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Development and characterization of human and mouse specific antibodies to CuZn-superoxide dismutase (SOD1).
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| Author |
Bartlett, S E, et al. |
| Citation Information |
J. Neurosci. Methods, 98: 63-7 (2000), : (2000) |
| Related Products |
AB5480, AB5482 |
| Pub Med ID |
10837872 |
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Abstract
Mutations in the copper/zinc superoxide dismutase (SOD1) gene are associated with 15-20% of the familial forms of motor neuron disease. Mice where a transgene has been incorporated that encodes for the human SOD1 mutation develop a form of motor neurone disease that closely resembles human forms of this disease. We have produced and characterized species-specific antibodies to epitopes in the SOD1 protein, amino acids 25-37, a region that distinguishes between the human and the mouse species of SOD1. The antisera generated were unable to immunoprecipitate the mouse or the human forms of SOD1 from tissue extracts unless the homodimeric complex of SOD1 was denatured. As SOD1 exists as a homodimeric complex in the cytoplasm of cells, this suggests that amino acids in position, 25-37 are close to the dimeric interface of SOD1.
