AGXT Polyclonal Antibody (E-AB-12706)
For research use only.
| Verified Samples |
Verified Samples in WB: Human fetal liver, HepG2 |
| Dilution | WB 1:500-1:2000 |
| Isotype | IgG |
| Host | Rabbit |
| Reactivity | Human, Mouse, Rat |
| Applications | WB |
| Clonality | Polyclonal |
| Immunogen | Synthetic peptide of human AGXT |
| Abbre | AGXT |
| Synonyms | AGT, AGT1, AGXT1, Agxt, Alanine glyoxylate aminotransferase, Alanine glyoxylate aminotransferase3, Alanine--glyoxylate aminotransferase, EC 2.6.1.44, EC 2.6.1.51, Hepatic peroxisomal alanine glyoxylate aminotransferase, Hepatic peroxisomal alanine:glyoxylate aminot |
| Swissprot | |
| Calculated MW | 43 kDa |
| Cellular Localization | Peroxisome. Mitochondrion matrix. Except in some HP1 patients where AGT is found in the mitochondrial matrix. |
| Concentration | 0.6 mg/mL |
| Buffer | Phosphate buffered solution, pH 7.4, containing 0.05% stabilizer and 50% glycerol. |
| Purification Method | Affinity purification |
| Research Areas | Cancer, Metabolism, Signal Transduction |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | The product is shipped with ice pack,upon receipt,store it immediately at the temperature recommended. |
| background | Serine—pyruvate aminotransferase is an enzyme that in humans is encoded by the AGXT gene. 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. 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. |
Other Clones
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Unconjugated
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