Superxoide Dismutase Fish Antibodies

Description: Quantitativecompetitive ELISA kit for measuring Fish Superoxide Dismutase (SOD) in samples from serum, plasma, tissue homogenates. A new trial version of the kit, which allows you to test the kit in your application at a reasonable price.

Description: A polyclonal antibody for detection of Fish from Human, Mouse. This Fish antibody is for IHC-P, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from the N-terminal region of human Fish

Description: A polyclonal antibody for detection of Fish from Human, Mouse. This Fish antibody is for IHC-P, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from the N-terminal region of human Fish

Description: A polyclonal antibody for detection of Fish from Human, Mouse. This Fish antibody is for IHC-P, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from the N-terminal region of human Fish

Description: This gene is a member of the iron/manganese superoxide dismutase family. It encodes a mitochondrial protein that forms a homotetramer and binds one manganese ion per subunit. This protein binds to the superoxide byproducts of oxidative phosphorylation and converts them to hydrogen peroxide and diatomic oxygen. Mutations in this gene have been associated with idiopathic cardiomyopathy (IDC), premature aging, sporadic motor neuron disease, and cancer. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.

Description: SOD3 is a member of the superoxide dismutase(SOD) protein family. SODs are antioxidant enzymes that catalyze the dismutation of two superoxide radicals into hydrogen peroxide and oxygen. This protein is thought to protect the brain, lungs, and other tissues from oxidative stress. The protein is secreted into the extracellular space and forms a glycosylated homotetramer that is anchored to the extracellular matrix (ECM) and cell surfaces through an interaction with heparan sulfate proteoglycan and collagen. A fraction of the protein is cleaved near the C-terminus before secretion to generate circulating tetramers that do not interact with the ECM.

Description: SOD3 (Superoxide Dismutase 3), also called Superoxide Dismutase extracellular, EC-SOD, and Cu-Zn, is an enzyme that in humans is encoded by the SOD3 gene. This gene encodes a member of the superoxide dismutase (SOD) protein family. SODs are antioxidant enzymes that catalyze the dismutation of two superoxide radicals into hydrogen peroxide and oxygen. Hendrickson et al. (1990) mapped the SOD3 gene to 4pter-q21 by a study of somatic cell hybrids. Stern et al. (2003) narrowed the assignment to 4p15.3-p15.1 by somatic cell and radiation hybrid analysis, linkage mapping, and FISH. The product of this gene is thought to protect the brain, lungs, and other tissues from oxidative stress. The protein is secreted into the extracellular space and forms a glycosylated homotetramer that is anchored to the extracellular matrix (ECM) and cell surfaces through an interaction with heparan sulfate proteoglycan and collagen. A fraction of the protein is cleaved near the C-terminus before secretion to generate circulating tetramers that do not interact with the ECM.

Description: Superoxide dismutases are a class of enzymes that catalyze the dismutation of superoxide into oxygen and hydrogen peroxide. As such, they are an important antioxidant defense in nearly all cells exposed to oxygen. One of the exceedingly rare exceptions is Lactobacillus plantarum and related lactobacilli, which use a different mechanism.Cu,Zn-SOD was found widely distributed in the cell cytosol and in the cell nucleus, consistent with it being a soluble cytosolic protein. Mitochondria and secretory compartments did not label for this protein. In human cells, peroxisomes showed a labeling density slightly less than that of cytoplasm.

Description: Superoxide Dismutase 2, also called IPO-B or MNSOD, is a mitochondrial matrix enzyme that scavenges oxygen radicals produced by the extensive oxidation-reduction and electron transport reactions occurring in mitochondria. This gene is a member of the iron/manganese superoxide dismutase family. Using a somatic cell hybrid panel containing different segments of chromosome 6, they demonstrated that SOD2 is located in the region 6q25.3-qter which, together with the FISH analysis, indicated that the enzyme is in the distal portion of 6q25. The gene encodes an intramitochondrial free radical scavenging enzyme that is the first line of defense against superoxide produced as a byproduct of oxidative phosphorylation. Adeno-associated viral delivery of the human gene resulted in suppression of optic nerve degeneration and rescue of retinal ganglion cells. The findings suggested that reactive oxygen species contributed to retinal cell death and optic nerve damage in mice with complex I deficiency, and that expression of SOD2 attenuated the disease process.

Description: Superoxide Dismutase 3 is an enzyme that in humans is encoded by the SOD3 gene. This gene encodes a member of the superoxide dismutase (SOD) protein family. SODs are antioxidant enzymes that catalyze the dismutation of two superoxide radicals into hydrogen peroxide and oxygen. Hendrickson et al.(1990) mapped the SOD3 gene to 4pter-q21 by a study of somatic cell hybrids. Stern et al.(2003) narrowed the assignment to 4p15.3-p15.1 by somatic cell and radiation hybrid analysis, linkage mapping, and FISH. The product of this gene is though to protect the brain, lungs, and other tissues from oxidative stress. The protein is secreted into the extracellular space and forms a glycosylated homotetramer that is anchored to the extracellular matrix(ECM) and cell surfaces through an interaction with heparan sulfate proteoglycan and collagen. A fraction of the protein is cleaved near the C-terminus before secretion to generate circulating tetramers that do not interact with the ECM.

