Blue Separopore® 4B-CL
€0.00
In stock
SKU
BW-20181096
Application:
Blue-Separopore® 4B-CL is Cibacron™ Blue F3G-A covalently attached to the Separopore® 4B-CL matrix by the triazine coupling method. The structure of the blue dye makes it a very versatile tool for separating many proteins, e.g. albumin, interferon, lipoproteins and blood coagulation factors. It also binds several enzymes including kinases, dehydrogenases, and most enzymes requiring adenyl-containing cofactors e.g. NAD+. The highly cross-linked matrix provides a stable, rigid medium.
Blue-Separopore® 4B-CL is a dye-ligand affinity matrix for purification of albumin, enzymes (including NAD+ and NADP+), coagulation factors, interferons and related proteins. The ligand, Cibacron Blue F3G-A, is covalently coupled to Separopore® 4B-CL via chlorotriazine ring. Due to a broad spectrum of the affinity, this product can be used as a general purpose protein purification tool often used for the removal of BSA from serum for the enrichment of less abundant proteins.
Note: Separopore® is a cost-effective equivalent to Sepharose® in all of its physical properties and binding characteristics.
Technical Specifications:
Ligand: Cibacron Blue F3G-A
Matrix: Separopore® 4B-CL (crosslinked agarose beads, 4%)
Particle size range: 53 – 180 µm
Matrix activation: Triazine coupling
Binding capacity: ~15 mg bovine serum albumin / ml drained gel
pH stability: 3 – 13
Storage: 2 – 8 °C
Supplied as 50% slurry in 20% ethanol
References:
Elution relationships to model affinity chromatography using a general rate model. J Mol Recognit. (2012) 25: 571-9.
Expression and purification of recombinant human serum albumin fusion protein with VEGF165b in Pichia pastoris. Protein Expr Purif. (2012) 85: 32-7.
Stereoselective binding of mexiletine and ketoprofen enantiomers with human serum albumin domains. Acta Pharmacol Sin. (2012) 33: 710-6.
Purification and characterization of an endo-D:-arabinase produced by cellulomonas. Protein J. (2012) 31: 51-8.
Cibacron Blue and proteomics: the mystery of the platoon missing in action. J Proteomics. (2011) 74: 2856-65.
Determination of robustness and optimal work conditions for a purification process of a therapeutic recombinant protein using response surface methodology. Biotechnol Prog. (2011) 27: 724-32.
An alternative method for purifying and detoxifying diphtheria toxin. Toxicon. (2011) 57: 1093-100.
Simple method for isolation of glyceraldehyde 3-phosphate dehydrogenase and the improvement of myofibril gel properties. Anim Sci J. (2011) 82: 136-43.
Extension of the selection of protein chromatography and the rate model to affinity chromatography. J Mol Recognit. (2010) 23: 609-17.
Inhibition of neutrophil migration by hemopexin leads to increased mortality due to sepsis in mice. Am J Respir Crit Care Med. (2011) 183: 922-31.
Identification, cloning and characterization of an aldo-keto reductase from Trypanosoma cruzi with quinone oxido-reductase activity. Mol Biochem Parasitol. (2010) 173: 132-41.
Bioactivity and pharmacokinetics of two human serum albumin-thymosin alpha1-fusion proteins, rHSA-Talpha1 and rHSA-L-Talpha1, expressed in recombinant Pichia pastoris. Cancer Immunol Immunother. (2010) 59: 1335-45.
Structural and catalytic properties of the D-3-hydroxybutyrate dehydrogenase from Pseudomonas aeruginosa. Curr Microbiol. (2010) 61: 7-12.
Analysis of nucleoside-binding proteins by ligand-specific elution from dye resin: application to Mycobacterium tuberculosis aldehyde dehydrogenases. J Struct Funct Genomics. (2009) 10: 291-301.
Isolation and characterization of a French bean hemagglutinin with antitumor, antifungal, and anti-HIV-1 reverse transcriptase activities and an exceptionally high yield. Phytomedicine. (2010) 17: 457-62.
Proteomics-based approach for identification and purification of human phosphate binding apolipoprotein from amniotic fluid. Genet Mol Res. (2009) 8: 929-37.
Immunoaffinity purification and characterization of glyceraldehyde-3-phosphate dehydrogenase from human erythrocytes. Acta Biochim Biophys Sin (Shanghai). (2009) 41: 399-406.
Purification and characterization of hemolymph prophenoloxidase from Ostrinia furnacalis (Lepidoptera: Pyralidae) larvae. Comp Biochem Physiol B Biochem Mol Biol. (2008) 151: 139-46.
Characterization and large-scale production of recombinant Streptoverticillium platensis transglutaminase. J Ind Microbiol Biotechnol. (2008) 35: 981-90.
