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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


Catalog Number: (BOSSBS-3577R-CY3)
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.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-3896R)
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


Catalog Number: (BOSSBS-15436R-CY5)
Supplier: Bioss
Description: HEAB is a 425 amino acid nuclear protein that belongs to the Clp1 family. Utilising magnesium, manganese or nickel as cofactors, HEAB participates in the phosphorylation of the 5'-hydroxyl groups of double- and single- stranded RNA and DNA. HEAB is a member of the tRNA splicing endonuclease complex, in conjunction with TSEN2, TSEN15, TSEN34 and TSEN54, and is also a member of the pre-mRNA cleavage complex II. The gene encoding HEAB maps to human chromosome 11q12.1 and mouse chromosome 2 D; mutations to this gene may lead to a reduced pre-mRNA cleavage activity. HEAB exists as two isoforms due to alternative splicing events.
UOM: 1 * 100 µl


Supplier: Thermo Fisher Scientific
Description: NaF in H₂O; MDL No.: MFCD00144315
Catalog Number: (BOSSBS-3577R-A488)
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.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-15436R-FITC)
Supplier: Bioss
Description: HEAB is a 425 amino acid nuclear protein that belongs to the Clp1 family. Utilising magnesium, manganese or nickel as cofactors, HEAB participates in the phosphorylation of the 5'-hydroxyl groups of double- and single- stranded RNA and DNA. HEAB is a member of the tRNA splicing endonuclease complex, in conjunction with TSEN2, TSEN15, TSEN34 and TSEN54, and is also a member of the pre-mRNA cleavage complex II. The gene encoding HEAB maps to human chromosome 11q12.1 and mouse chromosome 2 D; mutations to this gene may lead to a reduced pre-mRNA cleavage activity. HEAB exists as two isoforms due to alternative splicing events.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-15436R-CY7)
Supplier: Bioss
Description: HEAB is a 425 amino acid nuclear protein that belongs to the Clp1 family. Utilising magnesium, manganese or nickel as cofactors, HEAB participates in the phosphorylation of the 5'-hydroxyl groups of double- and single- stranded RNA and DNA. HEAB is a member of the tRNA splicing endonuclease complex, in conjunction with TSEN2, TSEN15, TSEN34 and TSEN54, and is also a member of the pre-mRNA cleavage complex II. The gene encoding HEAB maps to human chromosome 11q12.1 and mouse chromosome 2 D; mutations to this gene may lead to a reduced pre-mRNA cleavage activity. HEAB exists as two isoforms due to alternative splicing events.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-3756R-FITC)
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.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-8585R-CY3)
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.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-8585R-A750)
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 localises 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 localisation sequence.
UOM: 1 * 100 µl


Supplier: Merck
Description: Manganese, powder, Sigma-Aldrich®

Catalog Number: (BOSSBS-8585R-A350)
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.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13273R-A647)
Supplier: Bioss
Description: The UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes are substrate-specific proteins that catalyze the transfer of GalNAc (N-acetylgalactosamine) to serine and threonine residues onto various proteins, thereby initiating mucin-type O-linked glycosylation in the Golgi apparatus. GalNAc-T1, also known as GALNT1 (Polypeptide N-acetylgalactosaminyltransferase 1), is a ubiquitously expressed 559 amino acid single-pass type II membrane protein that localizes to the Golgi apparatus and, like other GalNAc-Ts, contains a stem region and a C-terminal ricin/lectin-like domain. GalNAc-T1 catalyzes the first reaction in O-linked oligosaccharide biosynthesis, namely the transfer of an N-acetyl-D-galactosamine residue to a protein acceptor. GalNAc-T1 uses calcium and manganese as cofactors. Due to alternative splicing events, two GalNAc-T1 isoforms are expressed.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13271R-A555)
Supplier: Bioss
Description: The UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes are substrate-specific proteins that catalyze the transfer of GalNAc (N-acetylgalactosamine) to serine and threonine residues onto various proteins, thereby initiating mucin-type O-linked glycosylation in the Golgi apparatus. GalNAc-T11 (Polypeptide N-acetylgalactosaminyltransferase 11), also known as UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11, is a 608 amino acid protein that catalyzes glycosylation of Muc1, Muc4.1 and EA2, though it does not display enzymatic preference for erythropoitein. The N-terminal domain is involved in substrate binding and manganese coordination, while the C-terminal domain is involved in UDP-Gal binding and catalytic reaction. GalNAc-T11 is highly expressed in kidney tubules, though it is not expressed in glomeruli. There are two isoforms of GalNAc-T11 that are produced as a result of alternative splicing events.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13273R-A555)
Supplier: Bioss
Description: The UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes are substrate-specific proteins that catalyze the transfer of GalNAc (N-acetylgalactosamine) to serine and threonine residues onto various proteins, thereby initiating mucin-type O-linked glycosylation in the Golgi apparatus. GalNAc-T1, also known as GALNT1 (Polypeptide N-acetylgalactosaminyltransferase 1), is a ubiquitously expressed 559 amino acid single-pass type II membrane protein that localizes to the Golgi apparatus and, like other GalNAc-Ts, contains a stem region and a C-terminal ricin/lectin-like domain. GalNAc-T1 catalyzes the first reaction in O-linked oligosaccharide biosynthesis, namely the transfer of an N-acetyl-D-galactosamine residue to a protein acceptor. GalNAc-T1 uses calcium and manganese as cofactors. Due to alternative splicing events, two GalNAc-T1 isoforms are expressed.
UOM: 1 * 100 µl


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