S Tag Peptide 目录号 GP10155 |
Sample solution is provided at 25 µL, 10mM.
Quality Control & SDS
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Purity > 98.00%
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S Tag Peptide Dilution Calculator

S Tag Peptide Molarity Calculator
Cas No. | N/A | SDF | |
别名 | H-Lys-Glu-Thr-Ala-Ala-Ala-Lys-Phe-Glu-Arg-Gln-His-Met-Asp-Ser-OH | ||
化学名 | S Tag | ||
Canonical SMILES | CC(C(C(=O)NC(C)C(=O)NC(C)C(=O)NC(C)C(=O)NC(CCCCN)C(=O)NC(CC1=CC=CC=C1)C(=O)NC(CCC(=O)O)C(=O)NC(CCCNC(=N)N)C(=O)NC(CCC(=O)N)C(=O)NC(CC2=CN=CN2)C(=O)NC(CCSC)C(=O)NC(CC(=O)O)C(=O)NC(CO)C(=O)O)NC(=O)C(CCC(=O)O)NC(=O)C(CCCCN)N)O | ||
分子式 | C73H117N23O25S | 分子量 | 1748.91 |
溶解度 | ≥ 174.9mg/mL in DMSO, ≥ 50 mg/mL in H2O | 储存条件 | Desiccate at -20°C |
General tips | For obtaining a higher solubility , please warm the tube at 37 ℃ and shake it in the ultrasonic bath for a while.Stock solution can be stored below -20℃ for several months. | ||
Shipping Condition | Evaluation sample solution : ship with blue ice All other available size: ship with RT , or blue ice upon request |
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, it is 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 ribonuclease activity. This 15 amino acids long peptide is called S15 or S-tag.
It is believed that the peptide with its abundance of charged and polar residues could improve solubility of proteins it is attached to. Moreover, the peptide alone is thought not to fold into a distinct structure. On DNA-level the S-tag can be attached to the N- or C-terminus of any protein. After gene expression, such a tagged protein can be detected by commercially available antibodies. [1]
References:
1. R.T. Raines et al., The S-Tag Fusion System for Protein Purification. Methods Enzymol. 326, 362-367 (2000)