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Manganese(II)+oxide
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Manganese(II)+oxide
Catalog Number:
(10387-394)
Supplier:
Bioss
Description:
PPP1A is a serine/threonine protein phosphatase catalytic subunit that is essential for regulating cellular stress responses in eukaryotes. It binds to magnesium or manganese ions and exists as a monomer. It is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. PPP1A is involved in the regulation long term synaptic plasticity and may play an important role in dephosphorylating substrates such as Ca2+/calmodulin dependent protein kinase II.
Catalog Number:
(89359-732)
Supplier:
Genetex
Description:
Superoxide dismutase (SOD) is responsible for the elimination of cytotoxic active oxygen by catalyzing the dismutation of the superoxide radical to oxygen and hydrogen peroxide. There are three SOD isoenzymes in mammalian cells. They are: extracellular SOD (EC SOD), copper and zinc-containing SOD (Cu/Zn SOD) and manganese-containing SOD (Mn SOD). The Cu/Zn form contains Cu and Zn ions and exists as a 32 kDa dimer in the cytosol. Mn SOD is an 80 kDa tetramer that contains Mn ion and resides in the mitochondrial matrix. Mn SOD is a tumor necrosis factor (TNF)-inducible enzyme that protects cells from TNF-mediated apoptosis via superoxide anion detoxification and the subsequent regulation of apoptosis through cytochrome c release and the modulation of the redox state of the mitochondria. Mn SOD has also been shown to be a tumor suppressor in human breast cancer. Overexpression of this enzyme protects neurons from NMDA- and nitric oxide-induced neurotoxicity.
Catalog Number:
(10387-388)
Supplier:
Bioss
Description:
PPP1A is a serine/threonine protein phosphatase catalytic subunit that is essential for regulating cellular stress responses in eukaryotes. It binds to magnesium or manganese ions and exists as a monomer. It is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. PPP1A is involved in the regulation long term synaptic plasticity and may play an important role in dephosphorylating substrates such as Ca2+/calmodulin dependent protein kinase II.
Catalog Number:
(10387-392)
Supplier:
Bioss
Description:
PPP1A is a serine/threonine protein phosphatase catalytic subunit that is essential for regulating cellular stress responses in eukaryotes. It binds to magnesium or manganese ions and exists as a monomer. It is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. PPP1A is involved in the regulation long term synaptic plasticity and may play an important role in dephosphorylating substrates such as Ca2+/calmodulin dependent protein kinase II.
Catalog Number:
(10387-396)
Supplier:
Bioss
Description:
PPP1A is a serine/threonine protein phosphatase catalytic subunit that is essential for regulating cellular stress responses in eukaryotes. It binds to magnesium or manganese ions and exists as a monomer. It is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. PPP1A is involved in the regulation long term synaptic plasticity and may play an important role in dephosphorylating substrates such as Ca2+/calmodulin dependent protein kinase II.
Catalog Number:
(10663-526)
Supplier:
Bioss
Description:
Arginase I which is expressed almost exclusively in the liver, catalyzes the conversion of arginine to ornithine and urea . The human arginase I gene, which maps to chromosome 6q23, encodes a 322 amino acid protein. Arginase I exists as a homotrimeric protein and contains a binuclear manganese cluster. Arginase II catalyzes the same reaction as arginase I, but differs in its tissue specificity and subcellular location. Specifically, arginase II localizes to the mitochondria. Arginase II is expressed in non-hepatic tissues, with the highest levels of expression in the kidneys, but, unlike arginase I, is not expressed in liver. The human arginase II gene, which maps to chromosome 14q24.1-q24.3, encodes a 354 amino acid protein. In addition, arginase II contains a putative amino-terminal mitochondrial localization sequence.
