400-998-5282
专注多肽 服务科研
400-998-5282
专注多肽 服务科研
S-tag是一种来源于胰腺核糖核酸酶 A的标签肽。
编号：188345
CAS号：7429-70-1
单字母：H2N-KETAAAKFERQHMDS-OH
S-tag是一种来源于胰腺核糖核酸酶 A的标签肽。
S Tag Peptide 是一种合成的多肽，由15个氨基酸残基构成。
S Tag Peptide is a 15 amino acid peptide derived from RNase A.
S Tag是胰核糖核酸酶A（RNase A）衍生的的寡肽。如果RNase A用枯草杆菌蛋白酶（subtilisin）消化，单肽键被裂解，得到两个保持弱结合的产物，该蛋白被称为核糖核酸酶S，仍具有活性，但两个产物单独不具有酶活性。原RNase A的N端，也称为S-肽，由20个氨基酸组成，只有前15个氨基酸是核糖核酸酶活性所必须的。这15个氨基酸的长肽被称为S15或S-tag。
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.
据报道，富含带电和极性残基的多肽可改善它所连接蛋白的溶解性。而且，多肽单独不能折叠成独特的结构。在DNA水平，S-tag可以附着在任何蛋白的N端或C端。基因表达后，这种标签蛋白可通过商业化的抗体来检测。
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)
Peptide H-KETAAAKFERQHMDS-OH is a Research Peptide with significant interest within the field academic and medical research. Recent citations using H-KETAAAKFERQHMDS-OH include the following: Structure and design of Langya virus glycoprotein antigens Z Wang, M McCallum , L Yan - Proceedings of the , 2024 - National Acad Scienceshttps://www.pnas.org/doi/abs/10.1073/pnas.2314990121 A peptidyl linker for protein cross-linking catalyzed by microbial transglutaminase T Tanaka, N Kamiya , T Nagamune - Asian Pacific Confederation of , 2004 - jstage.jst.go.jphttps://www.jstage.jst.go.jp/article/apcche/2004/0/2004_0_377/_article/-char/ja/ Suppression of wild-type rhodopsin maturation by mutants linked to autosomal dominant retinitis pigmentosa RS Rajan, RR Kopito - Journal of Biological Chemistry, 2005 - ASBMBhttps://www.jbc.org/article/S0021-9258(20)76501-4/abstract Site-specific cross-linking of functional proteins by transglutamination N Kamiya , T Takazawa, T Tanaka , H Ueda - Enzyme and Microbial , 2003 - Elsevierhttps://www.sciencedirect.com/science/article/pii/S0141022903001546 Combinatorics of peptide sextets encoded by a single microgene K Kashiwagi, K Shiba - Journal of Molecular Catalysis B: Enzymatic, 2004 - Elsevierhttps://www.sciencedirect.com/science/article/pii/S1381117704000918 Epitope mapping of antibodies against S-tagged fusion proteins and molecular weight markers K Daskalow, P Boisguerin , B Jandrig - Bioscience , 2008 - academic.oup.comhttps://academic.oup.com/bbb/article-abstract/72/2/346/5941340 Display of functional proteins on supramolecular peptide nanofibrils using a split-protein strategy JTM DiMaio, DM Raymond, BL Nilsson - Organic & Biomolecular , 2017 - pubs.rsc.orghttps://pubs.rsc.org/en/content/articlehtml/2017/ob/c7ob01057e The soluble recombinant N-terminal domain of HMW 1Dx5 and its aggregation behavior JJ Wang, GY Liu , G Liu, QH Zeng, X Shen - Food Research , 2015 - Elsevierhttps://www.sciencedirect.com/science/article/pii/S0963996915302209 Crystallographic structure of an active, sequence-engineered ribonuclease. HC Taylor, A Komoriya - Proceedings of the , 1985 - National Acad Scienceshttps://www.pnas.org/doi/abs/10.1073/pnas.82.19.6423 Protein trans-splicing and functional mini-inteins of a cyanobacterial dnaB intein H Wu, MQ Xu, XQ Liu - Biochimica et Biophysica Acta (BBA)-Protein , 1998 - Elsevierhttps://www.sciencedirect.com/science/article/pii/S0167483898001575 Efficient endotoxin removal from T7 phage preparations by a mild detergent treatment followed by ultrafiltration H Hashemi , S Pouyanfard , M Bandehpour - Acta Virol, 2013 - researchgate.nethttps://www.researchgate.net/profile/Michele-Bernasconi/publication/256488791_Efficient_endotoxin_removal_from_T7_phage_preparations_by_a_mild_detergent_treatment_followed_by_ultrafiltration/links/5f861c9f458515b7cf7f5d9e/Efficient-endotoxin-removal-from-T7-phage-preparations-by-a-mild-detergent-treatment-followed-by-ultrafiltration.pdf Folding-Unfolding Dynamics of pH-Assisted Structures of S-Peptide DS Perumalla , G Govind , P Anjukandi - ChemistrySelect, 2020 - Wiley Online Libraryhttps://chemistry-europe.onlinelibrary.wiley.com/doi/abs/10.1002/slct.202000360 In silico tandem affinity purification refines an Oct4 interaction list CY Cheong, PM Lon Ng , R Ponnampalam - Stem cell research & , 2011 - Springerhttps://link.springer.com/article/10.1186/scrt67 Molecular Tags for Proteins and Their Biological Applications A Basak , S Basak - Current Proteomics, 2018 - ingentaconnect.comhttps://www.ingentaconnect.com/content/ben/cp/2018/00000015/00000005/art00010
专肽生物可以提供常见抗体制备、免疫学研究等生物科研需求的各类标签多肽（Tag peptide）以及蛋白底物产品，可用荧光标记(FITC、5-Fam)等。除常见抗体中抗原决定部位的标签多肽（tag: His | c-Myc | HA | FLAG | V5 | X-press | VSV tag | T7 tag | Snoop tag | E-tag | Sof tag 1 | Spy tag |等等），我们还提供各类定制标签肽的合成，并可提供荧光标记(FITC、5-Fam)等。同时，免费提供的MS和HPLC分析报告。
| DOI | 名称 | |
|---|---|---|
| 10.1016/s0076-6879(00)26065-5 | The S.Tag fusion system for protein purification | 下载 |
| 10.1016/j.celrep.2021.108708 | Semi-automated single-molecule microscopy screening of fast-dissociating specific antibodies directly from hybridoma cultures | 下载 |
