TA-IMAC FF is a metal chelating affinity chromatography medium that can be widely used for the separation and purification of proteins and peptides. The principle of TA-IMAC FF is to utilize the interaction of histidine, cysteine and tryptophan side chains of proteins with various transition metal ions, such as Cu2+, Zn2+, Ni2+, Co2+, and Fe3+, so as to achieve the purpose of separation and purification.
TA-IMAC FF is made of crosslinked agarose and ammonia triacetic acid (NTA), which can chelate the tetravalent level of metal ions, making the chelated metal ions more stable, tolerating a certain concentration of reducing agent, possessing the advantages of good physical and chemical stability, good specificity, and fast flow rate.
Specifications:
| Product |
TA-IMAC FF |
| Appearance |
White slurry, forms visible layering upon standing |
| Agarose Concentration |
6% |
| Particle Size Range |
45–165 µm |
| Metal Chelating Capacity |
Ni2+, Zn2+: 15 µmol/mL
Cu2+: 25 µmol/mL |
| Dynamic Binding |
Ni2+: approx. 40 mg/mL his-tagged protein/medium |
| Max. Pressure Tolerance |
0.3 MPa |
| Chemical Stability |
When metal ion are removed:
Stable in 40℃ for 1 week: 10mM HCl, 0.1M NaOH, 8M urea, 6M guanidine hydrochloride
40℃ for 12 hours: 1M NaOH, 70% acetic acid |
| pH Stability |
3–12 (operating), 2–14 (CIP, metal ion removed) |
| Recommended Flow Rate |
<150 cm/h |
| Storage Conditions |
2–30 °C, 20% ethanol or 2% benzyl alcohol |
