NTA-Co3+-His6 versus NTA-Ni2+-His6 mediated E-Cadherin surface immobilization enhances cellular traction
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چکیده
منابع مشابه
Cobalt(III) as a Stable and Inert Mediator Ion between NTA and His6-Tagged Proteins**
Don't let go! The Co(3+)-mediated interaction between nitrilotriacetic acid (NTA) and the His6-tag is so stable and inert towards ligand exchange that it has a half-life of 7 days in the presence of imidazole and survives even under strongly chelating as well as reducing conditions, unlike the commonly used Ni(2+) or Co(2+) complexes. Possible applications include the separation of labeled prot...
متن کاملControlling Protein Surface Orientation by Strategic Placement of Oligo-Histidine Tags
We report oriented immobilization of proteins using the standard hexahistidine (His6)-Ni2+:NTA (nitrilotriacetic acid) methodology, which we systematically tuned to give control of surface coverage. Fluorescence microscopy and surface plasmon resonance measurements of self-assembled monolayers (SAMs) of red fluorescent proteins (TagRFP) showed that binding strength increased by 1 order of magni...
متن کامل2 Dta 2 Nta Nta
15 2DTA 2NTA NTA p MITL k U k DTA Figure 5: Relationship between various classes Theorem 5.2 The membership problem for 2NTA is solvable in PSPACE. Proof. Consider a 2NTA A, and let k be the magnitude of the largest constant appearing in a clock constraint in the transitions of A. Given a timed word w = (;) of length n, deene R w to be the set comprising of i + c and (i + j + c)=2 for 1 i; j n ...
متن کاملDouble-hexahistidine tag with high-affinity binding for protein immobilization, purification, and detection on ni-nitrilotriacetic acid surfaces.
There is a particular need in protein analysis and purification for specific, functional, and generic methods of protein immobilization on solid supports. Here we describe a double-hexahistidine (His6) tag sequence, comprising two hexahistidines separated by an 11-amino acid spacer, which shows at least 1 order of magnitude stronger binding to Ni-NTA-modified surfaces than a conventional single...
متن کاملOligohis-tags: mechanisms of binding to Ni2+-NTA surfaces.
Since immobilized metal ion affinity chromatography (IMAC) was first reported, several modifications have been developed. Among them, Ni(2+) immobilized by chelation with nitrilotriacetic acid (NTA) bound to a solid support has become the most common method for the purification of proteins carrying either a C- or N-terminal histidine (His) tag. Despite its broad application in protein purificat...
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ژورنال
عنوان ژورنال: Biomaterials
سال: 2019
ISSN: 0142-9612
DOI: 10.1016/j.biomaterials.2018.10.042