Anti-SOD1 Magnetic Beads-IP Kit Product Components
| Components | Storage |
| Anti-SOD1 Magnetic Beads1,3 | 2-8℃ for 12 months |
| NP40 Cell Lysis Buffer2 | -20℃ for 12 months |
| 5×TBST（pH7.4） | |
| 1×TBST（pH7.4） | |
| ddH2O | |
| CD166 Positive Cell Lysate | -20℃ for 12 months |
| Alkaline Elution Buffer | 2-8℃ for 12 months |
| Acidity Elution Buffer | 2-8℃ for 12 months |
| Neutralization Buffer | 2-8℃ for 12 months |
[1] The IP KIT contains anti-SOD1 magnetic Beads (2 mg/mL) in phosphate buffered saline (PBS, pH 7.4) with sodium azide (0.1%).
[2] Using NP-40 cell lysate buffer in the kit is required,otherwise,the magnetic beads may be precipitated.
[3] Shipping: Magnetic Beads kits are shipped at ambient temperature in which magnetic beads are provided in liquid buffer.
Anti-SOD1 Magnetic Beads-IP Kit Product Description
The Anti-SOD1 magnetic Beads, conjugated with Anti-SOD1 antibody, are used for immuneprecipitation (IP) of SOD1 proteins which expressed in vitro expression systems. For IP, the beads are added to a sample containing SOD1 proteins to form a bead-protein complex. The complex is removed from the solution manually using a magnetic separator. The bound SOD1 proteins are dissociated from the magnetic beads using an elution buffer. Anti-SOD1 Magnetic Beads-IP Kit Antibody Information
Immunogen
Recombinant Human SOD1 / Superoxide Dismutase protein (Catalog#11727-H07E)
Species Reactivity
Human SOD1 / Superoxide Dismut
Source
Monoclonal Human Mouse IgG2b
Preparation
This antibody was produced from a hybridoma resulting from the fusion of a mouse myeloma with B cells obtained from a mouse immunized with purified, recombinant Human SOD1 / Superoxide Dismutase (rh SOD1 / Superoxide Dismutase; Catalog#11727-H07E; NP_000445.1; Ala 2-Gln 154).
Applications
Immunoprecipitation (IP), Minimum Protein Purification
Anti-SOD1 Magnetic Beads Immunoprecipitation (IP) Kit Alternative Names
Anti-ALSALCAM Magnetic Beads-Immunoprecipitatiopn (IP) Kit;Anti-ALS1ALCAM Magnetic Beads-Immunoprecipitatiopn (IP) Kit;Anti-HEL-S-44ALCAM Magnetic Beads-Immunoprecipitatiopn (IP) Kit;Anti-homodimerALCAM Magnetic Beads-Immunoprecipitatiopn (IP) Kit;Anti-hSod1ALCAM Magnetic Beads-Immunoprecipitatiopn (IP) Kit;Anti-IPOAALCAM Magnetic Beads-Immunoprecipitatiopn (IP) Kit;Anti-SODALCAM Magnetic Beads-Immunoprecipitatiopn (IP) Kit
SOD1 Background Information
SOD1 belongs to the Cu-Zn superoxide dismutase family. It binds copper and zinc ions and is one of two isozymes responsible for destroying free superoxide radicals in the body. The encoded 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. Mutations in this gene have been implicated as causes of familial amyotrophic lateral sclerosis. Rare transcript variants have been reported for this gene. SOD1 destroys radicals which are normally produced within the cells and which are toxic to biological systems. Defects in SOD1 are the cause of amyotrophic lateral sclerosis type 1 (ALS1). ALS1 is a familial form of amyotrophic lateral sclerosis, a neurodegenerative disorder affecting upper and lower motor neurons and resulting in fatal paralysis. Sensory abnormalities are absent. Death usually occurs within 2 to 5 years. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-1% of cases leading to familial forms.
Full Name
superoxide dismutase 1, soluble
References
Murakami K, et al. (2011) SOD1 (copper/zinc superoxide dismutase) deficiency drives amyloid β protein oligomerization and memory loss in mouse model of Alzheimer disease. J Biol Chem. 286(52):44557-68. Thompson M, et al. (2012) Paradoxical roles of serine racemase and D-serine in the G93A mSOD1 mouse model of amyotrophic lateral sclerosis. J Neurochem. 120(4):598-610. Magrané J, et al. (2012) Mitochondrial dynamics and bioenergetic dysfunction is associated with synaptic alterations in mutant SOD1 motor neurons. J Neurosci. 32(1):229-42. Gertz B, et al. (2012) Nuclear localization of human SOD1 and mutant SOD1-specific disruption of survival motor neuron protein complex in transgenic amyotrophic lateral sclerosis mice. J Neuropathol Exp Neurol. 71(2):162-77.
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