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SOD1 Antibody (Center) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | P00441 |
|---|---|
| Clone Names | 90504027 |
| Gene ID | 6647 |
|---|---|
| Other Names | Superoxide dismutase [Cu-Zn], Superoxide dismutase 1, hSod1, SOD1 |
| Target/Specificity | The synthetic peptide sequence used to generate the antibody AP8733c was selected from the Center region of human SOD1. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | SOD1 (HGNC:11179) |
|---|---|
| Function | Destroys radicals which are normally produced within the cells and which are toxic to biological systems. |
| Cellular Location | Cytoplasm. Nucleus. Note=Predominantly cytoplasmic; the pathogenic variants ALS1 Arg-86 and Ala-94 gradually aggregates and accumulates in mitochondria. |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Background
SOD1 binds copper and zinc ions and is one of two isozymes responsible for destroying free superoxide radicals in the body. This isozyme is a soluble cytoplasmic protein, acting as a homodimer to convert naturally-occuring but harmful superoxide radicals to molecular oxygen and hydrogen peroxide. The other isozyme is a mitochondrial protein.
References
Crapo,J.D., et.al., Proc. Natl. Acad. Sci. U.S.A. 89 (21), 10405-10409 (1992)
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