Product introduction
Ni-6FF (TED) can be used for separation and purification with the interactions between Ni2+and some amino acids (mainly include histidine, cysteine, tryptophan) on the side chain of protein, and it is suitable for separation and purification of His-tagged protein and biological molecules which interact with Ni2+. The strong binding Ni2+ can be directly used for His-tagged protein expressed by eukaryotic expression system, and it have resistance for higher concentration of reductant and chelating agent. In addition, sample pretreatment is unnecessary. The cleaning and reviving of media are simple, which can be washed directly without nickel removal.
Advantages
1. Quick and easy (one-step purification).
2. Tolerate to higher concentration of reductant and chelating agent. His-tagged protein expressed by eukaryotic expression system can be loading without pretreatment, which can protect the protein activity to the utmost.
3. There is no need to remove nickel removal can wash with NaOH directly, which greatly shorten the cleaning period.
4. Lower Ni2+ abscission than Ni-6FF (IMAC) and Ni-6FF (IDA). No need of repeated revival.
Performance index
Matrix | Highly cross-linked 6% agarose |
Particle size range | 45-165 µm |
Average particle size | 90 µm |
Binding capacity | 20~30 mg (His-tagged protein)/mL (media) |
pH stability | 3-12 (working) 2-14 (washing) |
Chemical stability | 0.01MHCl, 0.01M NaOH (1 week) 20 mM EDTA, 10 mM DTT, 1M NaOH, 8M Urea, 6M Guanidine hydrochloride (24 hours) 100 mM EDTA, 0.5M Iminazole (2 hours) 30% Isopropyl alcohol (20 minutes) |
Flow rate | 150-600 cm/h (0.3MPa, XK16/40. Column bed height:30 cm) |
Pressure | ≤ 0.3 MPa |
Storage buffer | 20% Ethanol |
Storage temperature | 4~8℃ |
Application examples
Example 1:
Example 2:
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