ChromoBlog

GFP-Trap^®Multiwell Plate for convenient high throughput analysis of protein interactions. It consists of our anti-GFP VHH immobilized in multiwell plates. The GFP-Trap Multiwell Plate is optimized for immunoprecipitation (IP), IP-MS, and ELISA. Here you can find the protocol for sandwich ELISA und immunoprecipitation (IP) with GFP-Trap

New iST Nano-Trap kits for immunoprecipitation (IP) and sample preparation for mass spectrometry (MS) in just 4 easy steps:

GFP-Booster and RFP-Booster conjugated to Alexa Fluor® 488, 568 and 647:

• Stronger signal in confocal and standard fluorescence microscopy
• More options in super-resolution microscopy including STORM and MINFLUX
• Constant degree of labeling (DOL = 2 dyes per Booster) for higher resolution
• More than 95% labeling efficiency

GFP-Trap^® Dynabeads is optimized for the immunoprecipitation (IP) of large GFP-tagged proteins and for Co-IP of protein complexes. It consists of ChromoTek’s established anti-GFP Nanobody conjugated to Dynabeads™. Hence, also GFP-Trap Dynabeads has the very high affinity of 1 pM like GFP-Trap Agarose and Magnetic Agarose.

Affinity tags are very useful tools for protein purification. Fused to the protein of interest, they streamline the purification process by binding to a tag-specific resin. Obviously, tag selection is an important step as the purification tag can affect expression level, solubility, facilitate correct folding, protect from proteolysis, and re-direct proteins to a cellular compartment. In addition, the purification tag determines the affinity resin used.

Bispecific T cell engagers are bispecific antibodies designed to link T cells with cancer cells. The simultaneous binding of the bispecific antibody to T cell and tumor cell initiates the activation of the T cell. For this purpose, the bispecific antibody carries two antigen binding domains against the T cell (often CD3 T cell receptor) and against a cell surface protein of the tumor cell.

ChromoTek offers two bispecific T cell engagers:

Crystal structure of the anti-GFP VHH-Green Fluorescent Protein complex.
The GFP Nanobody is displayed blue and the GFP in green color.

UV crosslinking techniques are the method of choice for a comprehensive analysis of in-vivo-mRNA targets of an RNA-binding protein (RBP). In the recent publication of Olgeiser et al. (2019), the authors applied individual-nucleotide resolution UV crosslinking and immunoprecipitation (iCLIP) to study fungal mRNA transport. For this approach, they have used strains expressing GFP-tagged versions of the two RBPs Grp1 and Rrm4; an optimized protocol was developed to uncover that Grp1 and Rrm4 conjointly bind thousands of shared target messenger ribonucleoproteins (mRNPs) in the fungus U. maydis. The protein:RNA complexes were immunoprecipitated in a multiple detergent containing buffer using ChromoTek’s GFP-Trap Magnetic Agarose. This is a transcriptome‐wide view to an endosomal mRNA transport machinery.

Jellyfish Green Fluorescent Protein (GFP) and its derivatives are still the most frequently used fluorescent proteins in biomedical research. Recently, additional green fluorescent proteins have been discovered in higher animals such as crustaceans and lancelets. These FPs share a common fold, but diverge widely in their primary sequence. Thus, they require novel, dedicated antibody research tools. Here is an overview about EGFP (the most commonly used GFP derivative), TurboGFP and mNeonGreen.

Chromotek’s GFP- binding protein, an anti- GFP Nanobody, is a very small and effective tool for binding and visualizing GFP-tagged proteins. In their recent publication, Modi et al. successfully functionalized quantum dots with the GFP- Nanobody (QD GFP- Nanobody). Thus, they created a small GFP- specific label with a very strong fluorescent signal.

TurboGFP is a bright green fluorescent protein used to study protein function, localization and dynamics in cells. Nanobody based research tools allow reproducible biochemical analysis including mass spectrometry and enzyme activity measurements of TurboGFP fusion proteins.