Well-characterized antibodies for epitope tags consisting of short sequences are widely used in the study of protein expression in various systems. The Nano-tag is a new streptavidin-binding peptide for both the purification and the detection of Nano-tagged proteins. This peptide possesses nanomolar-affinity for streptavidin and therefore is termed Nano-tag. The nano-tags have two types, Nano-tag15 (MDVEAWLGARVPLVET) and Nano-tag9 (MDVEAWLGAR), which bind to streptavidin with dissociation co

S-tag is the name of an oligopeptide derived from pancreatic ribonuclease A (RNase A). If RNase A is digested with subtilisin, a single peptide bond is cleaved, but the resulting two products remain weakly bound to each other and the protein, called ribonuclease S, remains active although each of the two products alone shows no enzymatic activity. The N-terminus of the original RNase A, also called S-peptide, consists of 20 amino acid residues, of which only the first 15 are required for ribon

Tandem affinity purification (TAP) is a purification technique for studying protein–protein interactions. It involves creating a fusion protein with a designed piece, the TAP tag, on the end. The original TAP method involves the fusion of the TAP tag to the C-terminus of the protein under study. The TAP tag consists of calmodulin binding peptide (CBP) from the N-terminal, followed by tobacco etch virus protease (TEV protease) cleavage site and Protein A, which binds tightly to IgG. The relati

The T7 tag is an 11 amino acid peptide encoded in the leader sequence of T7 bacteriophage gene10. This gene encodes a T7 major capsid protein whose function is not clear. The T7 tag serves as a tag in many expression vectors including the pET system that is based on the very efficient T7 RNA polymerase expression system. Monoclonal antibodies specific for T7 tag are an important tool for studying expression of recombinant T7-tagged proteins.

The Strep-tag system is a method which allows the purification and detection of proteins by affinity chromatography. The Strep-tag is a synthetic peptide consisting of eight amino acids (Trp-Ser-His-Pro-Gln-Phe-Glu-Lys). This peptide sequence exhibits intrinsic affinity towards Strep-Tactin, a specifically engineered streptavidin and can be N- or C- terminally fused to recombinant proteins. By exploiting the highly specific interaction, Strep-tagged proteins can be isolated in one step from c

AmCyan1 is a human codon-optimized variant of the wild-type Anemonia majano cyan fluorescent protein (AmCyan) that exhibits enhanced emission characteristics (excitation and emission maxima: 458nm and 489nm, respectively). DD-AmCyan1 is a modified version of AmCyan1 that is tagged on its N-terminus with the ProteoTuner destabilization domain (DD). The presence of this destabilization domain causes rapid, proteasomal degradation of the fluorescent fusion protein; however, when the membrane per