Superoxide Dismutase 1, Soluble (SOD1) antibody

Details for Product No. ABIN271658
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Antigen
Synonyms
ALS, ALS1, IPOA, SOD, hSod1, homodimer, CG11793, Cu, Cu-Zn SOD, Cu/Zn SOD, Cu/Zn sod, Cu/Zn superoxide dismutase, Cu/ZnSOD, CuSOD, CuZn SOD, CuZn-SOD, CuZn-SOD1, CuZnSOD, Cu[2+]/Zn[2+]SOD, Dmel\\CG117 ... show more
ALS, ALS1, IPOA, SOD, hSod1, homodimer, CG11793, Cu, Cu-Zn SOD, Cu/Zn SOD, Cu/Zn sod, Cu/Zn superoxide dismutase, Cu/ZnSOD, CuSOD, CuZn SOD, CuZn-SOD, CuZn-SOD1, CuZnSOD, Cu[2+]/Zn[2+]SOD, Dmel\\CG11793, G, Mn SOD, SOD-1, SOD1, Sod-1, Sod1, To, To-1, Zn SOD, Zn Sod, Zn-SOD, ZnSod, cSOD, cSod, dSOD1, l(3)108, l(3)68Af', l(3)G, sod, sod1, CU/ZN-SOD, B430204E11Rik, Cu/Zn-SOD, Ipo-1, Ipo1, SODC, SOD1L1, LOC692639, DKFZP469M1833 show less
Reactivity
Mouse (Murine)
(197), (89), (78), (59), (13), (11), (11), (7), (7), (6), (6), (6), (3), (2), (2), (2), (2), (2), (1), (1), (1), (1), (1), (1)
Host
Rabbit
(195), (67), (11), (9), (7), (1)
Clonality
Polyclonal
Conjugate
Un-conjugated
(17), (12), (5), (3), (3), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Application
Western Blotting (WB)
(254), (183), (94), (85), (50), (34), (30), (26), (13), (10), (5), (4), (2), (2), (2), (2), (2), (1)
Pubmed 4 references available
Catalog no. ABIN271658
Quantity 0.1 mL
Price
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Immunogen A synthetic peptide (ASGEPVV LSGQIT) as part of mouse superoxide dismutase (SOD1) protein (aa: 24-36) conjugated to diphtheria toxoid
Specificity Specificity was confirmed by western blot detecting mouse superoxide dismutase (SOD1).
Purification Whole antisera
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 Recommended dilutions: Western Blot 1:500-1:1000
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 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).

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).

Hosts (195), (67), (11), (9), (7), (1)
Reactivities (197), (89), (78), (59), (13), (11), (11), (7), (7), (6), (6), (6), (3), (2), (2), (2), (2), (2), (1), (1), (1), (1), (1), (1)
Applications (254), (183), (94), (85), (50), (34), (30), (26), (13), (10), (5), (4), (2), (2), (2), (2), (2), (1)
Conjugates (17), (12), (5), (3), (3), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Epitopes (14), (11), (7), (7), (4), (4), (4), (3), (3), (2), (2), (2), (2), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Request Want additional data for this product?

The Independent Validation Initiative strives to provide you with high quality data. Find out more

Add to Basket

Order hotline:

  • +1 404 474 4654
  • +1 888 205 9894 (TF)
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