Fusion of the peptide or protein which we called 'tag' into the target protein can increase the expression level, solubility, folding, purification and detection of the recombinant protein. The affinity-tag systems always have the following features:
One strategy for large-scale production of recombinant proteins is to use small peptide labels that do not interfere with the fusion protein. The most commonly used small peptide tags are Flag, HA, His, Myc.
Flag tag (DYKDDDDK) is a common, well-characterized hydrophilic tag. It is always used in conjunction with antibodies in protein pull-downs to study protein interactions. Flag tag can be incorporated on N-, C- or internal positions of the target protein.
HA tag (YPYDVPDYA) is derived from the human influenza hemagglutinin (HA) molecule corresponding to amino acids 98-106, and it is an ideal tag for co-IP and western blots, with small interference to the function of protein. HA tag has been extensively used as a general epitope tag in expression vectors.
His tag (HHHHHH) is the most common affinity tag used to purify proteins. His-Tag purification tag combined with metal chelate affinity chromatography provides a powerful tool for the separation and purification of recombinant proteins.
Myc tag (EQKLISEEDL) is a small, immunoreactive tag, and can be placed at the N- or C- terminus. Myc tag is a popular epitope tag for detecting the expression of recombinant proteins in yeast, bacteria, insect, and mammalian cell systems.
Creative Peptides has extensive experience in the preparation of peptide-tagged fusion proteins. In the process of tagged peptide synthesis, we are skilled in the use of various markers, and we have expressed and purified a number of peptide-tagged fusion proteins in bacterial, yeast and mammalian cells. If necessary, we can also use spacers to separate the tags from the peptide. Every step of peptide synthesis is subject to Creative Peptides' stringent quality control. Typical delivery specifications include:
Peptide tags are short peptide sequences fused to target proteins to enhance their expression, solubility, and purification. These tags, such as His, Flag, and HA, enable efficient protein production and analysis, simplifying the process of studying protein interactions and structures.
The most popular peptide tags include Flag (DYKDDDDK), HA (YPYDVPDYA), His (HHHHHH), and Myc (EQKLISEEDL). Each tag offers unique benefits for applications like protein pull-downs, co-immunoprecipitation (Co-IP), and affinity chromatography.
The Flag tag is a hydrophilic peptide sequence commonly used in protein-protein interaction studies. It is ideal for protein pull-down experiments and can be inserted at the N-, C-, or internal positions of the target protein without disrupting its function.
The His tag facilitates protein purification through metal chelate affinity chromatography. Its ability to bind to metal ions like nickel or cobalt makes it one of the most effective and widely-used methods for purifying recombinant proteins.
The HA tag is a small epitope derived from the influenza hemagglutinin protein, commonly used for Western blotting and co-immunoprecipitation (Co-IP) experiments. It is designed to cause minimal interference with the target protein's function, making it ideal for protein expression analysis.
Yes, peptide tags can be easily and specifically removed after purification, allowing the production of native proteins. This is especially useful in studies where the tag may interfere with the protein's function or structure.
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