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Exclusive Ni-Super Resin Product for His-tag Protein Purification released

Abbkine Scientific unravels an exclusive Ni-Super Resin portfolio under the Purification tools category called PurKine™ His-Tag Ni-Super Resin which is said to be featured two prominent advantages compared to Ni-NTA and Ni-IDA, high tolerance and easy cleaning.

Expression and purification of recombinant protein is the foundation of studying protein structure, regulation and function. To simplify purification, affinity purification tags are often fused to a recombinant protein of interest.The most popular tag is the polyhistidine (6xHis) tag. Some proteins, like eukaryotic proteins may not exhibit proper protein activity or folding if expressed in E.coli . Cultured mammalian cells or insect cells might be better option. However, the low expression levels of recombinant proteins in those cells presents a challenge for their purification.

Structure of Ni-IDA, Ni-NTA and Ni-Super

Structure of Ni-IDA, Ni-NTA and Ni-Super shows Ni-Super has two prominent advantages compared to Ni-NTA and Ni-IDA with higher tolerance and easier cleaning.

Abbkine PurKine™ Ni-Super Resin is designed mainly for capturing and purification of histidine-tagged proteins secreted into eukaryotic cell, such as yeast, mammalian, and insect culture supernatants. PurKine™ Ni-Super Resin is a new immobilized metal ion affinity chromatography (IMAC) medium precharged with nickel ions via a proprietary, chemical-stable linker technology. The Resin consists of 90um beads of highly cross-linked 4% agarose, to which Super replacement to NTA has been coupled. Compared to Ni-NTA and Ni-IDA, Ni-Super resin has prominent advantages.

  • High toleration— More tolerable to various chemicals including reducing, chelating agents. The nickel ions have been shown to remain bound to the chelating ligand even after incubation for 24 hours in 10 mM EDTA.
  • Low nickel ion leaching— Best option for samples that can cause Ni stripping from the medium, like secreted proteins in liquids containing chelators. Do not need repeated regeneration.
  • Time-saving sample preparation— Direct loading of samples without extra pre-treatment procedures, enabling purification of low concentrations of target proteins at large volumes.
  • Easy cleaning— Directly use NaOH to cleaning-in-place, reducing cleaning cycle.

Ni-Super resin is more tolerable to various chemicals including reducing, chelating agents. The nickel ions have been shown to remain bound to the chelating ligand even after incubation for 24 hours with 10 mM EDTA. When cleaning, directly use NaOH. It is easy to pack and use, and its fast flow properties make it excellent for scaling-up. 

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PurKine™ His-Tag Purification system is based on innovative high-capacity IMAC matrix for convenient single-step purifications of His-tag proteins from total lysates. Our propriety ion-chelate chemistry ensures extraordinary compatibility with commonly used reducing agents such as DTT, chelating metalloprotease inhibitors such as EDTA, and a wide range of buffer substances and salt conditions. The portfolio provides wide choice of chelating group (IDA, NTA or Super NTA), cross-linked agarose (crosslinked 4% or 6% agarose), ions (Nick, Colbat, Copper, or non ion charged) and compatible ingredients to allow optimization of process for maximum protein yield, stability and solubility. Tests also confirm that no decrease in performance occurs after at least five repeated uses. The PurKine™ His-Tag Purification resin is also available as prepacked spin column and kit formats.

Abbkine Scientific Co, Ltd was founded by a number of scientists and marketing experts in the field of life science in California in 2012. With growing demands from Asia Pacific, it move its headquarters to China. Abbkine started featured and exclusive products from protein detection tools, and devoted to developing and providing the most innovative solutions for global customers covering all kinds of antibodies, biochemicals, proteins and assay kits.

  • Editor Rating

  • Rated 5 stars
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  • Last modified: January 22, 2017
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