Saturday, August 13, 2016

Protein Purification Solutions

Strep-tag®Tools + Strep-Tactin Columns

We are seeing a notable uptick in use of our Protein Purification Tools. This includes vectors and purification columns. We are especially delighted with the increased use of of our Strep-Tag + Strep-Tactin Columns.
Figure: Strep-Tag+Strep-Tactin Methods
Here's an example of researchers using the technology to purify heme proteins for the study of the diptheria pathogen: Courtni E. Allen and Michael P. Schmitt. Utilization of Host Iron Sources by Corynebacterium diphtheriae: Multiple Hemoglobin-Binding Proteins Are Essential for the Use of Iron from the Hemoglobin-Haptoglobin Complex. J. Bacteriol. February 2015 vol. 197 no. 3 553-562. doi: 10.1128/JB.02413-14...Cell debris was removed by centrifugation at 12,000 × g at 4°C, and the supernatant fraction containing the soluble protein was purified on Strep-Tactin columns (Neuromics) for Strep-tagged constructs...

Figure: (A) HtaA and derivatives were assessed for the ability to bind Hb-Hp by ELISA. GST was included as a negative control. Experiments were repeated at least three times, with similar results. Results of a representative experiment are shown. (B) Binding of HtaA and various derivatives to Hb-Hp at a 200 nM concentration is shown. Binding of HtaA-Y361A and CR2-Y361A to Hb-Hp was significantly different from binding with HtaA-wt and CR2, respectively (**, P less than 0.0001). Binding of CR1 to Hb-Hp was significantly different from that with HtaA-wt (***, P less than 0.05). *, HtaA does not bind Hp (HtaA-Hp). Values represent the means from three independent experiments (±SD).

Looking for protein purification solutions? Do not hesitate to contact me: 612-801-1007 or

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