Chicken Hydroxyacylglutathione hydrolase, mitochondrial (HAGH) ELISA Kit
| Product Name | Chicken Hydroxyacylglutathione hydrolase, mitochondrial (HAGH) ELISA Kit |
|---|---|
| Description | Glyoxalase II, otherwise known as hydroxyacyl-glutathione hydrolase, converts the intermediate substrate S-lactoyl-glutathione to reduced glutathione and D-lactate. By study of somatic cell hybrids, Honey and Shows (1981) concluded that the gene for glyoxalase II is on chromosome 16. Mulley and Callen (1986) confirmed the assignment of HAGH to chromosome 16 by studies of a human-mouse hybrid panel. They found that both HAGH and phosphoglycolate phosphatase (PGP) were present only in those cell lines containing 16p13. Board (1980) described rare polymorphism, observed only in a Micronesian population in which a new variant allele had a frequency of 0.016. In the heterozygotes, the electrophoretic pattern was a double band, suggesting that the structure of glyoxalase II is monomeric. This assay has high sensitivity and excellent specificity for detection of Chicken HAGH. No significant cross-reactivity or interference between Chicken HAGH and analogues was observed. |
| Synonyms | GLO2, GLX2, GLXII, HAGH1, glyoxalase II|hydroxyacylglutathione hydroxylase |
| Method | Sandwich ELISA |
| Detection Range | 0.312-20 ng/mL |
| Sensitivity | 0.129 ng/mL |
| Reactivity | Chicken |
| Sample Types | Serum, Plasma, Other biological fluids. |
| Background | Glyoxalase II, otherwise known as hydroxyacyl-glutathione hydrolase, converts the intermediate substrate S-lactoyl-glutathione to reduced glutathione and D-lactate. By study of somatic cell hybrids, Honey and Shows (1981) concluded that the gene for glyoxalase II is on chromosome 16. Mulley and Callen (1986) confirmed the assignment of HAGH to chromosome 16 by studies of a human-mouse hybrid panel. They found that both HAGH and phosphoglycolate phosphatase (PGP) were present only in those cell lines containing 16p13. Board (1980) described rare polymorphism, observed only in a Micronesian population in which a new variant allele had a frequency of 0.016. In the heterozygotes, the electrophoretic pattern was a double band, suggesting that the structure of glyoxalase II is monomeric. |
| Supplier | Abebio |
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