Anti-Aldolase/ALDOA Antibody Picoband® (monoclonal, 6H8) Fluoro594 Conjugated

Aldolase A (ALDOA, or ALDA), also known as fructose-bisphosphate aldolase, is an enzyme that in humans is encoded by the ALDOA gene on chromosome 16. This gene encodes a member of the class I fructose-bisphosphate aldolase protein family. The encoded protein is a glycolytic enzyme that catalyzes the reversible conversion of fructose-1,6-bisphosphate to glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. Three aldolase isozymes (A, B, and C), encoded by three different genes, are differentially expressed during development. Mutations in this gene have been associated with Glycogen Storage Disease XII, an autosomal recessive disorder associated with hemolytic anemia. Disruption of this gene also plays a role in the progression of multiple types of cancers. Related pseudogenes have been identified on chromosomes 3 and 10.

Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. Its F-actin depolymerization activity is regulated by association with CSPR3. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. It is the major component of intranuclear and cytoplasmic actin rods. Required for muscle maintenance. May play a role during the exchange of alpha-actin forms during the early postnatal remodeling of the sarcomere.

1. Du, S; Guan, Z; Hao, L; Song, Y; Wang, L; Gong, L; Liu, L; Qi, X; Hou, Z; Shao, S (2014) . Fructose-bisphosphate aldolase a is a potential metastasis-associated marker of lung squamous cell carcinoma and promotes lung cell tumorigenesis and migration. PLOS ONE. 9 (1) : e85804. 2. Yao, DC; Tolan, DR; Murray, MF; Harris, DJ; Darras, BT; Geva, A; Neufeld, EJ (15 March 2004) . Hemolytic anemia and severe rhabdomyolysis caused by compound heterozygous mutations of the gene for erythrocyte/muscle isozyme of aldolase, ALDOA (Arg303X/Cys338Tyr) . Blood. 103 (6) : 2401–3. 3. St-Jean, M; Izard, T; Sygusch, J (11 May 2007) . A hydrophobic pocket in the active site of glycolytic aldolase mediates interactions with Wiskott-Aldrich syndrome protein. The Journal of Biological Chemistry. 282 (19) : 14309–15.