Dextran Separopore® 4B-CL (Epoxy-Coupled)
€0.00
In stock
SKU
BW-20181005
Application:
Dextran is coupled to a high strength Separopore® 4B-CL matrix. Coupling dextran to this material expands the surface area of the Separopore® beads allowing for further binding of macromolecules. Dextran-Separopore® 4B-CL is used in affinity chromatography as a protein binding site. It has been used to study Alzheimer’s disease by quantifying cerebrospinal fluid (CSF) in relation to amyloid accumulation in rat brain parenchyma.
Note: Separopore® is a cost-effective equivalent to Sepharose® in all of its physical properties and binding characteristics.
Note: Separopore® is a cost-effective equivalent to Sepharose® in all of its physical properties and binding characteristics.
Technical Specifications:
Ligand: Dextran
Matrix: Separopore® 4B-CL (crosslinked agarose beads, 4%)
Particle size range: 52 – 165 µm
Matrix activation: Epoxy
Ligand density: 1 – 5 mg dextran / ml drained gel
Matrix attachment: Hydroxyl
Supplied as saline suspension in 0.5M NaCl containing 0.02% thimerosal
Storage temp: 2 – 8 °C
References:
Characterization of the Concentration-Dependence of Solute Diffusivity and Partitioning in a Model Dextran-Agarose Transport System. Cell Mol Bioeng. (2009) 2: 295-305.
Expression, purification, and initial characterization of a recombinant form of plant PEP-carboxylase kinase from CAM-induced Mesembryanthemum crystallinum with enhanced solubility in Escherichia coli. Protein Expr Purif. (2003) 29: 123-31.
Use of dextrans as long and hydrophilic spacer arms to improve the performance of immobilized proteins acting on macromolecules. Biotechnol Bioeng. (1998) 60: 518-23.
Evidence for a slow-turnover form of the Ca2+-independent phosphoenolpyruvate carboxylase kinase in the aleurone-endosperm tissue of germinating barley seeds. Plant Physiol. (1999) 119: 511-20.
Purification and properties of the pyruvate kinase isozyme M1 from the pig brain. Int J Biochem Cell Biol. (1995) 27: 1145-51.
Salt induction and the partial purification/characterization of phosphoenolpyruvate carboxylase protein-serine kinase from an inducible crassulacean-acid-metabolism (CAM) plant, Mesembryanthemum crystallinum L. Arch Biochem Biophys. (1994) 314: 247-54.
Induction, modification, and perception of the salicylic acid signal in plant defence. Biochem Soc Symp. (1994) 60: 219-29.
Partial purification and characterization of phosphoenolpyruvate carboxylase protein-serine kinase from illuminated maize leaves. Arch Biochem Biophys. (1993) 304: 496-502.
Regulatory phosphorylation of Sorghum leaf phosphoenolpyruvate carboxylase. Identification of the protein-serine kinase and some elements of the signal-transduction cascade. Eur J Biochem. (1992) 204: 821-30.
Regulatory seryl-phosphorylation of C4 phosphoenolpyruvate carboxylase by a soluble protein kinase from maize leaves. Arch Biochem Biophys. (1989) 269: 526-35.
Purification of bovine liver S-adenosylhomocysteine hydrolase by affinity chromatography on blue dextran-agarose. Biochim Biophys Acta. (1988) 965: 22-8.
Purification and partial characterization of the multicomponent dextranase complex of Streptococcus sobrinus and cloning of the dextranase gene. Infect Immun. (1987) 55: 792-802.
Detergent-solubilization, purification, and characterization of membrane-bound 3-hydroxy-3-methylglutaryl-coenzyme A reductase from radish seedlings. Eur J Biochem. (1986) 154: 103-11.
Correlation between immunosuppressive activity and translation regulatory activity. Immunol Lett. (1985) 9: 123-9.
Synthesis of factor II antigen by isolated perfused rat liver. Biochim Biophys Acta. (1981) 676: 365-72.
Probing the molecular structure of phytochrome with immobilized Cibacron blue 3GA and blue dextran. Proc Natl Acad Sci U S A. (1981) 78: 2977-80.
Purification of dihydropterin reductase using immobilized Cibacron Blue. Can J Biochem. (1979) 57: 178-87.
Binding of human interferons to immobolized Cibacron Blue F3GA: The nature of molecular interaction. Biochemistry. (1976) 15: 5182-7.
Purification of human blood clotting factor X by Blue Dextran agarose affinity chromatography. Biochim Biophys Acta. (1976) 434: 199-208.
Purification of NADH-Nitrate Reductase by Affinity Chromatography. Plant Physiol. (1975) 56: 853-5.
Related products:
Fucose-Separopore® 4B-CL (SKU # 20181010)
Galactose-Separopore® 4B-CL (SKU # 20181011)
Glucose-Separopore® 4B-CL (SKU # 20181076)
Lactose-Separopore® 4B-CL (SKU # 20181017)
Maltose-Separopore® 4B (SKU # 20181072)
Mannose-Separopore® 4B-CL (SKU # 20181019)
Guar Gum-Separopore® 4B-CL (SKU # 20181052)
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: 2-8°C
Brand Name: bioPLUS™, Separopore®
Dextran is coupled to a high strength Separopore® 4B-CL matrix. Coupling dextran to this material expands the surface area of the Separopore® beads allowing for further binding of macromolecules. Dextran-Separopore® 4B-CL is used in affinity chromatography as a protein binding site. It has been used to study Alzheimer’s disease by quantifying cerebrospinal fluid (CSF) in relation to amyloid accumulation in rat brain parenchyma.
