Superoxide Dismutase 1 (SOD1) Rabbit Polyclonal Antibody
CNY 5,250.00
Cited in 2 publications. |
CNY 300.00
CNY 1,430.00
CNY 2,900.00
CNY 6,650.00
Specifications
Product Data | |
Applications | WB |
Recommend Dilution | WB |
Reactivity | Human, Mouse |
Host | Rabbit |
Clonality | Polyclonal |
Immunogen | The immunogen for anti-SOD1 antibody is: synthetic peptide directed towards the C-terminal region of Human SOD1. Synthetic peptide located within the following region: DVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLA |
Formulation | Liquid. Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose. |
Conjugation | Unconjugated |
Storage Condition | Store at -20°C as received. |
Predicted Protein Size | 17 kDa |
Gene Name | superoxide dismutase 1, soluble |
Database Link | |
Background | SOD1 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 its gene have been implicated as causes of familial amyotrophic lateral sclerosis. |
Synonyms | ALS; ALS1; HEL-S-44; homodimer; hSod1; IPOA; SOD |
Note | Immunogen Sequence Homology: Pig: 100%; Rat: 100%; Goat: 100%; Horse: 100%; Human: 100%; Mouse: 100%; Sheep: 100%; Yeast: 100%; Bovine: 100%; Guinea pig: 100%; Rabbit: 93%; Zebrafish: 92%; Dog: 86% |
Reference Data | |
Protein Families | Druggable Genome |
Protein Pathways | Amyotrophic lateral sclerosis (ALS), Huntington's disease, Prion diseases |
Citations (2)
The use of this Antibodies has been cited in the following citations: |
---|
S-Sulfocysteine simplifies fed-batch processes and increases the CHO specific productivity via anti-oxidant activity.
,null,
Journal of biotechnology
,PubMed ID 26654938
[SOD1]
|
S-Sulfocysteine simplifies fed-batch processes and increases the CHO specific productivity via anti-oxidant activity
,Hecklau, C;Pering, S;Seibel, R;Schnellbaecher, A;,
Journal of Biotechnology Jan2016
[SOD1]
|
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