You Searched For: Manganese+(IV)+telluride

Catalog Number: (CA97013-302)

Supplier: PerkinElmer

Description: Series N30502XX Lumina™ 2" (50 mm) diameter multi-element lamps are designed to be used with the PinAAcle™ and AAnalyst™ Atomic Absorption spectrometer series of instruments.

Supplier: Thermo Scientific Chemicals

Description: For the colorimetric determination of Mn (oxidizes manganese compounds to permanganates), as oxidizing agent

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Supplier: Thermo Scientific Chemicals

Description: Bromopentacarbonylmanganese(I) ≥98%

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Catalog Number: (76085-288)

Supplier: Bioss

Description: Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3). SOD1 is found in all eukaryotic species as a homodimeric 32 kDa enzyme containing one each of Cu and Zn ion per subunit. The manganese containing 80 kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain. SOD3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways. SOD4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor.

Supplier: PHOTRON PTY LTD.

Description: Hollow cathode lamps produced by Photron are designed and manufactured to achieve all of the following fundamental requirements for a spectral line source: Intense emission of resonance (ground state derived) lines. Narrow line width, for maximum sensitivity and linearity. Minimal spectral interference from continuum emission, present in the cathode. Rapid warm up to produce stable long term light emission. Noise free operation. Long running life and a 5 year shelf life. Cathode materials and geometry achieve a combination of spectral purity and a suitable sputtering rate. (A high sputtering rate will give high intensity at the expense of lamp life, sensitivity and linearity).

Catalog Number: (10373-608)

Supplier: Bioss

Description: Important in metal transport, in particular iron. Can also transport manganese, cobalt, cadmium, nickel, vanadium and lead. Involved in apical iron uptake into duodenal enterocytes. Involved in iron transport from acidified endosomes into the cytoplasm of erythroid precursor cells. May play an important role in hepatic iron accumulation and tissue iron distribution. May serve to import iron into the mitochondria.

Catalog Number: (76120-198)

Supplier: Bioss

Description: Metalloprotease that acts as a negative regulator of the Wnt signaling pathway by mediating the cleavage of the 8 N-terminal residues of a subset of Wnt proteins. Following cleavage, Wnt proteins become oxidized and form large disulfide-bond oligomers, leading to their inactivation. Able to cleave WNT3A, WNT5, but not WNT11. Required for head formation. [COFACTOR] Divalent metal cations. Manganese or cobalt.

Catalog Number: (75790-716)

Supplier: Prosci

Description: Methionine Aminopeptidase 1D (METAP1D) is a mitochondrion protein that belongs to the peptidase M24A family. METAP1D is overexpressed at the protein level in colon cancer cell lines and colon tumors as compared to normal tissues. N-terminal methionine removal is an important cellular process required for proper biological activity, subcellular localization, and eventual degradation of many proteins. METAP1D is also active with zinc, manganese or divalent ions. It may also play an important role in colon tumorigenesis.

Catalog Number: (10389-498)

Supplier: Bioss

Description: Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3). SOD1 is found in all eukaryotic species as a homodimeric 32 kDa enzyme containing one each of Cu and Zn ion per subunit. The manganese containing 80 kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain. SOD3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways. SOD4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor.

Catalog Number: (10389-496)

Supplier: Bioss

Description: Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3). SOD1 is found in all eukaryotic species as a homodimeric 32 kDa enzyme containing one each of Cu and Zn ion per subunit. The manganese containing 80 kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain. SOD3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways. SOD4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor.

Supplier: Thermo Scientific Chemicals

Description: Manganese testing in iron, steel, ores

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Catalog Number: (76084-430)

Supplier: Bioss

Description: Important in metal transport, in particular iron. Can also transport manganese, cobalt, cadmium, nickel, vanadium and lead. Involved in apical iron uptake into duodenal enterocytes. Involved in iron transport from acidified endosomes into the cytoplasm of erythroid precursor cells. May play an important role in hepatic iron accumulation and tissue iron distribution. May serve to import iron into the mitochondria.

Catalog Number: (76084-886)

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: (10096-606)

Supplier: Proteintech

Description: SLC39A8 also known as ZIP8 belongs to the ZIP family of metal ion transporters which function to transport zinc and/or other metal ion substrates from the extracellular space or organellar lumen into the cytoplasm. Recently it was found that Zip8 expression is upregulated in human monocytes in response to LPS, TNF-α, and live bacteria, facilitating cytoprotection during the early inflammation. Besides zinc ZIP8 can also transport cadmium and manganese efficiently. It is predicted that ZIP8 contains 3 potential N-linked glycosylation sites and is subject to glycosylation, which may account for the presences of multiple molecular weights.

Supplier: Hach

Description: For determination of low level manganese by the PAN method

Catalog Number: (10389-502)

Supplier: Bioss

Description: Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3). SOD1 is found in all eukaryotic species as a homodimeric 32 kDa enzyme containing one each of Cu and Zn ion per subunit. The manganese containing 80 kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain. SOD3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways. SOD4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor.