| 货号 | AF3787-SP |
| 别名 | ALS; ALS1; amyotrophic lateral sclerosis 1 (adult); Cu; Cu/Zn superoxide dismutase; Cu-Zn SOD; EC 1.15.1.1; homodimer; hSod1; indophenoloxidase A; Ipo1; IPOA; SOD; SOD, cytosolic; SOD, Soluble; superoxide dismutase [Cu-Zn]; Superoxide dismutase 1; superoxide dismutase 1, soluble; Zn superoxide dismutase, EC 1.15.1.110superoxide dismutase, cystolic | 全称 | Superoxide Dismutase-1 |
| 反应种属 | Mouse/Rat |
| 应用 | Western Blot(0.2 µg/mL) |
| 目标/特异性 | Detects endogenous mouse and rat SOD1 in Western blots. In Western blots, this antibody shows no cross‑reacivity with recombinant human SOD2 or SOD3. |
| 使用方法 | Western Blot: 0.2 µg/mL |
| 来源 | Reconstitute at 0.2 mg/mL in sterile PBS. |
| 产品组分 |
| 供应商 | R&D Systems |
| Entrez Gene IDs | 6647 (Human); 20655 (Mouse); 24786 (Rat) |
| 应用文献 | |
| R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions. Adverse effects of reduced oxygen tension on the proliferative capacity of rat kidney and insulin-secreting cell lines involve DNA damage and stress responses. | |
| 纯化方式 | Antigen Affinity-purified |
| 免疫原 | E. coli-derived recombinant mouse SOD1 Met1-Gln154 Accession # P08228 |
| 生物活性 | Mouse, Rat |
| 标记 | Unconjugated |
| 溶解方法 | Reconstitute at 0.2 mg/mL in sterile PBS. |
| 背景 | Superoxide Dismutases (SODs), originally identified as Indophenoloxidase (IPO), are enzymes that catalyze the converversion of naturally-occuring but harmful superoxide radicals into molecular oxygen and hydrogen peroxide. Superoxide Dismutases 1, SOD1, also known as Cu/Zn SOD, soluble SOD, and IPO-A, is a soluble, cytoplasmic 16 kDa homodimer. Each SOD1 monomer binds one Cu2+ and Zn2+ ion. Three isozymes of SOD have been identified and are functionally related but have very modest sequence homology. SOD1 shares 23% and 27% sequence identity with SOD2 and SOD3, respectively. Mouse SOD1 is 97% aa identcal to rat SOD1. Mutations in SOD1 have been suggested to be the cause of familial amyotrophic lateral sclerosis (ALS). The ALS-causing mutations of SOD1 are scattered throughout the protein and provide no clear functional or structural clues to the underlying disease mechanism. The oligomerization hypothesis suggests that mutant SOD1 proteins become misfolded and consequently oligomerize into high molecular weight aggregates that result in the death of motor neurons. The oxidative damage hypothesis suggests that loss of function mutations in SOD1 result in the intracellular accumulation of the superoxide radical, leading to free radical-mediated damage, the release of cytochrome c, and apoptosis. |
| 运输条件 | Blue Ice |
| 存放说明 | 4℃ |
| 参考文献 |
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Detection of Mouse/Rat SOD1/Cu-Zn SOD by Western Blot. Western blot shows lysates of NIH-3T3 mouse embryonic fibroblast cell line and NRK rat normal kidney cell line. PVDF membrane was probed with 0.2 µg/mL of Goat Anti-Mouse/Rat SOD1/Cu-Zn SOD Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3787) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF017). A specific band was detected for SOD1/Cu-Zn SOD at approximately 19 kDa (as indicated). This experiment was conducted using Immunoblot Buffer Group 2. |
