ATP Separopore® 4B-CL
€0.00
In stock
SKU
BW-20181080
Application:
Adenosine 5'-triphosphate (ATP)-Separopore® 4B-CL is used in the purification of ATP binding proteins. Any protein with an accessible ATP-binding domain will bind to ATP- Separopore® 4B-CL, regardless of activation state. The activated proteins will bind to ATP-Separopore® 4B-CL with higher affinity than the corresponding inactivated protein. This is important when purifying proteins from crude fractions where protein concentration is low, as this prevents non-specific binding. Better recovery and yields may be obtained when the ATP-Separopore® 4B-CL purification is followed by ion exchange chromatography.
The production method involves alkylation of the nucleotide, ATP followed by alkaline rearrangement to yield the corresponding N6-carboxymethyl derivative with subsequent condensation using 1,6-diaminohexane to give N6-[(6-aminohexyl)carbamoylmethyl)].
Note: Separopore® is a cost-effective equivalent to Sepharose® in all of its physical properties and binding characteristics.
Technical Specification:
Ligand: ATP
Matrix: Separapore® 4B-CL (crosslinked agarose beads, 4%)
Particle size range: 52 – 165 μm
Matrix activation: Cyanogen bromide
Ligand density: 2 – 5 ATP μmol / ml drained gel
Attachment: N6 of the purine ring
Spacer: 11 atoms
Supplied as lyophilized powder, 1g powder yields 8 – 10 ml of gel
References:
Chemoproteomic characterization of protein kinase inhibitors using immobilized ATP. Methods Mol Biol. (2012) 795: 119-34.
Heme-dependent activation of neuronal nitric oxide synthase by cytosol is due to an Hsp70-dependent, thioredoxin-mediated thiol-disulfide interchange in the heme/substrate binding cleft. Biochemistry. (2011) 50: 7146-56.
6-Alkylsalicylic acid analogues inhibit in vitro ATPase activity of heat shock protein 90. Arch Pharm Res. (2010) 33: 1997-2001.
Dominant-negative Hsp90 reduces VEGF-stimulated nitric oxide release and migration in endothelial cells. Arterioscler Thromb Vasc Biol. (2008) 28: 105-11.
Structural basis for depletion of heat shock protein 90 client proteins by deguelin. J Natl Cancer Inst. (2007) 99: 949-61.
Improved performance of column chromatography by arginine: dye-affinity chromatography. Protein Expr Purif. (2007) 52: 410-4.
Unusual properties of the prespore-specific enzyme, UDPgalactose:polysaccharide galactosyl transferase, of Dictyostelium discoideum. J Basic Microbiol. (2004) 44: 459-70.
Discovery of novel targets of quinoline drugs in the human purine binding proteome. Mol Pharmacol. (2002) 62: 1364-72.
Characterization of the 105-kDa molecular chaperone. Identification, biochemical properties, and localization. Eur J Biochem. (2002) 269: 5632-41.
Selected BTB/POZ-kelch proteins bind ATP. FEBS Lett. (2002) 516: 20-6.
Cloning, sequencing, expression, and purification of the C isozyme of mouse phosphofructokinase. Protein Expr Purif. (1999) 16: 448-53.
Secretory immunoglobulin A from human milk catalyzes milk protein phosphorylation. Appl Biochem Biotechnol. (1998) 75: 77-91.
Identification and characterization of individual cyclin-dependent kinase complexes from Saccharomyces cerevisiae. Yeast. (1999) 15: 295-309.
Molecular shape and ATP binding activity of rat p50, a putative mammalian homologue of RuvB DNA helicase. J Biochem. (1999) 125: 487-94.
Rapid identification of protein phosphatase 1-binding proteins by mixed peptide sequencing and data base searching. Characterization of a novel holoenzymic form of protein phosphatase 1. J Biol Chem. (1998) 273: 24396-405.
A nucleotide-binding domain of porcine liver annexin VI. Proteolysis of annexin VI labelled with 8-azido-ATP, purification by affinity chromatography on ATP-agarose, and fluorescence studies. Mol Cell Biochem. (1998) 181: 11-20.
Rapid purification and characterization of nucleoside diphosphate kinase isoforms using ATP-sepharose affinity column chromatography. Mol Cells. (1997) 7: 630-4.
Novel 30 kDa protein possessing ATP-binding and chaperone activities. Biochem J. (1997) 326: 567-72.
Interaction of annexins IV and VI with ATP. An alternative mechanism by which a cellular function of these calcium- and membrane-binding proteins is regulated. FEBS Lett. (1997) 409: 300-6.
Phosphorylation of different human milk proteins by human catalytic secretory immunoglobulin A. Biochem Mol Biol Int. (1996) 39: 521-7.
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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.
Hazmat Shipping: Non-hazardous
Storage: -20°C
Appearance Form: Powder
Appearance Color: White
Brand Name: bioPLUS™, Separopore™
Adenosine 5'-triphosphate (ATP)-Separopore® 4B-CL is used in the purification of ATP binding proteins. Any protein with an accessible ATP-binding domain will bind to ATP- Separopore® 4B-CL, regardless of activation state. The activated proteins will bind to ATP-Separopore® 4B-CL with higher affinity than the corresponding inactivated protein. This is important when purifying proteins from crude fractions where protein concentration is low, as this prevents non-specific binding. Better recovery and yields may be obtained when the ATP-Separopore® 4B-CL purification is followed by ion exchange chromatography.
