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
Product No.
Description
Pricing
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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John G Vontas et al.
The Biochemical journal, 362(Pt 2), 329-337 (2002-02-21)
A novel glutathione S-transferase (GST)-based pyrethroid resistance mechanism was recently identified in Nilaparvata lugens [Vontas, Small and Hemingway (2001) Biochem. J. 357, 65-72]. To determine the nature of GSTs involved in conferring this resistance, the GSTs from resistant and susceptible
Engineering a Disulfide Bond in Recombinant Manganese Peroxidase Results in Increased Thermostability
Reading, N.S., and Aust, S.D.
Biotechnol. Progress, 16(3), 326-333 (2000)
Sofia R Pauleta et al.
Biochemistry, 43(35), 11214-11225 (2004-09-16)
The gene for pseudoazurin was isolated from Paracoccus pantotrophus LMD 52.44 and expressed in a heterologous system with a yield of 54.3 mg of pure protein per liter of culture. The gene and protein were shown to be identical to
L Shilpa Satheesh et al.
Indian journal of experimental biology, 49(5), 366-374 (2011-05-28)
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
Fatah Chérifi et al.
The protein journal, 29(7), 466-474 (2010-08-19)
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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