SOD-1 rabbit pAb

• Background :

  The protein encoded by this gene 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. [provided by RefSeq, Jul 2008]

• Description :

  The protein encoded by this gene 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. [provided by RefSeq, Jul 2008],

• UniProt :

  P00441

• Swiss Prot :

  P00441

• Reactivity :

  Human; Mouse; Rat

• Immunogen :

  The antiserum was produced against synthesized peptide derived from human SOD-1. AA range:36-85

• Clonality :

  Polyclonal

• Source :

  Rabbit

• Applications :

  WB; ELISA

• Concentration :

  1 mg/ml

• Dilution :

  Western Blot: 1/500 - 1/2000. ELISA: 1/10000. Not yet tested in other applications.

• Molecular Weight :

  18kD

• Storage Conditions :

  -20°C/1 year

• Observed Molecular Weight :

  18kD

• Fragment :

  IgG

• Subcellular Location :

  Cytoplasm . Mitochondrion . Nucleus . Predominantly cytoplasmic; the pathogenic variants ALS1 Arg-86 and Ala-94 gradually aggregates and accumulates in mitochondria. .

• Other Product Names :

  SOD1; Superoxide dismutase [Cu-Zn]; Superoxide dismutase 1; hSod1

• Gene ID (Human) :

  6647