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SOD1 AntibodyRabbit Monoclonal Antibody
| Country | United States
Ordering Information
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|---|---|---|---|---|
| Catalog # | Size | Availability | Price | |
| AJ1729c | 100ul 400 ul | 2-3 days | $ 315.00 | DISCONTINED INQUIRE CLICK INQUIRE Add to cart |
- Specification
- Citiations : 0
- Reviews
- Protocols
- Backgrounds
SOD1 Antibody - Product info | |
| Application | WB, IHC
|
| Primary Accession | P00441 |
| Reactivity | Human |
| Clone Names | EPR1726 |
| Calculated MW | 15936 Da |
| Gene ID 6647 | |
| Other Names SOD1, Superoxide dismutase [Cu-Zn] | |
| Target/Specificity A synthetic peptide corresponding to residues in human SOD1 was used as an immunogen. | |
| Dilution WB~~1:100000~500000 IHC~~1:250~500 | |
| Format 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA. | |
| Storage Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. | |
| Precautions SOD1 Antibody is for research use only and not for use in diagnostic or therapeutic procedures. | |
SOD1 Antibody - Protein Information | |
| Name SOD1 | |
| Function Destroys radicals which are normally produced within the cells and which are toxic to biological systems | |
| Cellular Location Cytoplasm. Note=The pathogenic variants ALS1 Arg-86 and Ala-94 gradually aggregates and accumulates in mitochondria | |
SOD1 Antibody - Related products
AP8733c: SOD1 Antibody (Center)
LY11098a: SOD1 Over-expression Lysate
SOD1 Antibody - Application data
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A.Western blot analysis on (A) HeLa, (B) MCF-7, (C) Jurkat and (D) HT-29 cell lysates using anti-SOD1 RabMAb (Cat. #AJ1729c), dilution 1:200,000.
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B. Immunohistochemical analysis of paraffin-embedded human kidneys using anti-SOD1 RabMAb (Cat. #AJ1729c).
SOD1 Antibody - Research Areas
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BACKGROUND
Cu/Zn superoxide dismutase (SOD1), a major intracellular antioxidant enzyme, metabolizes superoxide radicals to molecular oxygen and hydrogen peroxide (1). SOD1 is primarily a cytosolic protein, and is ubiquitously expressed in many tissues at higher levels than in the brain and spinal cord (1, 2). The structural interplay of the conserved disulfide bond and metal-site occupancy in SOD1 is of increasing interest as these post-translational modifications are known to dramatically alter the catalytic chemistry, the subcellular localization, and the susceptibility of the protein to aggregation (3). Defective SOD is linked to motor neuron death and carries implications for understanding and possible treatment of the fatal neurodegenerative disorder familial amyotrophic lateral sclerosis (FALS) (4).
REFERENCES
1. Jun-ichi Niwa, et al. J. Biol. Chem., 282(38):28087-28095, 2007
2. P. Andreas Jonsson, et al. Brain 129: 451-464, 2006
3. Arnesano F, et al. J Biol Chem 279(46):47998-8003, 2004
4. Deng HX, et al. Science 261(5124):1047-51, 1993