You Searched For: Aluminium+lanthanum+(III)+oxide


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Supplier: Thermo Fisher Scientific
Description: Intermediate activity flux. Suitable for aluminosilicates and calcareous refractories. Often used in testing of cement and steel. Samples must be fully oxidized
Spectroflux 110, Lithium tetraborate & Lithium metaborate, 66.5:33.5 w/w% is used to dissolve aluminosilicates ranging from 100% silicon dioxide to 100% aluminum(III) oxide. It has intermediate acidity and suitable for aluminosilicates and calcareous refractories.
Catalog Number: (BOSSBS-12448R)
Supplier: Bioss
Description: The alcohol dehydrogenase family of proteins metabolize a wide variety of substrates, including retinol, hydroxysteroids, ethanol, aliphatic alcohols and lipid peroxidation products. ADH5 (alcohol dehydrogenase 5 (class III)), also known as FDH (formaldehyde dehydrogenase), ADHX, ADH-3 or GSNOR, is a 374 amino acid cytoplasmic protein that belongs to the class III subfamily of alcohol dehydrogenases. Expressed ubiquitously, ADH5 uses iron as a cofactor to catalytically oxidize both long-chain primary alcohols and S-hydroxymethyl-glutathione, a product formed spontaneously between formaldehyde and glutathione. ADH5 exists as a homodimer and, via its ability to oxidize S-hydroxymethyl-glutathione and, thus, eliminate formaldehyde, functions as an important component of cellular metabolism. Genetic variations in the gene encoding ADH5 may affect drug and alcohol dependence in humans.
UOM: 1 * 100 µl


Catalog Number: (ACRO463350010)
Supplier: Thermo Fisher Scientific
Description: Aluminium oxide basic Brockmann Grade I 50-200 µm, 90A for chromatography
UOM: 1 * 1 kg


Catalog Number: (ACRO190410010)
Supplier: Thermo Fisher Scientific
Description: Aluminium oxide neutral Brockmann Grade I 50-200 µm, 90A for chromatography
UOM: 1 * 1 kg


Catalog Number: (BOSSBS-12448R-CY3)
Supplier: Bioss
Description: The alcohol dehydrogenase family of proteins metabolize a wide variety of substrates, including retinol, hydroxysteroids, ethanol, aliphatic alcohols and lipid peroxidation products. ADH5 (alcohol dehydrogenase 5 (class III)), also known as FDH (formaldehyde dehydrogenase), ADHX, ADH-3 or GSNOR, is a 374 amino acid cytoplasmic protein that belongs to the class III subfamily of alcohol dehydrogenases. Expressed ubiquitously, ADH5 uses iron as a cofactor to catalytically oxidize both long-chain primary alcohols and S-hydroxymethyl-glutathione, a product formed spontaneously between formaldehyde and glutathione. ADH5 exists as a homodimer and, via its ability to oxidize S-hydroxymethyl-glutathione and, thus, eliminate formaldehyde, functions as an important component of cellular metabolism. Genetic variations in the gene encoding ADH5 may affect drug and alcohol dependence in humans.
UOM: 1 * 100 µl


Supplier: ENZO LIFE SCIENCES
Description: Cell permeable peptide that blocks eNOS (NOS III) activity and cellular nitric oxide (NO) release in vitro and reduces inflammation and tumorigenesis in vivo. Caveolin-1 interacts with several lipid-modified signalling ligands, such as EGFR, eNOS, G-protein α-subunits, PKCα, H-Ras, and Src, via the C1-SD82-101 sequence.

Catalog Number: (MOLE53253597-1KG)
Supplier: Molekula
Description: Aluminium chloride
UOM: 1 * 1 kg


Supplier: Merck
Description: Aluminium chloride, Sigma-Aldrich®

Supplier: Roth Carl
Description: Aluminium sulphate hydrate

Catalog Number: (BOSSBS-12448R-CY5)
Supplier: Bioss
Description: The alcohol dehydrogenase family of proteins metabolize a wide variety of substrates, including retinol, hydroxysteroids, ethanol, aliphatic alcohols and lipid peroxidation products. ADH5 (alcohol dehydrogenase 5 (class III)), also known as FDH (formaldehyde dehydrogenase), ADHX, ADH-3 or GSNOR, is a 374 amino acid cytoplasmic protein that belongs to the class III subfamily of alcohol dehydrogenases. Expressed ubiquitously, ADH5 uses iron as a cofactor to catalytically oxidize both long-chain primary alcohols and S-hydroxymethyl-glutathione, a product formed spontaneously between formaldehyde and glutathione. ADH5 exists as a homodimer and, via its ability to oxidize S-hydroxymethyl-glutathione and, thus, eliminate formaldehyde, functions as an important component of cellular metabolism. Genetic variations in the gene encoding ADH5 may affect drug and alcohol dependence in humans.
UOM: 1 * 100 µl


