Epoxy-Activated Separopore® 4B-CL
€0.00
In stock
SKU
BW-20181009
Highlights:
Used in coupling of hydroxyl, amino or thiol groups to Separopore® 4B via a 12-carbon hydrophilic spacer arm.
Pre-activated medium for immobilization of ligands containing amino (primary or secondary), hydroxyl or thiol group.
Ideal for immobilization of alkali-resistant small ligands such as peptides, amino acids and carbohydrates.
Epoxy-activated Separopore® 4B is a pre-activated medium for coupling sugars and other carbohydrates via an ether linkage to a hydroxyl group.
Medium has a long hydrophilic 12 atom spacer arm which makes it particularly suitable for immobilization of small molecules.
Note: Separopore® is a cost-effective equivalent to Sepharose® in all of its physical properties and binding characteristics.
Technical Specifications:
Matrix active group: Epoxy
Matrix: Separopore® 4B-CL (crosslinked agarose beads, 4%)
Particle size range: 52 – 165 μm
Group to be coupled: -NH2, -OH, or -SH
Molecular weight range: 6 x 104 – 2 x 107
Chemical linkage of ligand: Ether
Matrix spacer: 12 atoms (when ligands are coupled to free epoxy groups. Linkage is stable, uncharged ether)
Coupling conditions: pH 9 – 10 (amino ligands), pH 11 – 12 (hydroxyl ligands), pH 7.5 - 8.5 (thiol ligands); Temp: 4 – 37 °C; Time: 16 h to several days; organic solvents possible
pH stability: 2 – 11 (ligand dependent)
Storage: 2 – 8 °C
Supplied as lyophilized powder stabilized with lactose and dextran
1g swells to 3 – 4 ml
References:
Immunohistochemical localization, purification, and characterization of human urinary bladder glutathione S-transferases. Biochim Biophys Acta. (1991) 1074: 363-70.
Evaluation of a new reactive solid phase for radioimmunoassay of serum specific IgE against muscle relaxant drugs. Allergy. (1991) 46: 452-8.
Purification of a GSH-affinity binding protein from Bacteroides fragilis devoid of glutathione transferase activity. FEMS Microbiol Lett. (1991) 66: 101-5.
A T-antigen-binding lectin from Channa leucopunctatus (Murrel) plasma. Carbohydr Res. (1991) 213: 251-61.
Independent segregation of glutathione S-transferase and fatty acid ethyl ester synthase from pancreas and other human tissues. Biochem J. (1991) 275: 507-13.
Independent characterization of thymidine transport and subsequent metabolism in Hymenolepis diminuta--II. Purification and preliminary analysis of thymidine kinase. Comp Biochem Physiol B. (1991) 98: 181-6.
Characterization of affinity-purified juvenile hormone esterase from the plasma of the tobacco hornworm, Manduca sexta. J Biol Chem. (1990) 265: 21727-32.
Solubilization and partial purification of GABAB receptor from bovine brain. Biochem Biophys Res Commun. (1990) 172: 22-7.
Affinity purification of retinoic acid-binding proteins using immobilized 4-(2-hydroxyethoxy) retinoic acid. Protein Expr Purif. (1990) 1: 63-9.
Solubilization and purification of melatonin receptors from lizard brain. Endocrinology. (1990) 127: 1206-14.
Effect of polyethylene glycol on the non-specific adsorption of proteins to Eupergit C and agarose. J Chromatogr. (1990) 510: 271-9.
High-performance liquid chromatography of proteins on deformed non-porous agarose beads. Fast boronate affinity chromatography of haemoglobin at neutral pH. J Chromatogr. (1990) 500: 543-53.
Isolation of a lectin from the marine sponge Desmapsama anchorata by affinity chromatography on raffinose-sepharose 6B. Braz J Med Biol Res. (1990) 23: 191-4.
Purine nucleoside phosphorylase: purification using an ether-linked formycin B/sepharose 6B resin with unusual properties. Prep Biochem. (1990) 20: 75-85.
Preparation of an affinity chromatography matrix for the selective purification of the dopamine D2 receptor from bovine striatal membranes. Biochim Biophys Acta. (1989) 986: 271-80.
One-step affinity purification of amidase from mutant strains of Pseudomonas aeruginosa. Biochimie. (1989) 71: 1179-84.
L-asparaginase from Erwinia carotovora. An improved recovery and purification process using affinity chromatography. Appl Biochem Biotechnol. (1989) 22: 1-11.
An oligodeoxynucleotide affinity column for the isolation of sequence specific DNA binding proteins. Nucleic Acids Res. (1988) 16: 10283-99.
Isolation of Rhizobium loti Strain-Specific DNA Sequences by Subtraction Hybridization. Appl Environ Microbiol. (1988) 54: 2852-5.
Related products:
CDI-activated Separopore® 4B (SKU # 20181002)
CDI-activated Separopore® 6B-CL (SKU # 20181084)
CH-activated Separopore® 4B (SKU # 20181085)
CNBr-activated Separopore® 4B (SKU # 20181003)
CNBr-activated Separopore® 6B (SKU # 20181062)
Epoxy-activated Separopore® 6B-CL (SKU # 20181064)
NHS-activated Separopore® 4B-CL (SKU # 20181025)
Tosyl-activated Separopore® 4B-CL (SKU # 20181039)
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
Brand Name: bioPLUS™, Separopore®
Used in coupling of hydroxyl, amino or thiol groups to Separopore® 4B via a 12-carbon hydrophilic spacer arm.
