EnCor Biotechnology
Mouse Monoclonal Antibody to Aldolase C Cat# MCA-1A1
Description
The MCA-1A1 antibody was made against recombinant human aldolase C C-terminal peptide KYEGSGEDGGAAAQSLYIANHAY, amino acids 342-364 of the NCBI sequence 1XFB_A. We then used nested 20 amino acid peptides to map the MCA-1A1 epitope to the peptide KYEGSGEDGGA, amino acids 342-352 of the human aldolase C sequence. Interestingly the antibody does not bind mouse aldolase C, which is somewhat different in sequence, RYEGSGDGGA, with a R>K change and missing an E residue. Since MCA-1A1 binds to aldolases from other species also lacking the E residue and since the K>R change is unique to mouse we can conclude that the K342 is essential for MCA-1A1 binding. Since the three aldolase enzymes are quite similar in amino acid sequence many available antibodies to one protein often have undocumented cross-reactivity with the other two, see here. An alternative mouse antibody to aldolase C is MCA-4A9, which binds the N-terminal peptide of the human molecule, a region in which there is considerable variability between the three aldolase enzymes. A third EnCor mouse monoclonal antibody MCA-E9, binds a region in the center of aldolase c which is virtually identical in aldolase A and B, and consequently as would be expected binds all three proteins.
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| Name: | Aldolase C, mouse monoclonal, Cat# MCA-1A1 |
| Immunogen: | C-terminal sequence KYEGSGEDGGAAAQSLYIANHAY 342-364 in NCBI sequence 1XFB_A |
| HGNC Name: | ALDOC |
| UniProt: | P09972 |
| Molecular Weight: | 40kDa |
| Host: | Mouse |
| Isotype: | IgG1 |
| Species Cross-Reactivity: | Human, rat, dog, cow, not mouse |
| RRID: | AB_2572224 |
| Format: | Purified antibody at 1mg/mL in 50% PBS, 50% glycerol plus 5mM NaN3 |
| Applications: | WB, IF/ICC, IHC |
| Recommended Dilutions: | WB: 1:1,000. IF/IHC: 1:500-1:1,000. |
| Storage: | Store at 4°C for short term, for longer term at -20°C |
Aldolases are important glycolytic cytosolic enzymes which catalyse the reversible conversion of fructose-1,6-bisphosphate to glyceraldehyde 3-phosphate. There are three aldolase isozymes coded by three distinct genes in mammals, namely aldolases A, B, and C. Aldolase A is heavily expressed in muscle enzyme and aldolase B is heavily expressed in liver and is regarded as a liver specific enzyme (1-5). In the adult, aldolase C is the brain-specific isozyme expressed in astrocytes and a few classes of neurons, notably Purkinje cells (4). Appropriate antibodies to aldolase C are therefore useful to identify astrocytes in cell culture and sectioned material, and the enzyme may be over expressed in some forms of cancer (6). Recent studies also suggest that detection of aldolase C in blood may be a useful biomarker of the severity and recovery process in patients suffering from the sequelae of traumatic brain injury (7).
The antibody has been tested on formalin fixed paraffin embedded sections, and is not recommended for this purpose.
1. Popovici T, et al. Localization of aldolase C mRNA in brain cells. FEBS Lett. 268:189-193 (1990).
2. Weber A, et al. Dietary Control of Aldolase B and L-type Pyruvate Kinamse RNAs in Rat. J. Biol. Chem. 259:1798-802 (1984).
3. Mukai T, et al. The structure of the brain-specific rat aldolase C gene and its regional expression. BBRC 174:1035-42 (1991).
4. Royds J, et al. Monoclonal antibody to aldolase C: a selective marker for Purkinje cells in the human cerebellum. Neuropathol. Appl. Neurobiol. 13:11-21 (1987).
5. Thompson R., Kynoch P. Willson V. Cellular localization of aldolase C subunits in human brain. Brain Res. 232:489-93 (1982).
6. Schapira F, Reuber M, Hatzfeld A. Resurgence of two fetal-type of aldolases (A and C) in some fast-growing hepatomas. BBRC 40:321-27 (1970).
7. Arai Y, et al. Position-independent, high-level, and correct regional expression of the rat aldolase C gene in the central nervous system of transgenic mice. Eur. J. Biochem. 221:253-260 (1994).
8. Wachsmuth E, Thorner M, Pfleiderer G. The cellular distribution of aldolase isozymes in rat kidney and brain determined in tissue sections by the immuno-histochemical method. Histochem. 45:143-61 (1975).
9. Walther EU, et al. Genomic sequences of aldolase C (Zebrin II) direct lacZ expression exclusively in non-neuronal cells of transgenic mice. PNAS 95:2615-20 (1998).
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