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  • Accession
  • Catalog #

SOD1 AntibodyRabbit Monoclonal Antibody

Country
United States
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Ordering Information
Catalog # Size Availability Price  
AJ1729c 100ul 400 ul 2-3 days $ 315.00 Add to cart
  • Specification
  • Citiations : 0
  • Reviews
  • Protocols
  • Backgrounds

SOD1 Antibody - Product info

ApplicationWB, IHC
  • Applications Legend:
  • W=Western Blotting
  • IP=Immunoprecipitation
  • IHC-P=Immunohistochemistry (Paraffin)
  • IF-IC=Immunofluorescence (Immunocytochemistry)
  • F=Flow Cytometry
Primary AccessionP00441
ReactivityHuman
Clone NamesEPR1726
Calculated MW15936 Da
Gene ID 6647
Other Names
SOD1, Superoxide dismutase [Cu-Zn]
Target/Specificity
A synthetic peptide corresponding to residues in human SOD1 was used as an immunogen.
Dilution
WB~~1:100000~500000
IHC~~1:250~500
Format
50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.
Storage
Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
Precautions
SOD1 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.

SOD1 Antibody - Protein Information

Name SOD1
Function
Destroys radicals which are normally produced within the cells and which are toxic to biological systems
Cellular Location
Cytoplasm. Note=The pathogenic variants ALS1 Arg-86 and Ala-94 gradually aggregates and accumulates in mitochondria

SOD1 Antibody - Related products

AP8733c: SOD1 Antibody (Center)

RI15016: SOD1 predesign siRNA

LY11098a: SOD1 Over-expression Lysate

BP8733c: SOD1 Antibody (Center) Blocking Peptide

AO1280a: SOD1 Antibody

AJ1729a: SOD1 Antibody

AJ1729b: SOD1 Antibody

AJ1729c: SOD1 Antibody

AF2022a: SOD1 Antibody

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Provided below are standard protocols that you may find useful for product applications.

BACKGROUND

Cu/Zn superoxide dismutase (SOD1), a major intracellular antioxidant enzyme, metabolizes superoxide radicals to molecular oxygen and hydrogen peroxide (1). SOD1 is primarily a cytosolic protein, and is ubiquitously expressed in many tissues at higher levels than in the brain and spinal cord (1, 2). The structural interplay of the conserved disulfide bond and metal-site occupancy in SOD1 is of increasing interest as these post-translational modifications are known to dramatically alter the catalytic chemistry, the subcellular localization, and the susceptibility of the protein to aggregation (3). Defective SOD is linked to motor neuron death and carries implications for understanding and possible treatment of the fatal neurodegenerative disorder familial amyotrophic lateral sclerosis (FALS) (4).

REFERENCES

1. Jun-ichi Niwa, et al. J. Biol. Chem., 282(38):28087-28095, 2007
2. P. Andreas Jonsson, et al. Brain 129: 451-464, 2006
3. Arnesano F, et al. J Biol Chem 279(46):47998-8003, 2004
4. Deng HX, et al. Science 261(5124):1047-51, 1993