G7550
Sephadex® G-75
Superfine
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About This Item
Productos recomendados
Quality Level
technique(s)
buffer exchange: suitable
matrix active group
phase
swelling
1 g swells to 12-15 mL
bead size
20-50 μm
application(s)
life science and biopharma
compatibility
Cytiva
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General description
Sephadex® G-75 is well-established gel filtration medium for desalting and buffer exchange of large biomolecules >80,000 molecular weight.
Sephadex® is a gel filtration medium prepared by crosslinking dextran with epichlorohydrin. Different types of Sephadex™ differ in their degree of cross-linking and hence in their degree of swelling and their molecular fractionation range. Sephadex® G-75 is for larger molecules.
Sephadex® is a gel filtration medium prepared by crosslinking dextran with epichlorohydrin. Different types of Sephadex™ differ in their degree of cross-linking and hence in their degree of swelling and their molecular fractionation range. Sephadex® G-75 is for larger molecules.
Application
Sephadex® G-75 is a gel filtration media used in gel filtration chromatography and protein chromatography. It has been used for desaltation process to study the production, purification, and immobilization of l-asparaginase II (ASNase II) in chitosan nanoparticles (CSNPs).
Legal Information
Sephadex is a registered trademark of Cytiva
Sepharose is a trademark of Cytiva
Replaced by
Referencia del producto
Descripción
Precios
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Certificados de análisis (COA)
Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»
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Antimicrobial activity of protease inhibitor isolated from Coccinia grandis (L.) Voigt. has been reported. A 14.3 kDa protease inhibitor (PI) was isolated and purified to homogeneity by ammonium sulfate precipitation (20-85% saturation), sephadex G-75, DEAE sepharose column and trypsin-sepharose affinity
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A procoagulant metalloproteinase called CCSV-MPase was purified from C. cerastes venom by successive chromatographic methods starting with gel-filtration through Sephadex G-75; ion-exchange DEAE-Cellulose A-50; affinity chromatography on Benzamidine Sepharose 6B and RP-HPLC on a C8 column. CCSV-MPase has been isolated
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