ChromoBlog

How fluorescent proteins can be applied in SARS-CoV-2 research

Posted by Dr. Astrid Sitte on May 14, 2020 12:28:52 PM
Fluorescent proteins (FPs) like GFP or RFP and their derivatives are commonly used for virus research. Frequently, they are applied as fluorescent markers in microscopy or cell sorting experiments and as protein tags for protein purification, immunoprecipitation or protein-protein interaction assays. Here, we provide a short outline that describes how FPs have been used in the current SARS-CoV-2 research. Please note that this summary does not provide a complete overview; also, many referenced papers are pre-prints without peer reviews.
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SNAP-tag and CLIP-tag

Posted by Christoph Eckert on May 7, 2020 9:34:17 AM

SNAP-tag and CLIP-tag are self-labeling protein tags. The SNAP-tag protein and the CLIP-tag protein can be fused to a protein of interest (POI) and used for cellular and biochemical analysis.

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Topics: VHH, Nanobody, SNAP

HaloTag

Posted by Christoph Eckert on May 5, 2020 2:47:26 PM

HaloTag is a protein tag. The HaloTag protein can be fused to your protein of interest (POI) which enables it for cellular and biochemical analysis. It can also be used for live cell imaging.

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Topics: VHH, Nanobody

Do you purify a special protein?

Posted by Dr. Astrid Sitte on Apr 24, 2020 9:33:54 AM

Why Spot-Tag can be used to purify any protein

 

Introduction

Proteins often have very different individual characteristics and requirements for manipulation. Not every purification tag in combination with the desired purification resin is suitable for every protein. Some proteins are sensitive towards wash or elution buffers, while others are difficult to purify because the selected affinity resin can be contaminated by host cell proteins. Taking these points into consideration, the selection of both the affinity tag and the affinity resin can have a strong impact on protein purity and yield, which is often dependent on the target protein. Requirements for an affinity resin comprise (i) high purity (minimal contaminations), (ii) high yield of the purified protein, and (iii) a broad buffer stability. Ideally, affinity tags should be (iv) inert and (v) short in order to not or minimally affect the purified protein.

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Topics: Spot-Tag

Chromobodies for live cell imaging

Posted by Brandon Dinehart on Apr 16, 2020 4:27:04 PM

What’s a Chromobody?

Chromobodies® are fluorescent nanoprobes for real-time and live-cell imaging of intracellular endogenous proteins. A Chromobody is a small intracellular functional antibody. It consists of a VHH/Nanobody that is genetically fused to a fluorescent protein. Plasmids encoding for Chromobodies can be transiently transfected into cells and the Chromobody protein is intracellularly expressed.

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Topics: Chromobodies, live cell imaging

Spot-Trap or Spot-Cap?

Posted by Stephanie Dennison on Apr 9, 2020 4:40:23 PM

Our Sales Rep Stephanie Dennison answers one of the most frequent customer questions:

Nano-Traps are a great tool for easy, clean immunoprecipitation, but certain VHHs bind so effectively that it can be difficult or impossible to do native elution without a TEV cleavage site. After receiving feedback from our customers, we understood the need for capturing proteins in applications like affinity purification and then getting them off the bead while preserving their structure and function. We launched Nano-Caps in early 2020 starting with Spot-Cap®.

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Partnership with The Antibody Registry

Posted by Klaus Herick on Apr 8, 2020 4:42:06 PM

ChromoTek is excited to announce that it has partnered with The Antibody Registry to assign unique identifiers, RRIDs, to ChromoTek’s line of Nanobody based immunoreagents and antibodies. Both the Antibody Registry and ChromoTek are displaying the RRIDs so researchers can reliably find these identifiers, required by many of the top scientific journals on both.

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Green fluorescent protein (GFP) in plant research

Posted by Dr. Astrid Sitte on Apr 1, 2020 5:02:51 PM
Although the jellyfish Aequorea Victoria Green fluorescent protein (GFP) was already discovered in the 1960s, it took three more decades until it was eventually cloned and could be utilized as a marker protein in E.coli and C. elegans. Since then it has developed into one of the most widely studied and exploited proteins in life sciences. Correspondingly, the importance of GFP was recognized in 2008 when the Nobel Committee awarded Osamu Shimomura, Marty Chalfie, and Roger Tsien the Chemistry Nobel Prize "for the discovery and development of the green fluorescent protein, GFP."
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Topics: GFP, A. Thaliana, plant research

Virus research using GFP

Posted by Dr. Astrid Sitte on Mar 26, 2020 1:05:30 PM

An extract of the published literature since 2016

This blog provides references from the last 4 years in virus research using GFP. Most publications report how immunoprecipitation (IP)/Co-IP of GFP-fusions was conducted to identify host cell binding partners of virus proteins. In addition, mass spectrometry analysis and functional assays have been performed.

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Topics: GFP

Abstract on Nano-BiTEs: Bispecific T cell engagers based on nanobodies

Posted by Christian Linke-Winnebeck on Mar 23, 2020 11:13:01 AM

Christian Linke-Winnebeck[1]; Michael Metterlein[1]; Larisa Yurlova[1]; Sabrina Wendler[1]; Simge Yüz[2]; Björn Tränkle[3]; Jacqueline Boger[1]; Tanja Ertl[1]; Felix Hartlepp[1]

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Topics: Nano-BiTEs

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