Description: SOD3 (SUPEROXIDE DISMUTASE 3), also called SUPEROXIDE DISMUTASE, EXTRACELLULAR, EC-SOD, and Cu-Zn, is an enzyme that in humans is encoded by the SOD3 gene. This gene encodes a member of the superoxide dismutase (SOD) protein family. SODs are antioxidant enzymes that catalyze the dismutation of two superoxide radicals into hydrogen peroxide and oxygen. Hendrickson et al. (1990) mapped the SOD3 gene to 4pter-q21 by a study of somatic cell hybrids. Stern et al. (2003) narrowed the assignment to 4p15.3-p15.1 by somatic cell and radiation hybrid analysis, linkage mapping, and FISH. The product of this gene is thought to protect the brain, lungs, and other tissues from oxidative stress. The protein is secreted into the extracellular space and forms a glycosylated homotetramer that is anchored to the extracellular matrix (ECM) and cell surfaces through an interaction with heparan sulfate proteoglycan and collagen. A fraction of the protein is cleaved near the C-terminus before secretion to generate circulating tetramers that do not interact with the ECM.

Description: Superoxide dismutases (SOD) are a class of enzymes that catalyze the dismutation of superoxide into oxygen and hydrogen peroxide. As such, they are an important antioxidant defense in nearly all cells exposed to oxygen. One of the exceedingly rare exceptions is Lactobacillus plantarum and related lactobacilli, which use a different mechanism.Cu,Zn-SOD was found widely distributed in the cell cytosol and in the cell nucleus, consistent with it being a soluble cytosolic protein. Mitochondria and secretory compartments did not label for this protein. In human cells, peroxisomes showed a labeling density slightly less than that of cytoplasm.

Description: SOD2 (Superoxide Dismutase 2), also called IPO-B or MNSOD, is a mitochondrial matrix enzyme that scavenges oxygen radicals produced by the extensive oxidation-reduction and electron transport reactions occurring in mitochondria. This gene is a member of the iron/manganese superoxide dismutase family. Using a somatic cell hybrid panel containing different segments of chromosome 6, they demonstrated that SOD2 is located in the region 6q25.3-qter which, together with the FISH analysis, indicated that SOD2 is in the distal portion of 6q25. The SOD2 gene encodes an intramitochondrial free radical scavenging enzyme that is the first line of defense against superoxide produced as a byproduct of oxidative phosphorylation. Adeno-associated viral delivery of the human SOD2 gene resulted in suppression of optic nerve degeneration and rescue of retinal ganglion cells. The findings suggested that reactive oxygen species contributed to retinal cell death and optic nerve damage in mice with complex I deficiency, and that expression of SOD2 attenuated the disease process.

Description: SOD3 (SUPEROXIDE DISMUTASE 3), also called SUPEROXIDE DISMUTASE, EXTRACELLULAR, EC-SOD, and Cu-Zn, is an enzyme that in humans is encoded by the SOD3 gene. This gene encodes a member of the superoxide dismutase (SOD) protein family. SODs are antioxidant enzymes that catalyze the dismutation of two superoxide radicals into hydrogen peroxide and oxygen. Hendrickson et al. (1990) mapped the SOD3 gene to 4pter-q21 by a study of somatic cell hybrids. Stern et al. (2003) narrowed the assignment to 4p15.3-p15.1 by somatic cell and radiation hybrid analysis, linkage mapping, and FISH. The product of this gene is thought to protect the brain, lungs, and other tissues from oxidative stress. The protein is secreted into the extracellular space and forms a glycosylated homotetramer that is anchored to the extracellular matrix (ECM) and cell surfaces through an interaction with heparan sulfate proteoglycan and collagen. A fraction of the protein is cleaved near the C-terminus before secretion to generate circulating tetramers that do not interact with the ECM.

Description: SOD2 (Superoxide Dismutase 2), also called IPO-B or MNSOD, is a mitochondrial matrix enzyme that scavenges oxygen radicals produced by the extensive oxidation-reduction and electron transport reactions occurring in mitochondria. This gene is a member of the iron/manganese superoxide dismutase family. Using a somatic cell hybrid panel containing different segments of chromosome 6, they demonstrated that SOD2 is located in the region 6q25.3-qter which, together with the FISH analysis, indicated that SOD2 is in the distal portion of 6q25. The SOD2 gene encodes an intramitochondrial free radical scavenging enzyme that is the first line of defense against superoxide produced as a byproduct of oxidative phosphorylation. Adeno-associated viral delivery of the human SOD2 gene resulted in suppression of optic nerve degeneration and rescue of retinal ganglion cells. The findings suggested that reactive oxygen species contributed to retinal cell death and optic nerve damage in mice with complex I deficiency, and that expression of SOD2 attenuated the disease process.

