Superoxide Dismutase 1, Soluble (SOD1) antibody

Antigen: Superoxide Dismutase 1, Soluble (SOD1)

Synonyms: ALS, SOD, ALS1, IPOA, homodimer, Cu, Zn Sod, Zn-SOD, Cu-Zn SOD, Cu/Zn SOD, Cu/Zn superoxide dismutase, Cu/ZnSOD, CuSOD, CuZn SOD, CuZn-SOD, CuZnSOD, Cu[2+]/Zn[2+]SOD, G, SOD-1, SOD1, To, To-1, cSOD, l(3)108, l(3)68Af', l(3)G, DmelCG11793, CG11793, LOC692639, CU/ZN-SOD, sod1, SODC, DKFZP469M1833

Clonality: Polyclonal

Host: Rabbit

Reactivity: Human

Conjugate: Un-conjugated

Application: Immunohistochemistry (Frozen Sections) (IHC (fro)), Western Blotting (WB)

Catalog no.: ABIN271690

Additional Information

Alternative name: Superoxide Dismutase 1 (SOD1)

Immunogen: A synthetic peptide (HEKADDLGKGGNEESTKTG) corresponding to the amino acids121-139 of human superoxide dismutase (SOD1) conjugated to diphtheria toxin hasbeen used as the immunogen. The peptide is homologous with the correspondingsequence derived from superoxide dismutase (SOD1) protein in orangutan, chimpanzeeand fission yeast.

Cross-Reactivity: Human

Description: 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

Specificity: This antibody has been shown to be specific for superoxide dismutase (SOD1) protein. Species Reactivity: Human, other species have not yet been tested. Localization: Accession Number: SODC_HUMAN , SODC_PONPY , SODC_PANTR ,SODC_SCHPO.

Synonyms: ALS, SOD, ALS1, IPOA, homodimer, Cu, Zn Sod, Zn-SOD, Cu-Zn SOD, Cu/Zn SOD, Cu/Zn superoxide dismutase, Cu/ZnSOD, CuSOD, CuZn SOD, CuZn-SOD, CuZnSOD, Cu[2+]/Zn[2+]SOD, G, SOD-1, SOD1, To, To-1, cSOD, l(3)108, l(3)68Af', l(3)G, DmelCG11793, CG11793, LOC692639, CU/ZN-SOD, sod1, SODC, DKFZP469M1833

Application Details

Application Notes: IHC, WB. This antibody works superbly in Immunohistochemistry on frozen or paraffinembedded tissues. Antigen retrieval has been used in testing but may not be necessary.Typical working dilutions for routine immunohistochemistry are 1: 100 to 1: 1000depending 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 enduser.

Buffer: Reconstitute in 100 ul of sterile water. Centrifuge to remove any insoluble material. Preservative: No Preservative

Research Area: Inflammation, Enzymes, Metabolism

Restrictions: For Research Use only

Publications

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).

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).

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).

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).

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).

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).

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).