Catalog Number:
(10663-512)
Supplier:
Bioss
Description:
Arginase I which is expressed almost exclusively in the liver, catalyzes the conversion of arginine to ornithine and urea . The human arginase I gene, which maps to chromosome 6q23, encodes a 322 amino acid protein. Arginase I exists as a homotrimeric protein and contains a binuclear manganese cluster. Arginase II catalyzes the same reaction as arginase I, but differs in its tissue specificity and subcellular location. Specifically, arginase II localizes to the mitochondria. Arginase II is expressed in non-hepatic tissues, with the highest levels of expression in the kidneys, but, unlike arginase I, is not expressed in liver. The human arginase II gene, which maps to chromosome 14q24.1-q24.3, encodes a 354 amino acid protein. In addition, arginase II contains a putative amino-terminal mitochondrial localization sequence.
Catalog Number:
(89358-928)
Supplier:
Genetex
Description:
Superoxide dismutase (SOD) is responsible for the elimination of cytotoxic active oxygen by catalyzing the dismutation of the superoxide radical to oxygen and hydrogen peroxide. There are three SOD isoenzymes in mammalian cells. They are: extracellular SOD (EC SOD), copper and zinc-containing SOD (Cu/Zn SOD) and manganese-containing SOD (Mn SOD). The Cu/Zn form contains Cu and Zn ions and exists as a 32 kDa dimer in the cytosol. Mn SOD is an 80 kDa tetramer that contains Mn ion and resides in the mitochondrial matrix. Mn SOD is a tumor necrosis factor (TNF)-inducible enzyme that protects cells from TNF-mediated apoptosis via superoxide anion detoxification and the subsequent regulation of apoptosis through cytochrome c release and the modulation of the redox state of the mitochondria. Mn SOD has also been shown to be a tumor suppressor in human breast cancer. Overexpression of this enzyme protects neurons from NMDA- and nitric oxide-induced neurotoxicity.
Catalog Number:
(89359-696)
Supplier:
Genetex
Description:
Superoxide dismutase (SOD) is responsible for the elimination of cytotoxic active oxygen by catalyzing the dismutation of the superoxide radical to oxygen and hydrogen peroxide. There are three SOD isoenzymes in mammalian cells. They are: extracellular SOD (EC SOD), copper and zinc-containing SOD (CuZn SOD) and manganese-containing SOD (Mn SOD). The CuZn form contains Cu and Zn ions and exists as a 32 kDa dimer in the cytosol. Mn SOD is an 80 kDa tetramer that contains Mn ion and resides in the mitochondrial matrix. Mn SOD is a tumor necrosis factor (TNF)- inducible enzyme that protects cells from TNF-mediated apoptosis via superoxide anion detoxification and the subsequent regulation of apoptosis through cytochrome c release and the modulation of the redox state of the mitochondria. Mn SOD has also been shown to be a tumor suppressor in human breast cancer. Overexpression of this enzyme protects neurons from NMDA- and nitric oxide-induced neurotoxicity.
Catalog Number:
(76084-884)
Supplier:
Bioss
Description:
PPP1A is a serine/threonine protein phosphatase catalytic subunit that is essential for regulating cellular stress responses in eukaryotes. It binds to magnesium or manganese ions and exists as a monomer. It is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. PPP1A is involved in the regulation long term synaptic plasticity and may play an important role in dephosphorylating substrates such as Ca2+/calmodulin dependent protein kinase II.
Catalog Number:
(76109-472)
Supplier:
Bioss
Description:
Arginase I which is expressed almost exclusively in the liver, catalyzes the conversion of arginine to ornithine and urea . The human arginase I gene, which maps to chromosome 6q23, encodes a 322 amino acid protein. Arginase I exists as a homotrimeric protein and contains a binuclear manganese cluster. Arginase II catalyzes the same reaction as arginase I, but differs in its tissue specificity and subcellular location. Specifically, arginase II localizes to the mitochondria. Arginase II is expressed in non-hepatic tissues, with the highest levels of expression in the kidneys, but, unlike arginase I, is not expressed in liver. The human arginase II gene, which maps to chromosome 14q24.1-q24.3, encodes a 354 amino acid protein. In addition, arginase II contains a putative amino-terminal mitochondrial localization sequence.
