Superoxide Dismutase 1 (SOD1) Rabbit Polyclonal Antibody [Clone ID: N/A]

CAT#: TA326384

Rabbit polyclonal SOD (Cu/Zn) Antibody



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CNY 6,017.00


货期*
4周

规格
    • 100 ug

Cited in 3 publications.

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Specifications

Product Data
Clone Name N/A
Applications IF, WB
Recommend Dilution 0.2ug/ml was sufficient for detection of Cu/Zn SOD in 20ug of HeLa cell lysate
Reactivity Human, Rat, Mouse, Bovine, Monkey, Dog, Hamster, Rabbit, Pig, Sheep, Xenopus, Coral
Host Rabbit
Clonality Polyclonal
Immunogen Human Cu/Zn SOD
Formulation PBS pH7.0, 50% glycerol, 0.09% sodium azide
Concentration lot specific
Purification Affinity (antigen) Purified
Conjugation Unconjugated
Storage Condition Store at -20°C as received.
Gene Name superoxide dismutase 1, soluble
Background Superoxide dismutase (SOD) is an endogenously produced intracellular enzyme present in almost every cell in the body . It works by catalyzing the dismutation of the superoxide radical O2¯to O2 and H2O2, which are then metabolized to H2O and O2 by catalase and glutathione peroxidase . In general, SODs play a major role in antioxidant defense mechanisms . There are two main types of SOD in mammalian cells. One form (SOD1) contains Cu and Zn ions as a homodimer and exists in the cytoplasm. The two subunits of 16 kDa each are linked by two cysteines forming an intra-subunit disulphide bridge . The second form (SOD2) is a manganese containing enzyme and resides in the mitochondrial matrix. It is a homotetramer of 80 kDa. The third form (SOD3 or EC-SOD) is like SOD1 in that it contains Cu and Zn ions, however it is distinct in that it is a homotetramer, with a mass of 30 kDA and it exists only in the extracellular space. SOD3 can also be distinguished by its heparin-binding capacity .
Synonyms ALS; ALS1; HEL-S-44; homodimer; hSod1; IPOA; SOD
Note Detects a ~23kDa (human) and 19kDa (other species) proteins corresponding to the molecular mass of Cu/Zn superoxide dismutase (SOD) on SDS PAGE immunoblots.
Reference Data
Protein Families Druggable Genome
Protein Pathways Amyotrophic lateral sclerosis (ALS), Huntington's disease, Prion diseases
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Citations (3)

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