Note: Separopore® is a cost-effective equivalent to Sepharose® in all of its physical properties and binding characteristics.
Note: Separopore® is a cost-effective equivalent to Sepharose® in all of its physical properties and binding characteristics.
Technical Specifications:
Ligand: Dextran
Matrix: Separopore® 4B-CL (crosslinked agarose beads, 4%)
Particle size range: 52 – 165 µm
Matrix activation: Epoxy
Ligand density: 1 – 5 mg dextran / ml drained gel
Matrix attachment: Hydroxyl
Supplied as saline suspension in 0.5M NaCl containing 0.02% thimerosal
Storage temp: 2 – 8 °C
References:
Characterization of the Concentration-Dependence of Solute Diffusivity and Partitioning in a Model Dextran-Agarose Transport System. Cell Mol Bioeng. (2009) 2: 295-305.
Expression, purification, and initial characterization of a recombinant form of plant PEP-carboxylase kinase from CAM-induced Mesembryanthemum crystallinum with enhanced solubility in Escherichia coli. Protein Expr Purif. (2003) 29: 123-31.
Use of dextrans as long and hydrophilic spacer arms to improve the performance of immobilized proteins acting on macromolecules. Biotechnol Bioeng. (1998) 60: 518-23.
Evidence for a slow-turnover form of the Ca2+-independent phosphoenolpyruvate carboxylase kinase in the aleurone-endosperm tissue of germinating barley seeds. Plant Physiol. (1999) 119: 511-20.
Purification and properties of the pyruvate kinase isozyme M1 from the pig brain. Int J Biochem Cell Biol. (1995) 27: 1145-51.
Salt induction and the partial purification/characterization of phosphoenolpyruvate carboxylase protein-serine kinase from an inducible crassulacean-acid-metabolism (CAM) plant, Mesembryanthemum crystallinum L. Arch Biochem Biophys. (1994) 314: 247-54.
Induction, modification, and perception of the salicylic acid signal in plant defence. Biochem Soc Symp. (1994) 60: 219-29.
Partial purification and characterization of phosphoenolpyruvate carboxylase protein-serine kinase from illuminated maize leaves. Arch Biochem Biophys. (1993) 304: 496-502.
Regulatory phosphorylation of Sorghum leaf phosphoenolpyruvate carboxylase. Identification of the protein-serine kinase and some elements of the signal-transduction cascade. Eur J Biochem. (1992) 204: 821-30.
Regulatory seryl-phosphorylation of C4 phosphoenolpyruvate carboxylase by a soluble protein kinase from maize leaves. Arch Biochem Biophys. (1989) 269: 526-35.
Purification of bovine liver S-adenosylhomocysteine hydrolase by affinity chromatography on blue dextran-agarose. Biochim Biophys Acta. (1988) 965: 22-8.
Purification and partial characterization of the multicomponent dextranase complex of Streptococcus sobrinus and cloning of the dextranase gene. Infect Immun. (1987) 55: 792-802.
Detergent-solubilization, purification, and characterization of membrane-bound 3-hydroxy-3-methylglutaryl-coenzyme A reductase from radish seedlings. Eur J Biochem. (1986) 154: 103-11.
Correlation between immunosuppressive activity and translation regulatory activity. Immunol Lett. (1985) 9: 123-9.
Synthesis of factor II antigen by isolated perfused rat liver. Biochim Biophys Acta. (1981) 676: 365-72.
Probing the molecular structure of phytochrome with immobilized Cibacron blue 3GA and blue dextran. Proc Natl Acad Sci U S A. (1981) 78: 2977-80.
Purification of dihydropterin reductase using immobilized Cibacron Blue. Can J Biochem. (1979) 57: 178-87.
Binding of human interferons to immobolized Cibacron Blue F3GA: The nature of molecular interaction. Biochemistry. (1976) 15: 5182-7.
Purification of human blood clotting factor X by Blue Dextran agarose affinity chromatography. Biochim Biophys Acta. (1976) 434: 199-208.
Purification of NADH-Nitrate Reductase by Affinity Chromatography. Plant Physiol. (1975) 56: 853-5.
Related products:
Fucose-Separopore® 4B-CL (SKU # 20181010)
Galactose-Separopore® 4B-CL (SKU # 20181011)
Glucose-Separopore® 4B-CL (SKU # 20181076)
Lactose-Separopore® 4B-CL (SKU # 20181017)
Maltose-Separopore® 4B (SKU # 20181072)
Mannose-Separopore® 4B-CL (SKU # 20181019)
Guar Gum-Separopore® 4B-CL (SKU # 20181052)
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: 2-8°C
Brand Name: bioPLUS™, Separopore®
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