SOD1/Cu-Zn SOD Antibody Summary
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. |
Localization |
Accession Number: SODC_HUMAN ; SODC_PONPY ; SODC_PANTR ; SODC_SCHPO |
Specificity |
This has been shown to be specific for superoxide dismutase (SOD1) protein. |
Clonality |
Polyclonal |
Host |
Rabbit |
Gene |
SOD1 |
Purity |
Immunogen affinity purified |
Innovator's Reward |
Test in a species/application not listed above to receive a full credit towards a future purchase. |
Applications/Dilutions
Dilutions |
- Immunohistochemistry
- Immunohistochemistry-Paraffin
- Western Blot
|
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. |
Publications |
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Reactivity Notes
Human, other species have not yet been tested.
Packaging, Storage & Formulations
Storage |
Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles. |
Buffer |
No buffer |
Preservative |
No Preservative |
Concentration |
LYOPH |
Purity |
Immunogen affinity purified |
Reconstitution Instructions |
Reconstitute with deionized water. |
Alternate Names for SOD1/Cu-Zn SOD Antibody
Background
FUNCTION: Destroys radicals which are normally produced within the cells and which are toxic to biological systems. CATALYTIC ACTIVITY: 2 superoxide + 2 H+ = O2 + H2O2. COFACTOR: Binds 1 copper ion per subunit. COFACTOR: Binds 1 zinc ion per subunit. SUBUNIT: Homodimer. SUBCELLULAR LOCATION: Cytoplasm. DISEASE: Defects in SOD1 are the cause of familial amyotrophic lateral sclerosis (FALS); also called amyotrophic lateral sclerosis 1 (ALS1 or ALS). ALS is a degenerative disorder of motorneurons in the cortex, brainstem and spinal cord. ALS is characterized by muscular weakness and atrophy beginning in the hands and spreading to the forearms and legs. Muscle fasciculations are commonly visible. Sensory abnormalities are absent. Death usually occurs within 2 to 5 years. ALS is sometimes referred to as Lou Gehrig disease after the famous American baseball player who was diagnosed with the disorder. FALS, the familial form of ALS, accounts for about 10% of the cases and is transmitted in an autosomal dominant manner. The mean age at onset of FALS is 45 years. MISCELLANEOUS: Zinc binding promotes dimerization. SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
This product is distributed on behalf of Biosensis Pty. Ltd. of Australia.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are
guaranteed for 1 year from date of receipt.
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Publications for SOD1/Cu-Zn SOD Antibody (R-168-100)(10)
Showing Publications 1 -
10 of 10.
Publications using R-168-100 |
Applications |
Species |
Alexander MD, Traynor BJ, Miller N, Corr B, Frost E, McQuaid S, Brett FM, Green A, Hardiman O. True sporadic ALS associated with a novel SOD-1 mutation. Ann Neurol. 52(5):680-3. 2002-11-01 [PMID: 12402272] |
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Murakami T et al. J. Neurol. Sci. 189:45-47. 2001-01-01 [PMID: 11535232] |
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Gellera C et al. Neuromuscul. Disord. 11:404-410. 2001-01-01 [PMID: 11369193] |
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Penco S et al. Neurology 53:404-406. 1999-01-01 [PMID: 10430435] |
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Morita M et al. Neurosci. Lett. 205:79-82. 1996-01-01 [PMID: 8907321] |
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Jabusch JR et al. Biochemistry 19:2310-2316. 1980-01-01 [PMID: 6770891] |
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Sherman L et al. Proc. Natl. Acad. Sci. U.S.A. 80:5465-5469. 1983-01-01 [PMID: 6577438] |
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Hallewell RA et al. Nucleic Acids Res. 13:2017-2034. 1985-01-01 [PMID: 3889846] |
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Levanon D, Lieman-Hurwitz J, Dafni N et al. Architecture and anatomy of the chromosomal locus in human chromosome 21 encoding the Cu/Zn superoxide dismutase. EMBO J. 4:77-84. 1985-01-01 [PMID: 3160582] |
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Kajihara J, Enomoto M, Nishijima K et al. Comparison of properties between human recombinant and placental copper-zinc SOD. J. Biochem. 104:851-854. 1988-01-01 [PMID: 2853161] |
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