Catalog Number:
(10663-524)
Supplier:
Bioss
Description:
Arginase I which is expressed almost exclusively in the liver, catalyzes the conversion of arginine to ornithine and urea . The human arginase I gene, which maps to chromosome 6q23, encodes a 322 amino acid protein. Arginase I exists as a homotrimeric protein and contains a binuclear manganese cluster. Arginase II catalyzes the same reaction as arginase I, but differs in its tissue specificity and subcellular location. Specifically, arginase II localizes to the mitochondria. Arginase II is expressed in non-hepatic tissues, with the highest levels of expression in the kidneys, but, unlike arginase I, is not expressed in liver. The human arginase II gene, which maps to chromosome 14q24.1-q24.3, encodes a 354 amino acid protein. In addition, arginase II contains a putative amino-terminal mitochondrial localization sequence.
Catalog Number:
(10663-528)
Supplier:
Bioss
Description:
Arginase I which is expressed almost exclusively in the liver, catalyzes the conversion of arginine to ornithine and urea . The human arginase I gene, which maps to chromosome 6q23, encodes a 322 amino acid protein. Arginase I exists as a homotrimeric protein and contains a binuclear manganese cluster. Arginase II catalyzes the same reaction as arginase I, but differs in its tissue specificity and subcellular location. Specifically, arginase II localizes to the mitochondria. Arginase II is expressed in non-hepatic tissues, with the highest levels of expression in the kidneys, but, unlike arginase I, is not expressed in liver. The human arginase II gene, which maps to chromosome 14q24.1-q24.3, encodes a 354 amino acid protein. In addition, arginase II contains a putative amino-terminal mitochondrial localization sequence.
Catalog Number:
(10663-532)
Supplier:
Bioss
Description:
Arginase I which is expressed almost exclusively in the liver, catalyzes the conversion of arginine to ornithine and urea . The human arginase I gene, which maps to chromosome 6q23, encodes a 322 amino acid protein. Arginase I exists as a homotrimeric protein and contains a binuclear manganese cluster. Arginase II catalyzes the same reaction as arginase I, but differs in its tissue specificity and subcellular location. Specifically, arginase II localizes to the mitochondria. Arginase II is expressed in non-hepatic tissues, with the highest levels of expression in the kidneys, but, unlike arginase I, is not expressed in liver. The human arginase II gene, which maps to chromosome 14q24.1-q24.3, encodes a 354 amino acid protein. In addition, arginase II contains a putative amino-terminal mitochondrial localization sequence.
Catalog Number:
(10663-530)
Supplier:
Bioss
Description:
Arginase I which is expressed almost exclusively in the liver, catalyzes the conversion of arginine to ornithine and urea . The human arginase I gene, which maps to chromosome 6q23, encodes a 322 amino acid protein. Arginase I exists as a homotrimeric protein and contains a binuclear manganese cluster. Arginase II catalyzes the same reaction as arginase I, but differs in its tissue specificity and subcellular location. Specifically, arginase II localizes to the mitochondria. Arginase II is expressed in non-hepatic tissues, with the highest levels of expression in the kidneys, but, unlike arginase I, is not expressed in liver. The human arginase II gene, which maps to chromosome 14q24.1-q24.3, encodes a 354 amino acid protein. In addition, arginase II contains a putative amino-terminal mitochondrial localization sequence.
Catalog Number:
(76109-470)
Supplier:
Bioss
Description:
Arginase I which is expressed almost exclusively in the liver, catalyzes the conversion of arginine to ornithine and urea . The human arginase I gene, which maps to chromosome 6q23, encodes a 322 amino acid protein. Arginase I exists as a homotrimeric protein and contains a binuclear manganese cluster. Arginase II catalyzes the same reaction as arginase I, but differs in its tissue specificity and subcellular location. Specifically, arginase II localizes to the mitochondria. Arginase II is expressed in non-hepatic tissues, with the highest levels of expression in the kidneys, but, unlike arginase I, is not expressed in liver. The human arginase II gene, which maps to chromosome 14q24.1-q24.3, encodes a 354 amino acid protein. In addition, arginase II contains a putative amino-terminal mitochondrial localization sequence.
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Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the
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