Separopore® 4B
€0.00
In stock
SKU
BW-20181031
Application:
Separopore® 4B is a high gel strength bioagarose matrix for gel filtration and coupling of affinity ligands. It is ideal for both analytical and preparative protein purifications. Separopore® 4B is a proven base matrix for coupling affinity ligands. Separopore® 4B provides good separation over a wide molecular weight range. Larger volumes available at discounted prices (enquire).
Note: Separopore® is a cost-effective equivalent to Sepharose® in all of its physical properties and binding characteristics.
Technical Specifications:
Matrix: Separopore® 4B (agarose beads, 4%)
Particle size range: 52 – 165 μm
Molecular weight range: 6 x 104 – 2 x 107
pH stability: 4 – 9
Flow Specifications: 70 – 140 cm / h
Supplied as a slurry in 20% ethanol
Chemical stability: Stable to all solutions commonly used in gel filtration including 8M Urea, 6M guanidine hydrochloride
Physical stability: Negligible volume variation due to changes in pH or ionic strength
Sterilization: Chemical
References:
Coupling of glycosaminoglycans to agarose beads (sepharose 4B). Biochem J. (1971) 124: 677-83.
Purification of a calmodulin-binding protein from chicken gizzard that interacts with F-actin. Proc Natl Acad Sci U S A. (1981) 78: 5652-5.
Regulation of CD44-protein 4.1 interaction by Ca2+ and calmodulin. Implications for modulation of CD44-ankyrin interaction. J Biol Chem. (1997) 272: 30322-8.
Thrombin-induced exposure and prostacyclin inhibition of the receptor for factor VIII/von Willebrand factor on human platelets. J Clin Invest. (1982) 69: 1212-22.
Microdomains of distinctive glycoprotein composition in the kidney proximal tubule brush border. J Cell Biol. (1984) 98: 1505-13.
Studies of the prothrombin activation pathway utilizing radioimmunoassays for the F2/F1+2 fragment and thrombin--antithrombin complex. Blood. (1982) 59: 1086-97.
Purification and characterization of a plasminogen activator inhibitor 1 binding protein from human plasma. Identification as a multimeric form of S protein (vitronectin). J Biol Chem. (1988) 263: 15454-61.
Partial purification and properties of a rat brain phospholipase. J Biol Chem. (1979) 254: 9761-5.
Development of a novel immunoradiometric assay exclusively for biologically active whole parathyroid hormone 1-84: implications for improvement of accurate assessment of parathyroid function. J Bone Miner Res. (2001) 16: 605-14.
Purification of the inducible murine macrophage nitric oxide synthase. Identification as a flavoprotein. J Biol Chem. (1991) 266: 22789-91.
Cloning and characterization of novel ficolins from the solitary ascidian, Halocynthia roretzi. J Biol Chem. (2001) 276: 19959-65.
Improvements on the purification of mannan-binding lectin and demonstration of its Ca(2+)-independent association with a C1s-like serine protease. Biochem J. (1996) 319: 329-32.
Human plasma protein C: isolation, characterization, and mechanism of activation by alpha-thrombin. J Clin Invest. (1979) 64: 761-9.
Induction of nerve growth factor receptor in Schwann cells after axotomy. Proc Natl Acad Sci U S A. (1986) 83: 4094-8.
Purification and characterization of a calmodulin-dependent protein kinase that is highly concentrated in brain. J Biol Chem. (1983) 258: 12735-44.
The role of phospholipid and factor VIIIa in the activation of bovine factor X. J Biol Chem. (1981) 256: 3433-42.
Large, detergent-resistant complexes containing murine antigens Thy-1 and Ly-6 and protein tyrosine kinase p56lck. Eur J Immunol. (1993) 23: 825-31.
Human adenosine deaminase. Distribution and properties. J Biol Chem. (1976) 251: 5448-56.
Distinct forebrain and cerebellar isozymes of type II Ca2+/calmodulin-dependent protein kinase associate differently with the postsynaptic density fraction. J Biol Chem. (1985) 260: 9039-46.
The interaction of wheat germ agglutinin with sialoglycoproteins. The role of sialic acid. J Biol Chem. (1979) 254: 4000-8.
A membrane-bound ATPase from Halobacterium halobium: purification and characterization. J Biochem. (1987) 102: 591-8.
Differential subcompartmentation of terminal glycosylation in the Golgi apparatus of intestinal absorptive and goblet cells. J Biol Chem. (1986) 261: 14307-12.
Arachidonate 5-lipoxygenase of guinea pig peritoneal polymorphonuclear leukocytes. Activation by adenosine 5'-triphosphate. J Biol Chem. (1983) 258: 5754-8.
Insulin-sepharose and the dynamics of insulin action. Proc Natl Acad Sci U S A. (1971) 68: 2066-8.
The mechanism of thrombin-induced platelet factor 4 secretion. Blood. (1980) 55: 661-8.
Related products:
Separopore® 2B-CL (SKU # 20181053)
Separopore® 2B (SKU # 20181045)
Separopore® 2B-MB (Macrobeads) (SKU # 20181054)
Separopore® 4B-CL (SKU # 20181032)
Separopore® 4B-MB (Macrobeads) (SKU #20181033)
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Separopore® 6B-CL (SKU # 20181036)
Separopore® 6B-MB (Macrobeads) (SKU # 20181035)
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®
Separopore® 4B is a high gel strength bioagarose matrix for gel filtration and coupling of affinity ligands. It is ideal for both analytical and preparative protein purifications. Separopore® 4B is a proven base matrix for coupling affinity ligands. Separopore® 4B provides good separation over a wide molecular weight range. Larger volumes available at discounted prices (enquire).
