We started in the lab 30 years ago.
So the best purification resins are simply a higher standard we've come to expect.

Highly purified recombinant proteins are used in many areas of biomedical science, and many diverse methods exist for the expression and purification of proteins(1,2,3). As an example, the first steps of most protein structure determination efforts involve obtaining milligram quantities of highly pure protein. Anatrace is excited to offer most of the commonly used purification resins with superb performance at the right price.

Affinity Purification
Our Super-Nickel and Super-Cobalt resins are designed for affinity purification of poly-histidine tagged proteins through immobilized metal ion affinity chromatography (IMAC). IMAC was first described in 1975(4) based on the premise that certain amino acids, like histidine, can act as electron donors and bind reversibly to transition metal ions (e.g. Ni2+, Co2+, Cu2+, Zn2+) which are immobilized on a nitrilotriacetic (NTA) matrix(5). In practice, a 6-12x poly-histidine tag is engineered at the N or C-terminus of a recombinant protein. Nickel and Cobalt are the most widely used metal ions as they confer the highest affinity (Ni2+ > Co2+) with the highest specificity (Co2+ > Ni2+) for the IMAC tags.

For the purification of glutathione S-transferase (GST)-tagged proteins, we offer our Super-GLU glutathione coupled agarose resin. Another common method of purification, the 26 kDa GST protein is typically engineered as a fusion construct to the N or C-terminus of a recombinant protein(6). This GST protein binds to the glutathione resin, allowing for washing, and elution with reduced glutathione. Additionally, GST may help promote greater expression, solubility, and folding of recombinant proteins.  

Affinity tags are often removed after purification; however, one thing to keep in mind for membrane proteins is the variable detergent sensitivity of proteases that are used to remove these tags(7).

Immunoglobulin Purification
Affinity purification of monoclonal antibodies has been largely confined to the use of Protein A and Protein G chromatography. Our immobilized Protein A and Protein G resins are designed for simple, one-step and rapid antibody purification from serum, ascites and tissue culture supernatant such as those derived from static cultures and bioreactors. Protein A is a cell wall protein from Staphylococcus aureus that binds specifically to the Fc region of immunoglobulin molecules of many mammalian species(8). Protein G is a cell wall protein from group C and G Streptococci that binds strongly to the Fc region of IgG(9). Protein G is specific for IgG, and can bind to a wider range of immunoglobulins compared to Protein A, such as rat IgG2a, IgG2b, human IgG3, bovine IgG1 and sheep IgG1.

Introducing New Heparin Resin
The latest addition to our line of protein purification resins is our Super Heparin High Performance Resin. Heparin is a highly sulfated glycosaminoglycan with an average molecular weight of 12-15 kDa. When immobilized to agarose, heparin can interact with proteins in two ways: as a cation exchanger due to the high degree of sulfation, or through specific interaction with its carbohydrate backbone(10). Heparin resin is mainly used to purify nucleic acid binding proteins, but can also be used in the purification of enzymes, hormone receptors, and extracellular matrix proteins. 
 
All of our protein purification resins are available as loose resin, or prepacked in 1 ml and 5 ml HiFliQ columns compatible with any FPLC instrument. Also, click here for our full list of Anatrace protein purification tools, including empty FPLC columns, protein concentrators, and size-exclusion columns.


        

To make things even sweeter, until September 30th, we're offering 10% off your order of purification resins and HiFliQ FPLC Columns.  Just contact customerservice@anatrace.com for details.
 


 
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