AGT  [Similar Products]
UniProt Entry Name
SPYA_HUMAN
NCBI Summary for AGXT
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 Comments for AGXT
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
Product References and Citations for AGXT recombinant protein
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)

Precautions
All of MyBioSource's Products are for scientific laboratory research purposes and are not for diagnostic, therapeutics, prophylactic or in vivo use. Through your purchase, you expressly represent and warrant to MyBioSource that you will properly test and use any Products purchased from MyBioSource in accordance with industry standards. MyBioSource and its authorized distributors reserve the right to refuse to process any order where we reasonably believe that the intended use will fall outside of our acceptable guidelines.
Disclaimer
While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.

It is the responsibility of the customer to report product performance issues to MyBioSource within 30 days of receipt of the product. Please visit our Terms & Conditions page for more information.
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