Note: Separopore® is a cost-effective equivalent to Sepharose® in all of its physical properties and binding characteristics.
Technical Specifications:
Matrix: Separopore® 4B (agarose beads, 4%)
Particle size range: 52 – 165 μm
Molecular weight range: 6 x 104 – 2 x 107
pH stability: 4 – 9
Flow Specifications: 70 – 140 cm / h
Supplied as a slurry in 20% ethanol
Chemical stability: Stable to all solutions commonly used in gel filtration including 8M Urea, 6M guanidine hydrochloride
Physical stability: Negligible volume variation due to changes in pH or ionic strength
Sterilization: Chemical
References:
Coupling of glycosaminoglycans to agarose beads (sepharose 4B). Biochem J. (1971) 124: 677-83.
Purification of a calmodulin-binding protein from chicken gizzard that interacts with F-actin. Proc Natl Acad Sci U S A. (1981) 78: 5652-5.
Regulation of CD44-protein 4.1 interaction by Ca2+ and calmodulin. Implications for modulation of CD44-ankyrin interaction. J Biol Chem. (1997) 272: 30322-8.
Thrombin-induced exposure and prostacyclin inhibition of the receptor for factor VIII/von Willebrand factor on human platelets. J Clin Invest. (1982) 69: 1212-22.
Microdomains of distinctive glycoprotein composition in the kidney proximal tubule brush border. J Cell Biol. (1984) 98: 1505-13.
Studies of the prothrombin activation pathway utilizing radioimmunoassays for the F2/F1+2 fragment and thrombin--antithrombin complex. Blood. (1982) 59: 1086-97.
Purification and characterization of a plasminogen activator inhibitor 1 binding protein from human plasma. Identification as a multimeric form of S protein (vitronectin). J Biol Chem. (1988) 263: 15454-61.
Partial purification and properties of a rat brain phospholipase. J Biol Chem. (1979) 254: 9761-5.
Development of a novel immunoradiometric assay exclusively for biologically active whole parathyroid hormone 1-84: implications for improvement of accurate assessment of parathyroid function. J Bone Miner Res. (2001) 16: 605-14.
Purification of the inducible murine macrophage nitric oxide synthase. Identification as a flavoprotein. J Biol Chem. (1991) 266: 22789-91.
Cloning and characterization of novel ficolins from the solitary ascidian, Halocynthia roretzi. J Biol Chem. (2001) 276: 19959-65.
Improvements on the purification of mannan-binding lectin and demonstration of its Ca(2+)-independent association with a C1s-like serine protease. Biochem J. (1996) 319: 329-32.
Human plasma protein C: isolation, characterization, and mechanism of activation by alpha-thrombin. J Clin Invest. (1979) 64: 761-9.
Induction of nerve growth factor receptor in Schwann cells after axotomy. Proc Natl Acad Sci U S A. (1986) 83: 4094-8.
Purification and characterization of a calmodulin-dependent protein kinase that is highly concentrated in brain. J Biol Chem. (1983) 258: 12735-44.
The role of phospholipid and factor VIIIa in the activation of bovine factor X. J Biol Chem. (1981) 256: 3433-42.
Large, detergent-resistant complexes containing murine antigens Thy-1 and Ly-6 and protein tyrosine kinase p56lck. Eur J Immunol. (1993) 23: 825-31.
Human adenosine deaminase. Distribution and properties. J Biol Chem. (1976) 251: 5448-56.
Distinct forebrain and cerebellar isozymes of type II Ca2+/calmodulin-dependent protein kinase associate differently with the postsynaptic density fraction. J Biol Chem. (1985) 260: 9039-46.
The interaction of wheat germ agglutinin with sialoglycoproteins. The role of sialic acid. J Biol Chem. (1979) 254: 4000-8.
A membrane-bound ATPase from Halobacterium halobium: purification and characterization. J Biochem. (1987) 102: 591-8.
Differential subcompartmentation of terminal glycosylation in the Golgi apparatus of intestinal absorptive and goblet cells. J Biol Chem. (1986) 261: 14307-12.
Arachidonate 5-lipoxygenase of guinea pig peritoneal polymorphonuclear leukocytes. Activation by adenosine 5'-triphosphate. J Biol Chem. (1983) 258: 5754-8.
Insulin-sepharose and the dynamics of insulin action. Proc Natl Acad Sci U S A. (1971) 68: 2066-8.
The mechanism of thrombin-induced platelet factor 4 secretion. Blood. (1980) 55: 661-8.
Related products:
Separopore® 2B-CL (SKU # 20181053)
Separopore® 2B (SKU # 20181045)
Separopore® 2B-MB (Macrobeads) (SKU # 20181054)
Separopore® 4B-CL (SKU # 20181032)
Separopore® 4B-MB (Macrobeads) (SKU #20181033)
Separopore® 6B (SKU # 20181043)
Separopore® 6B-CL (SKU # 20181036)
Separopore® 6B-MB (Macrobeads) (SKU # 20181035)
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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