Description: 'Superoxide dismutase [Mn], mitochondrial' destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. [UniProt]

Description: Cu-Zn superoxide dismutase-1 (SOD-1) is a well-characterized cytosolic scavenger of oxygen free radicals that requires copper and zinc binding to potentiate its enzymatic activity. Enzymatically, SOD-1 facilitates the dismutation of oxygen radicals to hydrogen peroxide and also catalyzes pro-oxidant reactions, which include the peroxidase activity and hydroxyl radical generating activity. SOD-1 is ubiquitously expressed in somatic cells and functions as a homodimer. Defects in the gene encoding SOD-1 have been implicated in the progression of neurological diseases, including amyotrophic lateral sclerosis (ALS), a neurodegenerative disease characterized by the loss of spinal motor neurons, Down syndrome and Alzheimer s disease. In familial ALS, several mutations in SOD-1 predominate, resulting in the loss of zinc binding, the loss of scavenging activity of SOD-1, and correlate with an increase in neurotoxicity and motor neuron death.

Description: Cu-Zn superoxide dismutase-1 (SOD-1) is a well-characterized cytosolic scavenger of oxygen free radicals that requires copper and zinc binding to potentiate its enzymatic activity. Enzymatically, SOD-1 facilitates the dismutation of oxygen radicals to hydrogen peroxide and also catalyzes pro-oxidant reactions, which include the peroxidase activity and hydroxyl radical generating activity. SOD-1 is ubiquitously expressed in somatic cells and functions as a homodimer. Defects in the gene encoding SOD-1 have been implicated in the progression of neurological diseases, including amyotrophic lateral sclerosis (ALS), a neurodegenerative disease characterized by the loss of spinal motor neurons, Down syndrome and Alzheimer s disease. In familial ALS, several mutations in SOD-1 predominate, resulting in the loss of zinc binding, the loss of scavenging activity of SOD-1, and correlate with an increase in neurotoxicity and motor neuron death.

Description: Cu-Zn superoxide dismutase-1 (SOD-1) is a well-characterized cytosolic scavenger of oxygen free radicals that requires copper and zinc binding to potentiate its enzymatic activity. Enzymatically, SOD-1 facilitates the dismutation of oxygen radicals to hydrogen peroxide and also catalyzes pro-oxidant reactions, which include the peroxidase activity and hydroxyl radical generating activity. SOD-1 is ubiquitously expressed in somatic cells and functions as a homodimer. Defects in the gene encoding SOD-1 have been implicated in the progression of neurological diseases, including amyotrophic lateral sclerosis (ALS), a neurodegenerative disease characterized by the loss of spinal motor neurons, Down syndrome and Alzheimer s disease. In familial ALS, several mutations in SOD-1 predominate, resulting in the loss of zinc binding, the loss of scavenging activity of SOD-1, and correlate with an increase in neurotoxicity and motor neuron death.

Description: Cu-Zn superoxide dismutase-1 (SOD-1) is a well-characterized cytosolic scavenger of oxygen free radicals that requires copper and zinc binding to potentiate its enzymatic activity. Enzymatically, SOD-1 facilitates the dismutation of oxygen radicals to hydrogen peroxide and also catalyzes pro-oxidant reactions, which include the peroxidase activity and hydroxyl radical generating activity. SOD-1 is ubiquitously expressed in somatic cells and functions as a homodimer. Defects in the gene encoding SOD-1 have been implicated in the progression of neurological diseases, including amyotrophic lateral sclerosis (ALS), a neurodegenerative disease characterized by the loss of spinal motor neurons, Down syndrome and Alzheimer s disease. In familial ALS, several mutations in SOD-1 predominate, resulting in the loss of zinc binding, the loss of scavenging activity of SOD-1, and correlate with an increase in neurotoxicity and motor neuron death.

Description: Cu-Zn superoxide dismutase-1 (SOD-1) is a well-characterized cytosolic scavenger of oxygen free radicals that requires copper and zinc binding to potentiate its enzymatic activity. Enzymatically, SOD-1 facilitates the dismutation of oxygen radicals to hydrogen peroxide and also catalyzes pro-oxidant reactions, which include the peroxidase activity and hydroxyl radical generating activity. SOD-1 is ubiquitously expressed in somatic cells and functions as a homodimer. Defects in the gene encoding SOD-1 have been implicated in the progression of neurological diseases, including amyotrophic lateral sclerosis (ALS), a neurodegenerative disease characterized by the loss of spinal motor neurons, Down syndrome and Alzheimer s disease. In familial ALS, several mutations in SOD-1 predominate, resulting in the loss of zinc binding, the loss of scavenging activity of SOD-1, and correlate with an increase in neurotoxicity and motor neuron death.