Catalog Number: (SIAL450308-5G)
Supplier: Merck
Description: Aluminium sulphate hydrate, Sigma-Aldrich®
UOM: 1 * 5 g


Supplier: Merck
Description: Aluminium sulphate hydrate, Sigma-Aldrich®

Catalog Number: (BOSSBS-12448R-A555)
Supplier: Bioss
Description: The alcohol dehydrogenase family of proteins metabolize a wide variety of substrates, including retinol, hydroxysteroids, ethanol, aliphatic alcohols and lipid peroxidation products. ADH5 (alcohol dehydrogenase 5 (class III)), also known as FDH (formaldehyde dehydrogenase), ADHX, ADH-3 or GSNOR, is a 374 amino acid cytoplasmic protein that belongs to the class III subfamily of alcohol dehydrogenases. Expressed ubiquitously, ADH5 uses iron as a cofactor to catalytically oxidize both long-chain primary alcohols and S-hydroxymethyl-glutathione, a product formed spontaneously between formaldehyde and glutathione. ADH5 exists as a homodimer and, via its ability to oxidize S-hydroxymethyl-glutathione and, thus, eliminate formaldehyde, functions as an important component of cellular metabolism. Genetic variations in the gene encoding ADH5 may affect drug and alcohol dependence in humans.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12448R-FITC)
Supplier: Bioss
Description: The alcohol dehydrogenase family of proteins metabolize a wide variety of substrates, including retinol, hydroxysteroids, ethanol, aliphatic alcohols and lipid peroxidation products. ADH5 (alcohol dehydrogenase 5 (class III)), also known as FDH (formaldehyde dehydrogenase), ADHX, ADH-3 or GSNOR, is a 374 amino acid cytoplasmic protein that belongs to the class III subfamily of alcohol dehydrogenases. Expressed ubiquitously, ADH5 uses iron as a cofactor to catalytically oxidize both long-chain primary alcohols and S-hydroxymethyl-glutathione, a product formed spontaneously between formaldehyde and glutathione. ADH5 exists as a homodimer and, via its ability to oxidize S-hydroxymethyl-glutathione and, thus, eliminate formaldehyde, functions as an important component of cellular metabolism. Genetic variations in the gene encoding ADH5 may affect drug and alcohol dependence in humans.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-9095R-A680)
Supplier: Bioss
Description: Members of the class-III pyridoxal-phosphate-dependent aminotransferase family, such as AGXT2, catalyze the conversion of glyoxylate to glycine using L-alanine as the amino donor. AGXT2 protects from asymmetric dimethylarginine (ADMA)-induced inhibition in nitric oxide (NO) production. Elevated blood concentrations of ADMA, a methyl derivate of the amino acid arginine and an endogenous inhibitor of nitric oxide (NO) synthase, is produced by the physiological degradation of methylated proteins and is found in association with diabetes, hypertension, congestive heart failure and atherosclerosis. AGXT2L2 (alanine-glyoxylate aminotransferase 2-like 2) is a 450 amino acid pyridoxal phosphate that exists as a homotetramer. Belonging to the class-III pyridoxal-phosphate-dependent aminotransferase family, AGXT2L2 localises to the mitochondria and exists as three alternatively spliced isoforms. Encoded by a gene located on human chromosome 5q35.3, AGXT2L2 may have similar functions as AGXT2.
UOM: 1 * 100 µl


Catalog Number: (MOLE51729606-1KG)
Supplier: Molekula
Description: Aluminium isopropoxide
UOM: 1 * 1 kg


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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 call is still displayed and you need assistance, please call us at +43 1 97002 - 0.
Dual use goods can only be delivered within the European Union.
Dual use goods can only be delivered within the European Union.
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The original product is no longer available. The replacement shown is available.
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