You Searched For: Copper

Catalog Number: (BOSSBS-1718R-CY3)

Supplier: Bioss

Description: Involved in the export of copper out of the cells, such as the efflux of hepatic copper into the bile.

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-1718R-CY5)

Supplier: Bioss

Description: Involved in the export of copper out of the cells, such as the efflux of hepatic copper into the bile.

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-2617R-FITC)

Supplier: Bioss

Description: Plays a role in the export of proteins that lack a signal peptide and are secreted by an alternative pathway. Binds two calcium ions per subunit. Binds one copper ion. Binding of one copper ion does not interfere with calcium binding. Required for the copper-dependent stress-induced export of IL1A and FGF1. The calcium-free protein binds to lipid vesicles containing phosphatidylserine, but not to vesicles containing phosphatidylcholine (By similarity).

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-2617R-CY5)

Supplier: Bioss

Description: Plays a role in the export of proteins that lack a signal peptide and are secreted by an alternative pathway. Binds two calcium ions per subunit. Binds one copper ion. Binding of one copper ion does not interfere with calcium binding. Required for the copper-dependent stress-induced export of IL1A and FGF1. The calcium-free protein binds to lipid vesicles containing phosphatidylserine, but not to vesicles containing phosphatidylcholine (By similarity).

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-2617R-A350)

Supplier: Bioss

Description: Plays a role in the export of proteins that lack a signal peptide and are secreted by an alternative pathway. Binds two calcium ions per subunit. Binds one copper ion. Binding of one copper ion does not interfere with calcium binding. Required for the copper-dependent stress-induced export of IL1A and FGF1. The calcium-free protein binds to lipid vesicles containing phosphatidylserine, but not to vesicles containing phosphatidylcholine (By similarity).

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-15458R)

Supplier: Bioss

Description: Hephaestin is a single-pass type I membrane protein that belongs to the multicopper oxidase family of proteins. Hephaestin, a copper-dependant ferroxidase protein, is crucial for iron exiting intestinal enterocytes into the circulation. It mediates the movement of iron across the basolateral membrane in conjunction with ferroportin 1. This is an important link between iron and copper metabolism in mammalian systems, as copper deficiency leads to reduced hephaestin and reduced iron absorption resulting in anemia. Hephaestin can bind six copper ions per monomer and is regulated by the homeobox transcription factor CDX2. Increased levels of iron leads to an increase in CDX2 expression and thus Hephaestin. Hephaestin is primarily detected in the intestine, but is also expressed in colon, breast, bone trabecural cells and fibroblasts.

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-2617R-A647)

Supplier: Bioss

Description: Plays a role in the export of proteins that lack a signal peptide and are secreted by an alternative pathway. Binds two calcium ions per subunit. Binds one copper ion. Binding of one copper ion does not interfere with calcium binding. Required for the copper-dependent stress-induced export of IL1A and FGF1. The calcium-free protein binds to lipid vesicles containing phosphatidylserine, but not to vesicles containing phosphatidylcholine (By similarity).

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-3896R-A350)

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.

UOM: 1 * 100 µl

Sale

Supplier: Thermo Fisher Scientific

Description: Stabilized with copper

SDS Certificates

Catalog Number: (22780.09)

Supplier: Thermo Fisher Scientific

Description: Dicopper selenide ≥99.5% (metals basis)

UOM: 1 * 10 g

SDS Certificates Sale

Catalog Number: (BOSSBS-2617R-A750)

Supplier: Bioss

Description: Plays a role in the export of proteins that lack a signal peptide and are secreted by an alternative pathway. Binds two calcium ions per subunit. Binds one copper ion. Binding of one copper ion does not interfere with calcium binding. Required for the copper-dependent stress-induced export of IL1A and FGF1. The calcium-free protein binds to lipid vesicles containing phosphatidylserine, but not to vesicles containing phosphatidylcholine (By similarity).

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-15458R-A647)

Supplier: Bioss

Description: Hephaestin is a single-pass type I membrane protein that belongs to the multicopper oxidase family of proteins. Hephaestin, a copper-dependant ferroxidase protein, is crucial for iron exiting intestinal enterocytes into the circulation. It mediates the movement of iron across the basolateral membrane in conjunction with ferroportin 1. This is an important link between iron and copper metabolism in mammalian systems, as copper deficiency leads to reduced hephaestin and reduced iron absorption resulting in anemia. Hephaestin can bind six copper ions per monomer and is regulated by the homeobox transcription factor CDX2. Increased levels of iron leads to an increase in CDX2 expression and thus Hephaestin. Hephaestin is primarily detected in the intestine, but is also expressed in colon, breast, bone trabecural cells and fibroblasts.

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-15458R-A680)

Supplier: Bioss

Description: Hephaestin is a single-pass type I membrane protein that belongs to the multicopper oxidase family of proteins. Hephaestin, a copper-dependant ferroxidase protein, is crucial for iron exiting intestinal enterocytes into the circulation. It mediates the movement of iron across the basolateral membrane in conjunction with ferroportin 1. This is an important link between iron and copper metabolism in mammalian systems, as copper deficiency leads to reduced hephaestin and reduced iron absorption resulting in anemia. Hephaestin can bind six copper ions per monomer and is regulated by the homeobox transcription factor CDX2. Increased levels of iron leads to an increase in CDX2 expression and thus Hephaestin. Hephaestin is primarily detected in the intestine, but is also expressed in colon, breast, bone trabecural cells and fibroblasts.

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-2617R-CY3)

Supplier: Bioss

Description: Plays a role in the export of proteins that lack a signal peptide and are secreted by an alternative pathway. Binds two calcium ions per subunit. Binds one copper ion. Binding of one copper ion does not interfere with calcium binding. Required for the copper-dependent stress-induced export of IL1A and FGF1. The calcium-free protein binds to lipid vesicles containing phosphatidylserine, but not to vesicles containing phosphatidylcholine (By similarity).

UOM: 1 * 100 µl

Sale

Supplier: Merck

Description: Quick tests for visual colour comparison.

SDS

Catalog Number: (ICNA114027112)

Supplier: MP Biomedicals

Description: YNB media, a component of synthetic defined yeast media is a well defined composition of salts, vitamins and nitrogen source for a vigorous growth of <i>S. cerevisiae</i>.

UOM: 1 * 227 g

Sale