Aldolases are glycolytic enzyme that catalyzes the reversible aldol cleavage of fructose 1,6-bisphosphate and fructose-1-phosphate to dihydroxyacetone phosphate and either glyceraldehyde 3-phosphate or glyceraldehyde, respectively. Three aldolase isozymes are found in mammals specifically aldolases A, B, and C, each of which is encoded by a separate gene. Aldolase A is generally considered to be a muscle enzyme. Northern analysis of cultured cells suggests that it is present in both neurons and glia. Aldolase B is considered to be a liver-specific enzyme and it is transcriptionally activated by signals from hormones and dietary factors. In the adult, aldolase C is the brain-specific isozyme, with low but detectable activity in fetal tissues. Aldolase C shares 81% amino acid identity with aldolase A and 70% identity with aldolase B. Earlier studies using isozyme-specific antibodies report its location in gray matter astrocytes and cells of the pia mater. In situ hybridization of mouse central nervous system using isozyme-specific probes revealed that aldolase A and C are expressed in complementary cell types: aldolase A mRNA is found in neurons; aldolase C message is detected in astrocytes, some cells of the pia mater, and Purkinje cells. Aldolase C can in some situations be used as an astrocyte marker. However Purkinje cells of the cerebellum contain high levels of the enzyme, so the enzyme is not totally astrocyte specific.
Application information:
Western Blotting (WB) and Immunocytochemistry (IC). A dilution of 1:1,000 - 1:2,000 is recommended for WB. A dilution of 1:500 - 1:1,000 is recommended for IC. Biosensis recommends optimal dilutions/concentrations should be determined by the end user.
Type: Primary
Antigen: ALDOC
Clonality: Monoclonal
Clone: 4A9
Conjugation: Unconjugated
Epitope:
Host: Mouse
Isotype:
Reactivity: Human, Rat, Mouse, Cow, Pig