Recombinant Human AGXT
Cat.No. : | AGXT-26660TH |
Product Overview : | Recombinant fragment of Human AGXT with N-terminal proprietary tag. Predicted MW 36.63 kDa. |
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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. |
Protein length : | 100 amino acids |
Molecular Weight : | 36.630kDa inclusive of tags |
Source : | Wheat germ |
Tissue specificity : | Liver. |
Form : | Liquid |
Purity : | Proprietary Purification |
Storage buffer : | pH: 8.00Constituents:0.79% Tris HCl, 0.3% Glutathione |
Storage : | Shipped on dry ice. Upon delivery aliquot and store at -80oC. Avoid freeze / thaw cycles. |
Sequences of amino acids : | EAAAYLHGRLQALGLQLFVKDPALR LPTVTTVAVPAGYDWRDIVSYVIDH FDIEIMGGLGPSTGKVLRIGLLGCN ATRENVDRVTEALRAALQHCPKKKL |
Sequence Similarities : | Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. |
Gene Name : | AGXT alanine-glyoxylate aminotransferase [ Homo sapiens ] |
Official Symbol : | AGXT |
Synonyms : | AGXT; alanine-glyoxylate aminotransferase; SPAT; serine--pyruvate aminotransferase; AGT; AGT1; AGXT1; glycolicaciduria; L alanine: glyoxylate aminotransferase 1; oxalosis I; PH1; primary hyperoxaluria type 1; serine:pyruvate aminotransferase; SPT; |
Gene ID : | 189 |
mRNA Refseq : | NM_000030 |
Protein Refseq : | NP_000021 |
MIM : | 604285 |
Uniprot ID : | P21549 |
Chromosome Location : | 2q37.3 |
Pathway : | Alanine and aspartate metabolism, organism-specific biosystem; Alanine, aspartate and glutamate metabolism, organism-specific biosystem; Alanine, aspartate and glutamate metabolism, conserved biosystem; Glycine, serine and threonine metabolism, organism-specific biosystem; Glycine, serine and threonine metabolism, conserved biosystem; |
Function : | alanine-glyoxylate transaminase activity; amino acid binding; protein binding; protein homodimerization activity; pyridoxal phosphate binding; |
Products Types
◆ Recombinant Protein | ||
AGXT-225R | Recombinant Rat AGXT Protein, His (Fc)-Avi-tagged | +Inquiry |
AGXT-503H | Recombinant Human AGXT Protein, His-tagged | +Inquiry |
AGXT-1322M | Recombinant Mouse AGXT Protein (25-414 aa), His-tagged | +Inquiry |
AGXT-314M | Recombinant Mouse AGXT Protein (25-414 aa), His-SUMO-tagged | +Inquiry |
Agxt-504M | Recombinant Mouse Agxt Protein, His-tagged | +Inquiry |
◆ Lysates | ||
AGXT-8967HCL | Recombinant Human AGXT 293 Cell Lysate | +Inquiry |
Related Gene
For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.
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Q&As (10)
Ask a questionAGXT contains a PLP-binding domain, characteristic of aminotransferases, which is critical for its enzymatic activity and substrate specificity.
Yes, mutations in the AGXT gene can cause primary hyperoxaluria type 1 (PH1), a rare autosomal recessive disorder characterized by the overproduction and accumulation of oxalate, resulting in severe kidney and urinary tract complications.
Targeting AGXT enzymatic activity may hold promise for developing therapies to prevent kidney stone formation in non-PH1 patients; however, further research is needed to validate this approach.
AGXT is primarily localized in the peroxisomes, a subcellular organelle responsible for various metabolic processes, including lipid metabolism and detoxification.
Epigenetic modifications, such as DNA methylation or histone acetylation, could potentially regulate AGXT gene expression and activity, affecting oxalate metabolism.
AGXT activity can be regulated by phosphorylation, allosteric modulation, and interaction with other proteins involved in peroxisomal metabolism.
AGXT plays a crucial role in the peroxisomal glyoxylate pathway, converting glyoxylate to glycine to prevent the accumulation of harmful oxalate, which can lead to kidney stone formation.
In PH1 patients, AGXT deficiency impairs the conversion of glyoxylate to glycine, leading to the accumulation of glyoxylate. Excessive glyoxylate is converted to oxalate, which can form kidney stones and cause tissue damage.
AGXT may participate in other cellular processes or metabolic pathways, and its broader functional roles warrant further exploration.
AGXT catalyzes the conversion of glyoxylate and L-alanine to glycine and pyruvate, utilizing PLP as a cofactor.
Customer Reviews (5)
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