G100120
Sephadex® G-100
Medium
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About This Item
Quality Level
form
powder
technique(s)
LPLC: suitable
matrix
Agarose
matrix active group
polymer
swelling
1 g swells to 15-20 mL gel
bead size
40-120 μm
separation technique
size exclusion (SEC)
General description
Sephadex® is composed of repeating glucose units attached by α-1,6 glucosidic bonds. This structure ensures more aptamer binding sites and greater binding capacity. It is suitable for large-scale purification and is considered stable and can be utilized more than once.
Fractionation Range (MW)
Globular Proteins: 4,000 - 150,000
Dextrans: 1,000 - 100,000
Fractionation Range (MW)
Globular Proteins: 4,000 - 150,000
Dextrans: 1,000 - 100,000
Application
Sephadex®G-100 is a gel filtration medium used in protein chromatography, affinity chromatography and gel filtration chromatography
It has been used:
It has been used:
- in gel filtration column for α-amylase purification
- in gel filtration column for the purification of polysaccharidic fraction extracted from the skin of the ray Raja radula
- to remove excess protamine by size exclusion from cross-linked iron oxide (CLIO)-protamine-linked (B) peptides
Other Notes
G100120-100G′s updated product number is GE17-0060-01
Legal Information
Sephadex is a registered trademark of Cytiva
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Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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R H Coleman et al.
Current microbiology, 32(3), 147-150 (1996-03-01)
Pseudomonas syringae isolate BR2R produces tabtoxin, a beta-lactam-containing antibiotic, and the causative agent of wildfire disease of green bean (Phaseolus vulgaris). beta-Lactamase production has been suggested as the mechanism that protects P. syringae from tabtoxin. We sought to determine whether
Production, purification and characterization of an a-amylase produced by <I>Saccharomycopsis fibuligera</I>
Gogoi, B.K., et al.
Journal of Applied Microbiology, 63(5), 373-379 (1987)
Ahmed K A El-Sayed et al.
International journal of biological macromolecules, 132, 1274-1281 (2019-04-07)
AmyLa α-amylase gene from Laceyella sp. DS3 was heterologously expressed in E. coli BL21. E. coli BL21 maximally expressed AmyLa after 4 h of adding 0.02 mM IPTG at 37 °C. The recombinant AmyLa α-amylase was purified 2.19-fold through gel filtration and ion
Global Trade Item Number
| SKU | GTIN |
|---|---|
| G100120-500G | 04061832011301 |
| G100120-10G | 04061838551528 |
| G100120-50G | 04061833624630 |