Superoxide Dismutase 1, Soluble (SOD1) (AA 121-139) antibody

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AA 121-139
(23), (16), (11), (9), (6), (6), (4), (3), (3), (2), (2), (2), (2), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
(228), (76), (72), (46), (12), (12), (12), (8), (7), (7), (6), (6), (4), (3), (3), (2), (2), (2), (2), (2), (2), (1), (1), (1), (1), (1)
(212), (75), (12), (9), (5), (1), (1)
(16), (15), (8), (7), (3), (3), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (1), (1)
Western Blotting (WB), Immunohistochemistry (IHC), Immunohistochemistry (Paraffin-embedded Sections) (IHC (p))
(268), (181), (96), (90), (49), (33), (31), (29), (28), (13), (5), (4), (3), (2), (2), (2), (2), (2), (1)
Pubmed 10 references available
Quantity 0.1 mL
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Catalog No. ABIN271690
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Immunogen A synthetic peptide (HEKADDLGKGGNEESTKTG) corresponding to the amino acids 121-139 of human superoxide dismutase (SOD1) conjugated to diphtheria toxin has been used as the immunogen. The peptide is homologous with the corresponding sequence derived from superoxide dismutase (SOD1) protein in orangutan, chimpanzee and fission yeast.
Specificity This has been shown to be specific for superoxide dismutase (SOD1) protein.
Cross-Reactivity (Details) other species have not yet been tested.
Purification affinity purified
Alternative Name Superoxide Dismutase 1 (SOD1)
Background FUNCTION: Destroys radicals which are normally produced within the cells and whichare toxic to biological systems. CATALYTIC ACTIVITY: 2 superoxide + 2 H+ = O2 +H2O2. COFACTOR: Binds 1 copper ion per subunit. COFACTOR: Binds 1 zinc ion persubunit. SUBUNIT: Homodimer. SUBCELLULAR LOCATION: Cytoplasm. DISEASE:Defects in SOD1 are the cause of familial amyotrophic lateral sclerosis (FALS), alsocalled amyotrophic lateral sclerosis 1 (ALS1 or ALS). ALS is a degenerative disorder ofmotorneurons in the cortex, brainstem and spinal cord. ALS is characterized bymuscular weakness and atrophy beginning in the hands and spreading to the forearmsand legs. Muscle fasciculations are commonly visible. Sensory abnormalities areabsent. Death usually occurs within 2 to 5 years. ALS is sometimes referred to as LouGehrig disease after the famous American baseball player who was diagnosed with thedisorder. FALS, the familial form of ALS, accounts for about 10% of the cases and istransmitted in an autosomal dominant manner. The mean age at onset of FALS is 45years. MISCELLANEOUS: Zinc binding promotes dimerization. SIMILARITY: Belongs tothe Cu-Zn superoxide dismutase family. Alternate Names: anti-ALS antibody, anti-ALS1 antibody, anti-IPOA antibody, anti-SOD antibody,anti-homodimer antibody, biosensis. Related Diseases: Antioxidant Enzymes
Gene Symbol: SOD1
Gene ID 6647
Research Area Inflammation, Enzymes, Metabolism
Application Notes IHC-P, WB. This antibody works superbly in Immunohistochemistry on frozen or paraffin embedded tissues. Antigen retrieval has been used in testing but may not be necessary. Typical working dilutions for routine immunohistochemistry are 1: 100 to 1: 1000 depending on tissue and detection method. For western blotting a dilution range of 1: 1000 to 1: 4000 is recommended. The optimal dilution should be determined by the end user.
Restrictions For Research Use only
Format Lyophilized
Reconstitution Add diH20 to desired concentration.
Preservative Without preservative
Handling Advice Avoid freeze-thaw cycles
Storage 4 °C
Storage Comment 4 °C short term. Aliquot and store at -20 °C long term.
General Alexander, Traynor, Miller et al.: ""True" sporadic ALS associated with a novel SOD-1 mutation." in: Annals of neurology, Vol. 52, Issue 5, pp. 680-3, 2002 (PubMed).

Murakami, Warita, Hayashi et al.: "A novel SOD1 gene mutation in familial ALS with low penetrance in females." in: Journal of the neurological sciences, Vol. 189, Issue 1-2, pp. 45-7, 2001 (PubMed).

Gellera, Castellotti, Riggio et al.: "Superoxide dismutase gene mutations in Italian patients with familial and sporadic amyotrophic lateral sclerosis: identification of three novel missense mutations." in: Neuromuscular disorders : NMD, Vol. 11, Issue 4, pp. 404-10, 2001 (PubMed).

Penco, Schenone, Bordo et al.: "A SOD1 gene mutation in a patient with slowly progressing familial ALS." in: Neurology, Vol. 53, Issue 2, pp. 404-6, 1999 (PubMed).

Morita, Aoki, Abe et al.: "A novel two-base mutation in the Cu/Zn superoxide dismutase gene associated with familial amyotrophic lateral sclerosis in Japan." in: Neuroscience letters, Vol. 205, Issue 2, pp. 79-82, 1997 (PubMed).

Jabusch, Farb, Kerschensteiner et al.: "Some sulfhydryl properties and primary structure of human erythrocyte superoxide dismutase." in: Biochemistry, Vol. 19, Issue 11, pp. 2310-6, 1980 (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).

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).

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).

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).

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