ProteIndex™ Chemical-Tolerant Ni-Penta™ resins are specifically designed for capture and purification of polyhistidine-tagged proteins in much broader range of chemical agents, in comparison with conventional NTA-functionalized resins.
Ni-Penta™ affinity resins are able to retain high selectivity for polyhistidine in various buffer conditions. They are particularly ideal for purification applications that require the presence of EDTA and reducing agents (ie. DTT, β-ME) for the integrity and stability of the target protein. Therefore, the use of Ni-Penta resin allows the most stabilizing conditions for the target protein throughout the entire purification procedure. Furthermore, Ni-Penta™ resins are well suited for direct capture of polyhistidine-tagged proteins that are secreted into eukaryotic cell culture supernatant (i.e. CHO cells, other mammalian cells, and insect High Five™ cells* and Sf9 cells). Dialysis of sample to remove inhibitory agents prior to loading is usually not required.
The C. difficile toxin B membrane translocation machinery is an evolutionarily conserved protein delivery apparatus. Orrell KE, Mansfield MJ, Doxey AC, Melnyk RA. Nat Commun. 2020 Jan 23;11(1):432. PMID: 31974369
A Unique Protein Self-Assembling Nanoparticle with Significant Advantages in Vaccine Development and Production. DC Carter, B Wright, WG Jerome, JP Rose et al., Journal of Nanomaterials, 2020
Expression and purification of affinity-tagged variants of the photochemical reaction center from Heliobacterium modesticaldum. Orf GS, Redding KE. Photosynth Res. 2019 Dec;142(3):335-348. PMID: 31542861
Palladin Compensates for the Arp2/3 Complex and Supports Actin Structures during Listeria Infections.Dhanda AS, Vogl AW, Albraiki SE, Otey CA, Beck MR, Guttman JA. MBio. 2018 Apr 10;9(2). PMID: 29636431
Ubiquitinated Proteins Isolated from Tumor Cells Are Efficient Substrates for Antigen. Guangjie Yu, Tarsem Moudgil, Zhihua Cui, Yongbin Mou, Lixin Wang, Bernard A. Fox, and Hong-Ming Hu. J Immunotherapy 2017 Jun;40(5):155-163. PMID: 28368960
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