SOD1 (E4G1H) XP® Rabbit mAb (BSA and Azide Free) #65778
- WB
- IHC
Supporting Data
| REACTIVITY | H M R |
| SENSITIVITY | Endogenous |
| MW (kDa) | 16-18 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IHC-Immunohistochemistry
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
Product Information
Product Usage Information
This product is the carrier-free version of product #37385. All data were generated using the same antibody clone in the standard formulation which contains BSA and glycerol.
This formulation is ideal for use with technologies requiring specialized or custom antibody labeling, including fluorophores, metals, lanthanides, and oligonucleotides. It is not recommended for ChIP, ChIP-seq, CUT&RUN, or CUT&Tag assays. If you require a carrier-free formulation for chromatin profiling, please contact us. Optimal dilutions/concentrations should be determined by the end user.
Formulation
Supplied in 1X PBS, BSA and Azide Free.
For standard formulation of this product see product #37385.
Storage
Specificity / Sensitivity
SOD1 (E4G1H) XP® Rabbit mAb (BSA and Azide Free) recognizes endogenous levels of total SOD1 protein.
Species Reactivity:
Human, Mouse, Rat
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the amino terminus of human SOD1 protein.
Background
SOD1, Cu/Zn superoxide dismutase, is a major antioxidant enzyme that catalyzes the conversion of superoxide anion to hydrogen peroxide and molecular oxygen (1). SOD1 is ubiquitously expressed and is localized in the cytosol, nucleus, and mitochondrial intermembrane space. The SOD1 gene locus is on chromosome 21 in a region affected in Down Syndrome (2). In addition, over 100 distinct SOD1 inherited mutations have been identified in the familial form of amyotrophic lateral sclerosis (ALS), a progressive degenerative disease of motor neurons (3-5). Despite the fact that SOD1 helps to eliminate toxic reactive species, its mutations in ALS have been described as gain-of-function (5). The mechanism by which mutant SOD1 induces the neurodegeneration observed in ALS is still unclear. Mutant SOD1 proteins become misfolded and consequently oligomerize into high molecular weight species that aggregate and end up in proteinaceous inclusions (5).
Limited Uses
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