The production method involves alkylation of the nucleotide, ATP followed by alkaline rearrangement to yield the corresponding N6-carboxymethyl derivative with subsequent condensation using 1,6-diaminohexane to give N6-[(6-aminohexyl)carbamoylmethyl)].
Note: Separopore® is a cost-effective equivalent to Sepharose® in all of its physical properties and binding characteristics.
Technical Specification:
Ligand: ATP
Matrix: Separapore® 4B-CL (crosslinked agarose beads, 4%)
Particle size range: 52 – 165 μm
Matrix activation: Cyanogen bromide
Ligand density: 2 – 5 ATP μmol / ml drained gel
Attachment: N6 of the purine ring
Spacer: 11 atoms
Supplied as lyophilized powder, 1g powder yields 8 – 10 ml of gel
References:
Chemoproteomic characterization of protein kinase inhibitors using immobilized ATP. Methods Mol Biol. (2012) 795: 119-34.
Heme-dependent activation of neuronal nitric oxide synthase by cytosol is due to an Hsp70-dependent, thioredoxin-mediated thiol-disulfide interchange in the heme/substrate binding cleft. Biochemistry. (2011) 50: 7146-56.
6-Alkylsalicylic acid analogues inhibit in vitro ATPase activity of heat shock protein 90. Arch Pharm Res. (2010) 33: 1997-2001.
Dominant-negative Hsp90 reduces VEGF-stimulated nitric oxide release and migration in endothelial cells. Arterioscler Thromb Vasc Biol. (2008) 28: 105-11.
Structural basis for depletion of heat shock protein 90 client proteins by deguelin. J Natl Cancer Inst. (2007) 99: 949-61.
Improved performance of column chromatography by arginine: dye-affinity chromatography. Protein Expr Purif. (2007) 52: 410-4.
Unusual properties of the prespore-specific enzyme, UDPgalactose:polysaccharide galactosyl transferase, of Dictyostelium discoideum. J Basic Microbiol. (2004) 44: 459-70.
Discovery of novel targets of quinoline drugs in the human purine binding proteome. Mol Pharmacol. (2002) 62: 1364-72.
Characterization of the 105-kDa molecular chaperone. Identification, biochemical properties, and localization. Eur J Biochem. (2002) 269: 5632-41.
Selected BTB/POZ-kelch proteins bind ATP. FEBS Lett. (2002) 516: 20-6.
Cloning, sequencing, expression, and purification of the C isozyme of mouse phosphofructokinase. Protein Expr Purif. (1999) 16: 448-53.
Secretory immunoglobulin A from human milk catalyzes milk protein phosphorylation. Appl Biochem Biotechnol. (1998) 75: 77-91.
Identification and characterization of individual cyclin-dependent kinase complexes from Saccharomyces cerevisiae. Yeast. (1999) 15: 295-309.
Molecular shape and ATP binding activity of rat p50, a putative mammalian homologue of RuvB DNA helicase. J Biochem. (1999) 125: 487-94.
Rapid identification of protein phosphatase 1-binding proteins by mixed peptide sequencing and data base searching. Characterization of a novel holoenzymic form of protein phosphatase 1. J Biol Chem. (1998) 273: 24396-405.
A nucleotide-binding domain of porcine liver annexin VI. Proteolysis of annexin VI labelled with 8-azido-ATP, purification by affinity chromatography on ATP-agarose, and fluorescence studies. Mol Cell Biochem. (1998) 181: 11-20.
Rapid purification and characterization of nucleoside diphosphate kinase isoforms using ATP-sepharose affinity column chromatography. Mol Cells. (1997) 7: 630-4.
Novel 30 kDa protein possessing ATP-binding and chaperone activities. Biochem J. (1997) 326: 567-72.
Interaction of annexins IV and VI with ATP. An alternative mechanism by which a cellular function of these calcium- and membrane-binding proteins is regulated. FEBS Lett. (1997) 409: 300-6.
Phosphorylation of different human milk proteins by human catalytic secretory immunoglobulin A. Biochem Mol Biol Int. (1996) 39: 521-7.
Related products:
ADP-Separopore® 4B-CL (Lyophilized) (SKU # 20181057)
AMP-Separopore® 4B-CL (Lyophilized) (SKU # 20181000)
ATP-Separopore® 4B-CL (SKU # 20181051)
N-Acetyl-galactosamine Separopore® 4B-CL (SKU # 20181021)
N-Acetyl-glucosamine Separopore® 4B-CL (SKU # 20181022)
GTP-Separopore® 4B-CL (SKU # 20181066)
NAD-Separopore® 4B-CL (Lyophilized) (SKU # 20181024)
NADP-Separopore® 4B-CL (Lyophilized) (SKU # 20181023)
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.
Hazmat Shipping: Non-hazardous
Storage: -20°C
Appearance Form: Powder
Appearance Color: White
Brand Name: bioPLUS™, Separopore™
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