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SOD1 (Superoxide dismutase 1, SODC) (Internal Region) antibody
Alternatives Immunohistochemistry (IHC), Western Blotting (WB)
|5 references available|
|Price||454.67 $ Plus shipping costs $45.00|
|Availability||Will be delivered in 7 to 8 Business Days|
|Immunogen||A synthetic peptide from the internal part of human SOD1 (Superoxide dismutase 1, SODC) conjugated to an immunogenic carrier protein was used as the immunogen. The antigen is homologous in rat and mouse.|
|Description||Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Catalytic activity: 2 superoxide + 2 H(+) = O(2) + H(2)O(2). Subcellular location: Cytoplasm. Involvement in disease: Defects in SOD1 are the cause of amyotrophic lateral sclerosis type 1 (ALS1). ALS1 is a familial form of amyotrophic lateral sclerosis, a neurodegenerative disorder affecting upper and lower motor neurons and resulting in fatal paralysis. Sensory abnormalities are absent. Death usually occurs within 2 to 5 years. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of cases leading to familial forms. The protein (both wild-type and ALS1 variants) has a tendency to form fibrillar aggregates in the absence of the intramolecular disulfide bond or of bound zinc ions. These aggregates may have cytotoxic effects. Zinc binding promotes dimerization and stabilizes the native form. Also known as: SOD1, Superoxide dismutase 1, SODC.|
|Specificity||Appears to be specific for SOD1.|
|Application Notes||IHC, WB. A concentration of 10-50 µg/ml is recommended. The optimal concentration should be determined by the end user. Not yet tested in other applications.|
|Storage||Maintain the lyophilised/reconstituted antibodies frozen at -20°C for long term storage and refrigerated at 2-8°C for a shorter term. When reconstituting, glycerol (1:1) may be added for an additional stability. Avoid freeze and thaw cycles.|
|Restrictions||For Research Use only|
Kajihara, Enomoto, Nishijima et al.: "Comparison of properties between human recombinant and placental copper-zinc SOD." in: Journal of biochemistry, Vol. 104, Issue 5, pp. 851-4, 1989 (PubMed).
Levanon, Lieman-Hurwitz, Dafni et al.: "Architecture and anatomy of the chromosomal locus in human chromosome 21 encoding the Cu/Zn superoxide dismutase." in: The EMBO journal, Vol. 4, Issue 1, pp. 77-84, 1985 (PubMed).
Hallewell, Masiarz, Najarian et al.: "Human Cu/Zn superoxide dismutase cDNA: isolation of clones synthesising high levels of active or inactive enzyme from an expression library." in: Nucleic acids research, Vol. 13, Issue 6, pp. 2017-34, 1985 (PubMed).
Sherman, Dafni, Lieman-Hurwitz et al.: "Nucleotide sequence and expression of human chromosome 21-encoded superoxide dismutase mRNA." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 80, Issue 18, pp. 5465-9, 1983 (PubMed).
Ota, Suzuki, Nishikawa et al.: "Complete sequencing and characterization of 21,243 full-length human cDNAs." in: Nature genetics, Vol. 36, Issue 1, pp. 40-5, 2003 (PubMed).