Anti-PHGDH Antibody Picoband® HRP Conjugated

This gene encodes the enzyme which is involved in the early steps of L-serine synthesis in animal cells. L-serine is required for D-serine and other amino acid synthesis. The enzyme requires NAD/NADH as a cofactor and forms homotetramers for activity. Mutations in this gene have been found in a family with congenital microcephaly, psychomotor retardation and other symptoms. Multiple alternatively spliced transcript variants have been found, however the full-length nature of most are not known.

E.coli-derived human PHGDH recombinant protein (Position: L15-F533) . Human PHGDH shares 94.4% and 94.2% amino acid (aa) sequence identity with mouse and rat PHGDH, respectively.

1. Acuna-Hidalgo, R., Schanze, D., Kariminejad, A., Nordgren, A., Kariminejad, M. H., Conner, P., Grigelioniene, G., Nilsson, D., Nordenskjold, M., Wedell, A., Freyer, C., Wredenberg, A., and 18 others. Neu-Laxova syndrome is a heterogeneous metabolic disorder caused by defects in enzymes of the L-serine biosynthesis pathway. Am. J. Hum. Genet. 95: 285-293, 2014. 2. Baek, J. Y., Jun, D. Y., Taub, D., Kim, Y. H. Assignment of human 3-phosphoglycerate dehydrogenase (PHGDH) to human chromosome band 1p12 by fluorescence in situ hybridization. Cytogenet. Cell Genet. 89: 6-7, 2000. 3. Benke, P. J., Hidalgo, R. J., Braffman, B. H., Jans, J., van Gassen, K. L. I., Sunbul, R., El-Hattab, A. W. Infantile serine biosynthesis defect due to phosphoglycerate dehydrogenase deficiency: variability in phenotype and treatment response, novel mutations, and diagnostic challenges. J. Child Neurol. 32: 543-549, 2017.