07-403-I
Anti-Cu/Zn-SOD Antibody
from rabbit, purified by affinity chromatography
Synonym(s):
Superoxide dismutase [Cu-Zn], Cu/Zn-SOD, Superoxide dismutase 1, hSod1
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About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Recommended Products
biological source
rabbit
Quality Level
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
purified by
affinity chromatography
species reactivity
human, mouse, rat
species reactivity (predicted by homology)
monkey (based on 100% sequence homology), primate (based on 100% sequence homology)
technique(s)
immunohistochemistry: suitable
western blot: suitable
NCBI accession no.
UniProt accession no.
shipped in
wet ice
target post-translational modification
unmodified
Gene Information
human ... SOD1(6647)
General description
Superoxide dismutase [Cu-Zn] (EC 1.15.1.1; UniProt P00441; also known as Cu/Zn superoxide dismutase, Epididymis secretory protein Li 44, hSod1, Indophenoloxidase A, Superoxide dismutase 1) is encoded by the SOD1 (also known as ALS1) gene (Gene ID 6647) in human. Superoxide dismutases (SOD) provide important cellular antioxidant defense against oxidative damage by catalyzing the dismutation (or partitioning) of the superoxide (O2−) radical into either molecular oxygen (O2) or hydrogen peroxide (H2O2). Superoxide dismutases are divided into three families based on the metal cofactor. The Cu/Zn type binds both copper and zinc, the Fe and Mn types bind either iron or manganese, and the Ni type binds nickel. Three forms of SOD are present in mammals, the cytosolic SOD1, the mitochondrial SOD2, and the extracellular SOD3. SOD1 exists in dimeric form, whereas the SOD2 and SOD3 are tetrameric. SOD1 and SOD3 Cu/Zn type, whereas SOD2 is Mn type. Mutations in SOD1 gene have been linked to 20% of amyotrophic lateral sclerosis (ALS), also known as Lou Gehrig disease.
Immunogen
Epitope: C-terminal region
KLH-conjugated linear peptide corresponding to a C-terminal sequence of human Cu/Zn-SOD.
Application
Anti-Cu/Zn-SOD Antibody is an antibody against Cu/Zn-SOD for use in Western Blotting, Immunohistochemistry.
Immunohistochemistry Analysis: A 1:1,000 dilution from a representative lot detected Cu/Zn-SOD in human cerebral cortex, mouse cerebellum, and mouse kidney tissue.
Research Category
Neuroscience
Neuroscience
Research Sub Category
Developmental Neuroscience
Developmental Neuroscience
Quality
Evaluated by Western Blotting in human brain tissue lysate.
Western Blotting Analysis: 0.1 µg/mL of this antibody detected Cu/Zn-SOD in 10 µg of human brain tissue lysate.
Western Blotting Analysis: 0.1 µg/mL of this antibody detected Cu/Zn-SOD in 10 µg of human brain tissue lysate.
Target description
~16 kDa observed
Physical form
Affinity purified
Purified rabbit polyclonal antibody in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.
Storage and Stability
Stable for 1 year at 2-8°C from date of receipt.
Other Notes
Concentration: Please refer to lot specific datasheet.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Anne-Sophie Montero et al.
EBioMedicine, 106, 105235-105235 (2024-07-13)
Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disease characterized by a progressive loss of motor neurons. The limited efficacy of recent therapies in clinical development may be linked to lack of drug penetration to the affected motor neurons due
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François Muratet et al.
Journal of neurology, neurosurgery, and psychiatry, 92(9), 942-949 (2021-04-01)
Mutations in superoxide dismutase 1 gene (SOD1), encoding copper/zinc superoxide dismutase protein, are the second most frequent high penetrant genetic cause for amyotrophic lateral sclerosis (ALS) motor neuron disease in populations of European descent. More than 200 missense variants are
Chao He et al.
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The Journal of biological chemistry, 299(5), 104695-104695 (2023-04-13)
Pulmonary fibrosis is a progressive lung disease characterized by macrophage activation. Asbestos-induced expression of nicotinamide adenine dinucleotide phosphate hydrogen oxidase 4 (NOX4) in lung macrophages mediates fibrotic progression by the generation of mitochondrial reactive oxygen species (ROS), modulating mitochondrial biogenesis
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