| Product Name | Human Serine--pyruvate aminotransferase (AGXT) ELISA Kit |
|---|---|
| Description | Serine--pyruvate aminotransferase is an enzyme expressed only in the liver and the protein is localized mostly in the peroxisomes, where it is involved in glyoxylate detoxification. Mutations in this gene, some of which alter subcellular targeting, have been associated with type I primary hyperoxaluria.The human peroxisomal AGT showed about 78% amino acid sequence identity with rat mitochondrial AGT. The putative pyridoxal phosphate-binding lysine residue at position 209 is conserved. A comparison of the 5-prime sequences indicated that the N-terminal 22 amino acids of the rat translation product are absent from the human protein. The loss of this mitochondrial targeting sequence (MTS) signal during evolution may partly explain the species differences in intracellular localization of AGT. This assay has high sensitivity and excellent specificity for detection of Human AGXT. No significant cross-reactivity or interference between Human AGXT and analogues was observed. |
| Synonyms | AGT, AGT1, AGXT1, PH1, SPAT, SPT, TLH6, L-alanine: glyoxylate aminotransferase 1|hepatic peroxisomal alanine:glyoxylate aminotransferase|serine-pyruvate aminotransferase|serine:pyruvate aminotransfe |
| Method | Sandwich ELISA |
| Detection Range | 31.25-2000 pg/mL |
| Sensitivity | 7.81 pg/mL |
| Reactivity | Human |
| Sample Types | Serum, Plasma, Other biological fluids. |
| Background | Serine--pyruvate aminotransferase is an enzyme expressed only in the liver and the protein is localized mostly in the peroxisomes, where it is involved in glyoxylate detoxification. Mutations in this gene, some of which alter subcellular targeting, have been associated with type I primary hyperoxaluria.The human peroxisomal AGT showed about 78% amino acid sequence identity with rat mitochondrial AGT. The putative pyridoxal phosphate-binding lysine residue at position 209 is conserved. A comparison of the 5-prime sequences indicated that the N-terminal 22 amino acids of the rat translation product are absent from the human protein. The loss of this mitochondrial targeting sequence (MTS) signal during evolution may partly explain the species differences in intracellular localization of AGT. |
| Supplier | Abebio |
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