Pre-activated medium for immobilization of ligands containing amino (primary or secondary), hydroxyl or thiol group.
Ideal for immobilization of alkali-resistant small ligands such as peptides, amino acids and carbohydrates.
Epoxy-activated Separopore® 4B is a pre-activated medium for coupling sugars and other carbohydrates via an ether linkage to a hydroxyl group.
Medium has a long hydrophilic 12 atom spacer arm which makes it particularly suitable for immobilization of small molecules.
Note: Separopore® is a cost-effective equivalent to Sepharose® in all of its physical properties and binding characteristics.
Technical Specifications:
Matrix active group: Epoxy
Matrix: Separopore® 4B-CL (crosslinked agarose beads, 4%)
Particle size range: 52 – 165 μm
Group to be coupled: -NH2, -OH, or -SH
Molecular weight range: 6 x 104 – 2 x 107
Chemical linkage of ligand: Ether
Matrix spacer: 12 atoms (when ligands are coupled to free epoxy groups. Linkage is stable, uncharged ether)
Coupling conditions: pH 9 – 10 (amino ligands), pH 11 – 12 (hydroxyl ligands), pH 7.5 - 8.5 (thiol ligands); Temp: 4 – 37 °C; Time: 16 h to several days; organic solvents possible
pH stability: 2 – 11 (ligand dependent)
Storage: 2 – 8 °C
Supplied as lyophilized powder stabilized with lactose and dextran
1g swells to 3 – 4 ml
References:
Immunohistochemical localization, purification, and characterization of human urinary bladder glutathione S-transferases. Biochim Biophys Acta. (1991) 1074: 363-70.
Evaluation of a new reactive solid phase for radioimmunoassay of serum specific IgE against muscle relaxant drugs. Allergy. (1991) 46: 452-8.
Purification of a GSH-affinity binding protein from Bacteroides fragilis devoid of glutathione transferase activity. FEMS Microbiol Lett. (1991) 66: 101-5.
A T-antigen-binding lectin from Channa leucopunctatus (Murrel) plasma. Carbohydr Res. (1991) 213: 251-61.
Independent segregation of glutathione S-transferase and fatty acid ethyl ester synthase from pancreas and other human tissues. Biochem J. (1991) 275: 507-13.
Independent characterization of thymidine transport and subsequent metabolism in Hymenolepis diminuta--II. Purification and preliminary analysis of thymidine kinase. Comp Biochem Physiol B. (1991) 98: 181-6.
Characterization of affinity-purified juvenile hormone esterase from the plasma of the tobacco hornworm, Manduca sexta. J Biol Chem. (1990) 265: 21727-32.
Solubilization and partial purification of GABAB receptor from bovine brain. Biochem Biophys Res Commun. (1990) 172: 22-7.
Affinity purification of retinoic acid-binding proteins using immobilized 4-(2-hydroxyethoxy) retinoic acid. Protein Expr Purif. (1990) 1: 63-9.
Solubilization and purification of melatonin receptors from lizard brain. Endocrinology. (1990) 127: 1206-14.
Effect of polyethylene glycol on the non-specific adsorption of proteins to Eupergit C and agarose. J Chromatogr. (1990) 510: 271-9.
High-performance liquid chromatography of proteins on deformed non-porous agarose beads. Fast boronate affinity chromatography of haemoglobin at neutral pH. J Chromatogr. (1990) 500: 543-53.
Isolation of a lectin from the marine sponge Desmapsama anchorata by affinity chromatography on raffinose-sepharose 6B. Braz J Med Biol Res. (1990) 23: 191-4.
Purine nucleoside phosphorylase: purification using an ether-linked formycin B/sepharose 6B resin with unusual properties. Prep Biochem. (1990) 20: 75-85.
Preparation of an affinity chromatography matrix for the selective purification of the dopamine D2 receptor from bovine striatal membranes. Biochim Biophys Acta. (1989) 986: 271-80.
One-step affinity purification of amidase from mutant strains of Pseudomonas aeruginosa. Biochimie. (1989) 71: 1179-84.
L-asparaginase from Erwinia carotovora. An improved recovery and purification process using affinity chromatography. Appl Biochem Biotechnol. (1989) 22: 1-11.
An oligodeoxynucleotide affinity column for the isolation of sequence specific DNA binding proteins. Nucleic Acids Res. (1988) 16: 10283-99.
Isolation of Rhizobium loti Strain-Specific DNA Sequences by Subtraction Hybridization. Appl Environ Microbiol. (1988) 54: 2852-5.
Related products:
CDI-activated Separopore® 4B (SKU # 20181002)
CDI-activated Separopore® 6B-CL (SKU # 20181084)
CH-activated Separopore® 4B (SKU # 20181085)
CNBr-activated Separopore® 4B (SKU # 20181003)
CNBr-activated Separopore® 6B (SKU # 20181062)
Epoxy-activated Separopore® 6B-CL (SKU # 20181064)
NHS-activated Separopore® 4B-CL (SKU # 20181025)
Tosyl-activated Separopore® 4B-CL (SKU # 20181039)
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
Brand Name: bioPLUS™, Separopore®
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