NAD Separopore® (Agarose) 4B-CL (Lyophilized)

Applications:

NAD covalently bound to Separopore has a high affinity for NAD-dependent enzymes and dehydrogenases. NAD-Separopore 4B-CL has been used to purify Vibrio cholerae toxin, diptheria toxin and other NAD binding proteins.

Technical Specifications:

• Ligand: NAD
• Matrix: Separopore 4B-CL (crosslinked agarose beads, 4%)
• Particle size range: 52 - 165 µm
• Matrix activation: Cyanogen bromide
• Matrix attachment: N-6
• Ligand density: 2 µmol NAD / ml drained gel
• pH stability: 4 - 10
• Storage: -20 C
• Supplied as lyophilized powder stabilized with lactose
• Swelling: 1 g swells to approximately 5 ml

References:

• Purification of the poly-ADP-ribose polymerase-like thermozyme from the archaeon Sulfolobus solfataricus. Methods Mol Biol. (2011) 780: 443-60.
• Allosteric behaviour of 1:5 hybrids of mutant subunits of Clostridium symbiosum glutamate dehydrogenase differing in their amino acid specificity. Biochem J. (2001) 360: 651-6.
• The staphylococcal transferrin-binding protein is a cell wall glyceraldehyde-3-phosphate dehydrogenase. Infect Immun. (1999) 67: 1086-92.
• Purification and biochemical characterization of a poly(ADP-ribose) polymerase-like enzyme from the thermophilic archaeon Sulfolobus solfataricus. Biochem J. (1998) 335: 441-7.
• Use of protein engineering to explore subunit interactions in an allosteric enzyme: construction of inter-subunit hybrids in Clostridium symbiosum glutamate dehydrogenase. Protein Eng. (1998) 11: 569-75.
• Purification of NAD-dependent mannitol dehydrogenase from celery suspension cultures. Plant Physiol. (1995) 108: 1219-25.
• Evidence for the presence of two pyridine nucleotide-binding sites on the beta subunit of the Escherichia coli pyridine nucleotide transhydrogenase. Biochem Mol Biol Int. (1995) 35: 297-306.
• Purification and partial characterization of microsomal NADH-cytochrome b5 reductase from higher plant Catharanthus roseus. Biochem Biophys Res Commun. (1993) 197: 518-22.
• A mutation at Gly314 of the beta subunit of the Escherichia coli pyridine nucleotide transhydrogenase abolishes activity and affects the NADP(H)-induced conformational change. Eur J Biochem. (1992) 207: 733-9.
• Mechanistic studies of the biosynthesis of 3,6-dideoxyhexoses in Yersinia pseudotuberculosis. Purification and stereochemical analysis of CDP-D-glucose oxidoreductase. J Biol Chem. (1992) 267: 5868-75.
• Topological analysis of the pyridine nucleotide transhydrogenase of Escherichia coli using proteolytic enzymes. Biochim Biophys Acta. (1991) 1080: 19-28.
• Purification and characterization of NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase from porcine kidney. Biochim Biophys Acta. (1990) 1035: 190-6.
• Glyceraldehyde-3-phosphate dehydrogenase is a major protein associated with the plasma membrane of retinal photoreceptor outer segments. J Biol Chem. (1990) 265: 13308-13.
• Human aldehyde dehydrogenase. Purification and characterization of a third isozyme with low Km for gamma-aminobutyraldehyde. J Biol Chem. (1989) 264: 4715-21.
• A menadione-stimulated pyridine nucleotide oxidase from resting bovine neutrophil membranes. Purification, properties, and immunochemical cross-reactivity with the human neutrophil NADPH oxidase. J Biol Chem. (1988) 263: 11657-63.
• Purification and characterization of two types of NADH-quinone reductase from Thermus thermophilus HB-8. Biochemistry. (1988) 27: 2008-13.
• Amino acid specific ADP-ribosylation: specific NAD: arginine mono-ADP-ribosyltransferases associated with turkey erythrocyte nuclei and plasma membranes. Biochemistry. (1986) 25: 8057-62.
• Purification and characterization of NADH dehydrogenase complex from Paracoccus denitrificans. Arch Biochem Biophys. (1986) 250: 302-11.
• Mitochondrial nicotinamide nucleotide transhydrogenase: nonidentical modification by N,N'-dicyclohexylcarbodiimide and N-(ethoxycarbonyl)-2-ethoxy-1,2-dihydroquinoline at the NAD(H) binding site. Arch Biochem Biophys. (1985) 243: 298-304.
• Purification and characterization of the secondary alcohol dehydrogenase from propane-utilizing Mycobacterium vaccae strain JOB-5. J Gen Microbiol. (1985) 131: 2901-7.

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Usage : bioWORLD's products are supplied for LABORATORY RESEARCH USE ONLY. The product may not be used as a drug, agricultural or pesticidal product , food additive or as a household chemical.