Mouse/Rat SOD1/Cu-Zn SOD Alexa Fluor® 594-conjugated Antibody
R&D Systems, part of Bio-Techne | Catalog # AF3787T
Conjugate
Catalog #
Key Product Details
Species Reactivity
Mouse, Rat
Applications
Western Blot
Label
Alexa Fluor 594 (Excitation = 590 nm, Emission = 617 nm)
Antibody Source
Polyclonal Goat IgG
Product Specifications
Immunogen
E. coli-derived recombinant mouse SOD1
Met1-Gln154
Accession # P08228
Met1-Gln154
Accession # P08228
Specificity
Detects endogenous mouse and rat SOD1 in Western blots. In Western blots, this antibody shows no cross‑reacivity with recombinant human SOD2 or SOD3.
Clonality
Polyclonal
Host
Goat
Isotype
IgG
Applications
Application
Recommended Usage
Western Blot
Optimal dilution of this antibody should be experimentally determined.
Formulation, Preparation, and Storage
Purification
Antigen Affinity-purified
Formulation
Supplied 0.2mg/ml in 1X PBS with RDF1 and 0.09% Sodium Azide
Shipping
The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
Protect from light. Do not freeze. 12 months from date of receipt, 2 to 8 °C as supplied
Background: SOD1/Cu-Zn SOD
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.
Long Name
Superoxide Dismutase-1
Alternate Names
Cu-Zn SOD, CuZn SOD, Ipo1, IPOA, SOD, cytosolic, SOD, Soluble
Gene Symbol
SOD1
UniProt
Additional SOD1/Cu-Zn SOD Products
Product Specific Notices
This product is provided under an agreement between Life Technologies Corporation and R&D Systems, Inc, and the manufacture, use, sale or import of this product is subject to one or more US patents and corresponding non-US equivalents, owned by Life Technologies Corporation and its affiliates. The purchase of this product conveys to the buyer the non-transferable right to use the purchased amount of the product and components of the product only in research conducted by the buyer (whether the buyer is an academic or for-profit entity). The sale of this product is expressly conditioned on the buyer not using the product or its components (1) in manufacturing; (2) to provide a service, information, or data to an unaffiliated third party for payment; (3) for therapeutic, diagnostic or prophylactic purposes; (4) to resell, sell, or otherwise transfer this product or its components to any third party, or for any other commercial purpose. Life Technologies Corporation will not assert a claim against the buyer of the infringement of the above patents based on the manufacture, use or sale of a commercial product developed in research by the buyer in which this product or its components was employed, provided that neither this product nor any of its components was used in the manufacture of such product. For information on purchasing a license to this product for purposes other than research, contact Life Technologies Corporation, Cell Analysis Business Unit, Business Development, 29851 Willow Creek Road, Eugene, OR 97402, Tel: (541) 465-8300. Fax: (541) 335-0354.
For research use only
Loading...
Loading...
Loading...