Maltose Separopore® 4B (Divinyl Sulfone-Coupled)

Maltose Separopore® 4B (Divinyl Sulfone-Coupled)

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SKU
BW-20181072
Catalog Number: BW-20181072
Datasheet
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Application:
Maltose is coupled with Separopore® 4B. Maltose Separopore® 4B provides a convenient affinity purification of recombinant proteins tagged with maltose-binding protein (MBP). Maltose Separopore® 4B has high binding capacity for MBP-tagged proteins. Purification is performed under physiological conditions and the mild elution preserves the activity of the target protein. Due to the high specificity of the binding, very high purity of the eluted protein is achieved in just one step.

Maltose-Separopore® 4B is used in protein chromatography, affinity chromatography and carbohydrate matrices. Maltose-Separopore® 4B has been used to study surfactant protein D (SP-D), which plays an important role in innate immunity. Maltose-Separopore® 4B has also been used to study numerous pathological mechanisms for diseases in the human lung, including Aspergillus fumigatus, a pathogenic fungus, and the human influenza A virus.

Note: Separopore® is a cost-effective equivalent to Sepharose® in all of its physical properties and binding characteristics.

Technical Specifications:
Ligand: Maltose
Matrix: Separopore® 4B (agarose beads, 4%)
Particle size range: 52 – 165 µm.
Molecular weight range: 6 x 104 – 2 x 107
Matrix activation: Divinyl sulfone
Matrix attachment: Hydroxyl
Ligand density: ~20 μmol maltose / ml drained gel
Binding capacity: ≥20 mg MBP / ml drained gel
Flow Specifications: 70 – 140 cm / h
pH stability: 4 – 9
Supplied as suspension in 0.01M phosphate buffer (pH 6.8), 0.15M NaCl, 0.02% thimerosal

References:
Purification, characterization and immunolocalization of porcine surfactant protein D. Immunology. (2005) 114: 72-82.
Identification and characterization of a novel interaction between pulmonary surfactant protein D and decorin. J Biol Chem. (2003) 278: 25678-87.
Enhanced binding of Aspergillus fumigates spores to A549 epithelial cells and extracellular matrix proteins by a component from the spore surface and inhibition by rat lung lavage fluid. Thorax. (2000) 55: 579-84.
Structure of a truncated human surfactant protein D is less effective in agglutinating bacteria than the native structure and fails to inhibit haemagglutination by influenza A virus. Biochem J. (1997) 323: 393-9.
The alpha-helical neck region of human lung surfactant protein D is essential for the binding of the carbohydrate recognition domains to lipopolysaccharides and phospholipids. Biochem J. (1996) 318: 505-11.
Mite allergen induces nitric oxide production in alveolar macrophage cell lines via CD14/toll-like receptor 4, and is inhibited by surfactant protein D. Clin Exp Allergy. (2005) 35: 1615-24.
Purification, characterization and cDNA cloning of human lung surfactant protein D. Biochem J. (1992) 284: 795-802.

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Glucose-Separopore® 4B-CL (SKU # 20181076)
Lactose-Separopore® 4B-CL (SKU # 20181017)
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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: 2-8°C
Brand Name: bioPLUS™, Separopore®
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