205379-07-3Relevant articles and documents
Protein Delivery System Containing a Nickel-Immobilized Polymer for Multimerization of Affinity-Purified His-Tagged Proteins Enhances Cytosolic Transfer
Postupalenko, Viktoriia,Desplancq, Dominique,Orlov, Igor,Arntz, Youri,Spehner, Danièle,Mely, Yves,Klaholz, Bruno P.,Schultz, Patrick,Weiss, Etienne,Zuber, Guy
, p. 10583 - 10586 (2015)
Recombinant proteins with cytosolic or nuclear activities are emerging as tools for interfering with cellular functions. Because such tools rely on vehicles for crossing the plasma membrane we developed a protein delivery system consisting in the assembly
Synthesis of a pH-sensitive nitrilotriacetic linker to peptide transduction domains to enable intracellular delivery of histidine imidazole ring-containing macromolecules
June, Ronald K.,Gogoi, Khirud,Eguchi, Akiko,Cui, Xian-Shu,Dowdy, Steven F.
, p. 10680 - 10682 (2010)
Intracellular delivery of functional macromolecules using peptide transduction domains (PTDs) is an exciting technology with both experimental and therapeutic applications. Recent data indicate that PTD-mediated transduction occurs via fluid-phase macropi
Oriented insertion of phi29 N-hexahistidine-tagged gp10 connector protein assemblies into C20BAS bolalipid membrane vesicles
Hyun, Seok-Hee,Kim, Hee-Kwon,Kim, Jong-Mok,Thompson, David H.
, p. 17053 - 17055 (2010)
Ni2+:NTA-PEG600-grafted glass surfaces are capable of immobilizing N-his6 gp10 connector protein assemblies from the phi29 DNA packaging motor and mediating their transplantation into bolalipid vesicles whose membrane thickness is co
A supramolecular host-guest carrier system for growth factors employing VHH fragments
Cabanas-Dans, Jordi,Rodrigues, Emilie Dooms,Landman, Ellie,Van Weerd, Jasper,Van Blitterswijk, Clemens,Verrips, Theo,Huskens, Jurriaan,Karperien, Marcel,Jonkheijm, Pascal
, p. 12675 - 12681 (2014)
A supramolecular strategy is presented for the assembly of growth factors employing His6-tagged single-domain antibodies (VHH). A combination of orthogonal supramolecular interactions of β-cyclodextrin (βCD)-adamantyl (Ad) host-guest
Simple and efficient knockdown of His-tagged proteins by ternary molecules consisting of a His-tag ligand, a ubiquitin ligase ligand, and a cell-penetrating peptide
Hattori, Takayuki,Okitsu, Koyo,Yamazaki, Norikazu,Ohoka, Nobumichi,Shibata, Norihito,Misawa, Takashi,Kurihara, Masaaki,Demizu, Yosuke,Naito, Mikihiko
, p. 4478 - 4481 (2017)
We designed and synthesized hybrid molecules for a protein knockdown method based on the recognition of a His-tag fused to a protein of interest (POI). The synthesized target protein degradation inducers contained three functional moieties: a His-tag liga
High-affinity chelator thiols for switchable and oriented immobilization of histidine-tagged proteins: A generic platform for protein chip technologies
Tinazli, Ali,Tang, Juin,Valiokas, Ramunas,Picuric, Srdjan,Lata, Suman,Piehler, Jacob,Liedberg, Bo,Tampe, Robert
, p. 5249 - 5259 (2005)
Protein micro/nanoarrays are becoming increasingly important in systematic approaches for the exploration of protein-protein interactions and dynamic protein networks, so there is a high demand for specific, generic, stable, uniform, and locally addressab
Grid coatings for capture of proteins and other compounds
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Page/Page column 19-21, (2021/04/28)
Grids comprising a coating modified with one or more capture agents and a deactivating agent are disclosed. Methods of using such grids in connection with suitable microscopy techniques, such as for determining the structure of target compounds including proteins, are also disclosed.
Assessing changes in the expression levels of cell surface proteins with a turn-on fluorescent molecular probe
Hatai, Joydev,Prasad, Pragati Kishore,Lahav-Mankovski, Naama,Oppenheimer-Low, Noa,Unger, Tamar,Sirkis, Yael Fridmann,Dadosh, Tali,Motiei, Leila,Margulies, David
supporting information, p. 1875 - 1878 (2021/03/01)
Tri-nitrilotriacetic acid (NTA)-based fluorescent probes were developed and used to image His-tagged-labelled outer membrane protein C (His-OmpC) in liveEscherichia coli. One of these probes was designed to light up upon binding, which provided the means
Optimized reaction pair of the Cyshis tag and Ni(II)-Nta probe for highly selective chemical labeling of membrane proteins
Zenmyo, Naoki,Tokumaru, Hiroki,Uchinomiya, Shohei,Fuchida, Hirokazu,Tabata, Shigekazu,Hamachi, Itaru,Shigemoto, Ryuichi,Ojida, Akio
supporting information, p. 995 - 1000 (2019/07/18)
Chemical labeling of proteins with synthetic molecular probes offers the possibility to probe the functions of proteins of interest in living cells. However, the methods for covalently labeling targeted proteins using complementary peptide tag-probe pairs are still limited, irrespective of the versatility of such pairs in biological research. Herein, we report the new CysHis tag-Ni(II) probe pair for the specific covalent labeling of proteins. A broad-range evaluation of the reactivity profiles of the probe and the CysHis peptide tag afforded a tag-probe pair with an optimized and high labeling selectivity and reactivity. In particular, the labeling specificity of this pair was notably improved compared to the previously reported one. This pair was successfully utilized for the fluorescence imaging of membrane proteins on the surfaces of living cells, demonstrating its potential utility in biological research.
The Scaffold Design of Trivalent Chelator Heads Dictates Affinity and Stability for Labeling His-tagged Proteins in vitro and in Cells
Gatterdam, Karl,Joest, Eike F.,Gatterdam, Volker,Tampé, Robert
supporting information, p. 12395 - 12399 (2018/09/18)
Small chemical/biological interaction pairs are at the forefront in tracing protein function and interaction at high signal-to-background ratios in cellular pathways. However, the optimal design of scaffold, linker, and chelator head still deserve systematic investigation to achieve the highest affinity and kinetic stability for in vitro and especially cellular applications. We report on a library of N-nitrilotriacetic acid (NTA)-based multivalent chelator heads (MCHs) built on linear, cyclic, and dendritic scaffolds and compare these with regard to their binding affinity and stability for the labeling of cellular His-tagged proteins. Furthermore, we describe a new approach for tracing cellular target proteins at picomolar probe concentrations in cells. Finally, we outline fundamental differences between the MCH scaffolds and define a cyclic trisNTA chelator that displays the highest affinity and kinetic stability of all reported reversible, low-molecular-weight interaction pairs.