Business Directory, Press Releases, Jobs, Products, Services, Articles
Businesses Articles Press Releases Follow @PRcom
Press Release Pricing | News by Category | News by Country | News by US Region | Recent News | News on Your Site
MoBiTec GmbH

Company Overview

Contact Info & Offices

Press Releases


MoBiTec GmbH

Press Release

Receive press releases from MoBiTec GmbH: By Email RSS Feeds:

Now Available at MoBiTec: Ni-IDA Columns for Fast Purification of His-Tagged Proteins

MoBiTec Ni-IDA Columns containing a superior silica-based IDA resin provide a fast and convenient routine tool for purification of recombinant polyhistidine-tagged proteins by gravity flow.

Goettingen, Germany, June 05, 2015 --( Poly-histidine tags are often used for affinity purification of poly-histidine-tagged recombinant proteins expressed in Escherichia coli, Bacillus megaterium, Bacillus subtilis, and other prokaryotic expression systems. A poly-histidine tag is an amino acid motif in proteins that consists of multiple histidine (His) residues, mostly located at the N- or C-terminus of the protein. In order to facilitate the detection of successfully expressed his-tagged proteins the usage of anti-poly-histidine antibodies is a prevalent technique.

The form-stable silica matrix is precharged with Ni2+ ions and allows purification on the principle of Immobilized Metal Ion Affinity Chromatography (IMAC). Binding of proteins is based on the interaction between the polyhistidine tag of the recombinant protein and immobilized Ni2+ ions. The chelating group of the Ni-IDA resin is based on IDA (iminodiacetic acid), which enables strong and efficient binding of target protein onto the IMAC matrix.

In contrast to traditional IDA matrices, MoBiTec Ni-IDA is an optimized matrix with low density of IDA ligands. This non-saturating surface concentration of IDA eliminates almost all non-specific interactions of contaminating host proteins with the adsorbent. As a result, MoBiTec Ni-IDA provides higher target protein purity.

IDA is a tridentate chelator which occupies three of the six binding sites in the coordination sphere of the Ni2+ ion. The remaining three coordination sites are usually occupied by water molecules and can be exchanged with histidine residues of the recombinant protein.


• Excellent tool for routine purification of recombinant polyhistidine-tagged proteins
• Purification under native and denaturating conditions
• Starting from diverse expression systems, e.g., E. coli, yeast, insect, and mammalian cells
• Maximal binding capacity: 90 mg protein per column
• Protein recovery rate >80%
• Improved target specificity by optimized silica-based Ni2+-IDA matrix
• Imidazol-free loading and washing buffer
• Columns are long-term storable when kept dry

About MoBiTec GmbH

MoBiTec GmbH (Goettingen, Germany) is a privately held company (founded in 1987) that offers research tools for molecular and cell biology. Products include DNA vectors for cloning and expression, cell transfection reagents and cell culture tools, immobilized and soluble enzymes, products for genomics and proteomics research, numerous antibodies and recombinant proteins, superior fluorescence reagents and kits, affinity chromatography products, as well as general laboratory equipment.

In parallel to its own product lines, MoBiTec distributes products from international companies in Germany. MoBiTec products are distributed worldwide, in Germany from their home office, in other countries by distributors.
Contact Information
MoBiTec GmbH
Arne Schulz

Click here to view the company profile of MoBiTec GmbH
Click here to view the list of recent Press Releases from MoBiTec GmbH
Promote Your Business