Thermo Fisher Scientific Superoxide Dismutase 1 (SOD1) (Antioxidant Enzyme) Monoclonal Antibody (SOD1/3923)

Applications

Tested Dilution

Publications

Immunohistochemistry (Paraffin) (IHC (P))

1-2 µg/mL

-

Immunocytochemistry (ICC/IF)

1-2 µg/mL

-

Flow Cytometry (Flow)

1-2 µg/10^6 cells

-

Peptide Array (Array)

Assay-dependent

-

Immunoelectrophoresis (IE)

Assay-dependent

-

Product Specifications

Species Reactivity

Human

Host/Isotype

Mouse / IgG2b, kappa

Class

Monoclonal

Type

Antibody

Clone

SOD1/3923

Immunogen

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View immunogen .st0{fill:#FFFFFF;} .st1{fill:#1E8AE7;}

Conjugate

Unconjugated Unconjugated Unconjugated

Form

Liquid

Concentration

200 µg/mL

Purification

Protein A/G

Storage buffer

PBS with 0.05% BSA

Contains

0.05% sodium azide

Storage conditions

4° C

Shipping conditions

Ambient (domestic); Wet ice (international)

Product Specific Information

Antibody is stable for 24 months.

Positive Control: HeLa or Jurkat cells. Human breast or ovarian carcinoma Cellular Localization: Cytoplasm

Specificity Comments: Cu-Zn superoxide dismutase-1 (SOD-1) is a well-characterized cytosolic scavenger of oxygen free radicals that requires copper and zinc binding to potentiate its enzymatic activity. Enzymatically, SOD-1 facilitates the dismutation of oxygen radicals to hydrogen peroxide and also catalyzes pro-oxidant reactions, which include the peroxidase activity and hydroxyl radical generating activity. SOD-1 is ubiquitously expressed in somatic cells and functions as a homodimer. Defects in the gene encoding SOD-1 have been implicated in the progression of neurological diseases, including amyotrophic lateral sclerosis (ALS), a neurodegenerative disease characterized by the loss of spinal motor neurons, Down syndrome and Alzheimer s disease. In familial ALS, several mutations in SOD-1 predominate, resulting in the loss of zinc binding, the loss of scavenging activity of SOD-1, and correlate with an increase in neurotoxicity and motor neuron death.

Target Information

SOD1 (superoxide dismutase) binds copper and zinc ions and is one of two isozymes responsible for destroying free superoxide radicals in the body. This 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.

For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.