Tagged proteins are essential tools in modern research. With various tagging options, our recombinant proteins provide the versatility needed for different experimental workflows.

Purification tags: Tags like His-tag, GST, and FLAG make the purification process much simpler and more efficient. These tags allow proteins to be isolated quickly and specifically by using affinity chromatography. They bind only to certain ligands and make it easier to separate the protein of interest or the target protein from the rest of the cellular material. This saves time and improves the overall purity of the final protein sample.

Solubility and stability tags: Tags such as maltose-binding protein (MBP) and glutathione S-transferase (GST) are added to proteins to improve their solubility and stability. This means the proteins are less likely to form aggregates or degrade during experiments, making them much easier to work with. Maintaining protein integrity is crucial for achieving consistent and reliable results, especially in challenging experimental conditions.

Detection and quantification tags: Certain tags make it easier to detect and measure proteins in different types of assays, such as western blotting, immunoprecipitation, and flow cytometry. Tagged proteins are particularly useful for studying how proteins interact with each other, which is essential for uncovering the intricacies of cellular processes and signaling pathways. This ability to track and quantify proteins accurately plays a key role in both basic research and clinical studies.

Structural analysis tags: Tags are also valuable tools for structural studies, helping researchers crystallize proteins and analyze their three-dimensional structures. Understanding a protein’s 3D shape is vital for learning how it functions and for designing targeted therapeutics. Structural tags streamline this process, making it easier to obtain high-quality data for pre-clinical drug development and biological research.

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What are tagged proteins?

Tagged proteins are recombinant proteins with specific tags that facilitate purification, detection, and structural analysis.

How do purification tags work?

Purification tags bind to specific ligands, allowing proteins to be isolated using affinity chromatography. His-tag (histidine tag) is a peptide tag that binds to metal ions, such as nickel or cobalt. GST (Glutathione S-transferase) is a fusion tag that binds to glutathione-coated resins. GFP (Green Fluorescent Protein) functions as a large fusion tag, enabling both purification and real-time visualization. FLAG tag (DYKDDDDK) is a short epitope tag that binds to anti-FLAG antibodies or specific resins for precise purification.

What are the benefits of solubility and stability tags?

Tags such as MBP and GST enhance the solubility and stability of proteins, making them easier to work with during experiments.

How are tagged proteins used in detection and quantification?

Tagged proteins facilitate the detection and quantification of proteins in various assays, including Western blotting, immunoprecipitation, and flow cytometry.

Why are tags important for structural analysis?

Tags help in the crystallization and structural analysis of proteins, aiding in the determination of their 3D structures, which is vital for understanding protein function and designing targeted therapeutics.