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UNSPSC Code:
41115711
eCl@ss:
32110501
NACRES:
NB.21
L × i.d.:
5 cm × 7.8 mm
Particle size:
10 μm
Matrix active group:
iminodiacetic acid phase
Pore size:
1000 Å
Matrix:
polymer particle platform
产品名称
TSKgel® BioAssist® Chelate HPLC Column, phase iminodiacetic acid, L × I.D. 5 cm × 7.8 mm, 10 μm particle size, PEEK hardware
material
PEEK hardware
product line
TSKgel®
manufacturer/tradename
Tosoh 20022
extent of labeling
20 μmol/mL resin ligand density
parameter
≤20% organic solvent, ≤3 M salt concentration, ≤45 °C temperature, 1.2 mL/min flow rate, 10 bar max. pressure
technique(s)
HPLC: suitable
L × I.D.
5 cm × 7.8 mm
matrix
polymer particle platform
matrix active group
iminodiacetic acid phase
particle size
10 μm
pore size
1000 Å
operating pH
2-12
separation technique
affinity
General description
High efficiency, resin-based TSKgel affinity columns (10 μm particles) separate or purify many enzymes and other proteins.
TSKgel Chelate-5PW columns utilize the tendency of iminodiacetic acid (IDA) to form a complex with metal ions, such as Zn2+, Ni2+ and Cu2+. The column is loaded with divalent metal ions by chelation. Peptides and proteins containing histidine residues will normally adsorb to these chelated ions at neutral pH. The retained compounds can be eluted with buffer containing imidazole or glycine. The key to making successful use of this retention mechanism is the proper selection of metal ions for chelation and the elution buffer to desorb the analytes. In general, Cu2+, interacts better with proteins; however, resolution is usually enhanced with Zn2+. A gradient mobile phase containing increasing imidazole or glycine concentrations is used to elute the retained compounds. Alternatively, a decreasing pH gradient can be used for elution purposes as well.
Applications include: immunoglobulins, transferrin, lectins, milk proteins, membrane proteins and peptides.
TSKgel Chelate-5PW columns utilize the tendency of iminodiacetic acid (IDA) to form a complex with metal ions, such as Zn2+, Ni2+ and Cu2+. The column is loaded with divalent metal ions by chelation. Peptides and proteins containing histidine residues will normally adsorb to these chelated ions at neutral pH. The retained compounds can be eluted with buffer containing imidazole or glycine. The key to making successful use of this retention mechanism is the proper selection of metal ions for chelation and the elution buffer to desorb the analytes. In general, Cu2+, interacts better with proteins; however, resolution is usually enhanced with Zn2+. A gradient mobile phase containing increasing imidazole or glycine concentrations is used to elute the retained compounds. Alternatively, a decreasing pH gradient can be used for elution purposes as well.
Applications include: immunoglobulins, transferrin, lectins, milk proteins, membrane proteins and peptides.
Legal Information
BioAssist is a registered trademark of Tosoh Corporation
TSKgel is a registered trademark of Tosoh Corporation
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