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| Size | List Price | Price | Cart |
|---|---|---|---|
| 100 ul | $329.00 | Add to Cart |
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. Product Highlights: |
Images
Western blot analysis of 0.25µg of recombinant proteins expressed in pET family vectors and which all contain the S-tag sequence. They were probed with mouse mAb, MO22206, dilution 1:5,000 in green: [1] protein standard (red), [2] aldolase A, [2] myelin basic protein, [4] MAP2, P2 projection domain, [5] FOX2 C terminal region and [6] MAP2, P3 projection domain. The antibody binds to the S-tag present in all tested recombinant proteins and reveals protein bands of expected molecular size.
Western blot analysis of bovine pancreas tissue lysate using mouse mAb to S-tag protein, MO22206, dilution 1:2,000 in green: [1] protein standard (red), [2] 40µg of bovine pancreas. Strong band at about 15 kDa corresponds to intact RNAse A containing the S-tag sequence.