Related products:
Red-Separopore® 4B-CL (SKU # 20181095)
Reactive Blue 4-Separopore® 4B-CL (SKU #20181097)
Yellow-Separopore® 4B-CL (SKU # 20181098)
Green-Separopore® 4B-CL (SKU # 20181099)
Brown-Separopore® 4B-CL (SKU # 20181100)
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
Appearance Form: Suspension
Appearance Color: Blue
Brand Name: bioPLUS™, Separopore®
Blue-Separopore® 4B-CL is Cibacron™ Blue F3G-A covalently attached to the Separopore® 4B-CL matrix by the triazine coupling method. The structure of the blue dye makes it a very versatile tool for separating many proteins, e.g. albumin, interferon, lipoproteins and blood coagulation factors. It also binds several enzymes including kinases, dehydrogenases, and most enzymes requiring adenyl-containing cofactors e.g. NAD+. The highly cross-linked matrix provides a stable, rigid medium.
Blue-Separopore® 4B-CL is a dye-ligand affinity matrix for purification of albumin, enzymes (including NAD+ and NADP+), coagulation factors, interferons and related proteins. The ligand, Cibacron Blue F3G-A, is covalently coupled to Separopore® 4B-CL via chlorotriazine ring. Due to a broad spectrum of the affinity, this product can be used as a general purpose protein purification tool often used for the removal of BSA from serum for the enrichment of less abundant proteins.
Note: Separopore® is a cost-effective equivalent to Sepharose® in all of its physical properties and binding characteristics.
Technical Specifications:
Ligand: Cibacron Blue F3G-A
Matrix: Separopore® 4B-CL (crosslinked agarose beads, 4%)
Particle size range: 53 – 180 µm
Matrix activation: Triazine coupling
Binding capacity: ~15 mg bovine serum albumin / ml drained gel
pH stability: 3 – 13
Storage: 2 – 8 °C
Supplied as 50% slurry in 20% ethanol
References:
Elution relationships to model affinity chromatography using a general rate model. J Mol Recognit. (2012) 25: 571-9.
Expression and purification of recombinant human serum albumin fusion protein with VEGF165b in Pichia pastoris. Protein Expr Purif. (2012) 85: 32-7.
Stereoselective binding of mexiletine and ketoprofen enantiomers with human serum albumin domains. Acta Pharmacol Sin. (2012) 33: 710-6.
Purification and characterization of an endo-D:-arabinase produced by cellulomonas. Protein J. (2012) 31: 51-8.
Cibacron Blue and proteomics: the mystery of the platoon missing in action. J Proteomics. (2011) 74: 2856-65.
Determination of robustness and optimal work conditions for a purification process of a therapeutic recombinant protein using response surface methodology. Biotechnol Prog. (2011) 27: 724-32.
An alternative method for purifying and detoxifying diphtheria toxin. Toxicon. (2011) 57: 1093-100.
Simple method for isolation of glyceraldehyde 3-phosphate dehydrogenase and the improvement of myofibril gel properties. Anim Sci J. (2011) 82: 136-43.
Extension of the selection of protein chromatography and the rate model to affinity chromatography. J Mol Recognit. (2010) 23: 609-17.
Inhibition of neutrophil migration by hemopexin leads to increased mortality due to sepsis in mice. Am J Respir Crit Care Med. (2011) 183: 922-31.
Identification, cloning and characterization of an aldo-keto reductase from Trypanosoma cruzi with quinone oxido-reductase activity. Mol Biochem Parasitol. (2010) 173: 132-41.
Bioactivity and pharmacokinetics of two human serum albumin-thymosin alpha1-fusion proteins, rHSA-Talpha1 and rHSA-L-Talpha1, expressed in recombinant Pichia pastoris. Cancer Immunol Immunother. (2010) 59: 1335-45.
Structural and catalytic properties of the D-3-hydroxybutyrate dehydrogenase from Pseudomonas aeruginosa. Curr Microbiol. (2010) 61: 7-12.
Analysis of nucleoside-binding proteins by ligand-specific elution from dye resin: application to Mycobacterium tuberculosis aldehyde dehydrogenases. J Struct Funct Genomics. (2009) 10: 291-301.
Isolation and characterization of a French bean hemagglutinin with antitumor, antifungal, and anti-HIV-1 reverse transcriptase activities and an exceptionally high yield. Phytomedicine. (2010) 17: 457-62.
Proteomics-based approach for identification and purification of human phosphate binding apolipoprotein from amniotic fluid. Genet Mol Res. (2009) 8: 929-37.
Immunoaffinity purification and characterization of glyceraldehyde-3-phosphate dehydrogenase from human erythrocytes. Acta Biochim Biophys Sin (Shanghai). (2009) 41: 399-406.
Purification and characterization of hemolymph prophenoloxidase from Ostrinia furnacalis (Lepidoptera: Pyralidae) larvae. Comp Biochem Physiol B Biochem Mol Biol. (2008) 151: 139-46.
Characterization and large-scale production of recombinant Streptoverticillium platensis transglutaminase. J Ind Microbiol Biotechnol. (2008) 35: 981-90.
Related products:
Red-Separopore® 4B-CL (SKU # 20181095)
Reactive Blue 4-Separopore® 4B-CL (SKU #20181097)
Yellow-Separopore® 4B-CL (SKU # 20181098)
Green-Separopore® 4B-CL (SKU # 20181099)
Brown-Separopore® 4B-CL (SKU # 20181100)
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
Appearance Form: Suspension
Appearance Color: Blue
Brand Name: bioPLUS™, Separopore®
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