Traptavidin is the S52G, R53D mutant of streptavidin, the high affinity biotin binding protein. Useful in various imaging, protein purification, and nano-assembly applications.
Streptavidin binds biotin-conjugates with exceptional stability, but dissociation does occur and can be limiting in imaging, DNA amplification, and nanotechnology. This Traptavidin protein overcomes these limitations with a ~10-fold slower biotin off-rate, increased mechanical strength, and improved thermostability compared to streptavidin.
From the laboratory of Mark Howarth, PhD, University of Oxford.
|Source:||Recombinant, expressed in E. coli|
|Molecular Weight:||13.2 kDa (without boiling, traptavidin will run on SDS-PAGE as a tetramer and remain bound to biotin)|
|Amino Acid Sequence:||AEAGITGTWYNQLGSTFIVTAGADGALTGTYESAVGNAEGDYVLTGRYDSAPATDGSGTALGWTVAWKNNYRNAHSATTWSGQYVGGAEARINTQWLLTSGTTEANAWKSTLVGHDTFTKVKPSAAS|
|Purity:||>98% by SDS PAGE (Purified from inclusion body refolding with selective ammonium sulfate precipitation and then iminobiotin-agarose affinity chromatography.)|
|Buffer:||Phosphate buffered saline (PBS) pH 7.4; The protein is highly stable and should be compatible with a wide range of salts, ionic strengths and pH values (certainly 5-9), as well as DMF or DMSO up to 10%.|
|Concentration:||3.36 mg/mL in PBS.|
|Comments:||10-fold lower off-rate from biotin and biotin conjugates compared to streptavidin. Increased thermal stability and mechanical stability of biotin binding.|
|Storage:||-80°C, stable for 1-2 weeks when kept at 4°C (avoid multiple freeze-thaw cycles)|
Traptavidin has a reduced on-rate compared to streptavidin, depending on the nature of the biotin conjugate; binding should still be rapid when working with high concentrations of biotinylated target, but for binding sub-micromolar concentrations of biotinylated target then longer should be allowed for binding than would be required for streptavidin.
If you publish research with this product, please let us know so we can cite your paper.