The S-tag is one of many intrinsically unstructured peptides which only adopts a defined structure on binding to a structured substrate. The S-tag is incorporated into many vectors including the pET29 and 30 series, pCITE-3 and pCITE-4. The S-tag sequence was incorporated into many expression systems and is detectable with certain antibody reagents allowing researchers to check the size and correct expression of recombinant proteins. Proteins including the S-tag can be purified using a column to which is bound the RNAse-S-prot. The modern nomenclature for the enzyme is RNAase A or RNAse 1.
This antibody was made against a synthetic 53 amino acid peptide which is the sequence included in pET30a(+) and other vectors. A C-terminal cysteine was added to allow coupling to maleate activated KLH which was used as the immunogen. Numerous clones were screened by their ability to bind the immunogen and then re-screened for inhibition of this binding by the S-tag peptide. The bovine S-tag sequence is not well conserved across species boundaries, so this antibody is not likely to useful as a general marker for RNAase-1 from other species.
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