SAB1406464
Anti-SOD1 antibody produced in mouse
purified immunoglobulin, buffered aqueous solution
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About This Item
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41
Produits recommandés
Source biologique
mouse
Conjugué
unconjugated
Forme d'anticorps
purified immunoglobulin
Type de produit anticorps
primary antibodies
Clone
polyclonal
Forme
buffered aqueous solution
Poids mol.
antigen ~15.9 kDa
Espèces réactives
human
Technique(s)
western blot: 1 μg/mL
Numéro d'accès NCBI
Numéro d'accès UniProt
Conditions d'expédition
dry ice
Température de stockage
−20°C
Modification post-traductionnelle de la cible
unmodified
Informations sur le gène
human ... SOD1(6647)
Description générale
Superoxide Dismutase (SOD) or CuZn-SOD (SOD1), a cytoplasmic and mitochondrial intermembrane space protein, is located on human chromosome 21q22. It belongs to superoxide dismutase multigene family.
The protein encoded by this gene binds copper and zinc ions and is one of two isozymes responsible for destroying free superoxide radicals in the body. The encoded isozyme is a soluble cytoplasmic protein, acting as a homodimer to convert naturally-occuring but harmful superoxide radicals to molecular oxygen and hydrogen peroxide. The other isozyme is a mitochondrial protein. Mutations in this gene have been implicated as causes of familial amyotrophic lateral sclerosis. Rare transcript variants have been reported for this gene. (provided by RefSeq)
Immunogène
SOD1 (NP_000445.1, 1 a.a. ~ 154 a.a) full-length human protein.
Sequence
MATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERHVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
Sequence
MATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERHVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
Actions biochimiques/physiologiques
Superoxide Dismutase (SOD) or CuZn-SOD (SOD1) mutations results in amyotrophic lateral sclerosis. It acts as a mediator of the HMF (hypomagnetic field) effect.
Forme physique
Solution in phosphate buffered saline, pH 7.4
Clause de non-responsabilité
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Code de la classe de stockage
10 - Combustible liquids
Classe de danger pour l'eau (WGK)
WGK 1
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Certificats d'analyse (COA)
Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".
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Jianzhu Luo et al.
Frontiers in physiology, 4, 295-295 (2013-11-07)
ecSOD function has prototypically been associated with the extracellular space due to its secretion and localization to the extracellular matrix. A myocyte-specific ecSOD transgenic mouse has shown that it can also be localized to the myocyte intracellular compartment and is
Chen Wu et al.
Cell reports, 26(5), 1143-1156 (2019-01-31)
Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disease affecting both upper and lower motor neurons (MNs). To date, its underlying mechanisms have yet to be clarified completely, and there are no truly effective treatments. Here, we show that MAP4K4, a
Shielding of the geomagnetic field reduces hydrogen peroxide production in human neuroblastoma cell and inhibits the activity of CuZn superoxide dismutase
Zhang HT, et al.
Protein & cell, 8(7), 527-537 (2017)
A review of asthma genetics: gene expression studies and recent candidates
Malerba G1 and Pignatti PF
Journal of applied genetics, 46(1), 93-104 (2005)
An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria
Wong PC, et al.
Neuron, 14(6), 1105-1116 (1995)
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