FLAG Peptide TFA salt

FLAG peptide is an eight amino acids peptide (Asp-Tyr-Lys-Asp-Asp-Asp-Asp-Lys) with an enterokinase-cleavage site; designed for antibody-mediated identification and purification of recombinant proteins.

Signaling Pathways >> Others >> Others

Research Areas >> Inflammation/Immunology

Peptides

Fusion protein technology has become an important tool for solving numerous problems linked to recombinant protein production. The properties of the additional tag facilitate identification and provide a one-step purification procedure of the fusion protein by passing cell extracts or supernatants through columns of an appropriate matrix. FLAG peptide allows elution under non-denaturing conditions. Several antibodies against FLAG peptide have been developed. One antibody, M1, binds the peptide in the presence of bivalent metal cations, preferably Ca2+. Elution is effected by chelating agents. Another strategy is competitive elution with excess of free FLAGe peptide. Antibodies M2 and M5 are applied in this procedure[1]. The Flag-tag is first described as a calcium-dependent epitope of a monoclonal antibody. It is a highly acidic octapeptide which can be N-terminally fused to the protein of interest. As a very hydrophilic peptide the Flag–tag has a high surface probability. Flag-fusion proteins can be captured by an immunoaffinity column in the presence of Ca2+ and eluted byEDTA at low concentrations, neutral pH and thus, nearly physiological conditions[2].

[1]. Einhauer A, et al. The FLAG peptide, a versatile fusion tag for the purification of recombinant proteins. J Biochem Biophys Methods. 2001 Oct 30;49(1-3):455-65.

[2]. Schuster M, et al. Protein expression in yeast; comparison of two expression strategies regarding proteinmaturation. J Biotechnol. 2000 Dec 28;84(3):237-48.

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