1171:
Brune, Karl D.; LiekniĆa, Ilva; Sutov, Grigorij; Morris, Alexander R.; Jovicevic, Dejana; KalniĆĆĄ, Gints; KazÄks, Andris; Kluga, Rihards; Kastaljana, Sabine; Zajakina, Anna; Jansons, Juris; SkrastiĆa, Dace; Spunde, KarÄ«na; Cohen, Alexander A.; Bjorkman, Pamela J.; Morris, Howard R.; Suna, Edgars;
888:
De Genst, Erwin J.; Guilliams, Tim; Wellens, Joke; O'Day, Elizabeth M.; Waudby, Christopher A.; Meehan, Sarah; Dumoulin, Mireille; Hsu, Shang-Te Danny; Cremades, Nunilo; Verschueren, Koen H.G.; Pardon, Els; Wyns, Lode; Steyaert, Jan; Christodoulou, John; Dobson, Christopher M. (September 2010).
142:
for fluorescence imaging). Often tags are combined, in order to connect proteins to multiple other components. However, with the addition of each tag comes the risk that the native function of the protein may be compromised by interactions with the tag. Therefore, after purification, tags are
321:, an 18-amino-acid synthetic peptide (TKENPRSNQEESYDDNES) recognized by a monoclonal IgG1 antibody, which is useful in a wide spectrum of applications including Western blotting, ELISA, flow cytometry, immunocytochemistry, immunoprecipitation, and affinity purification of recombinant proteins
1879:
Kriznik, Alexandre; Yéléhé-Okouma, Mélissa; Lec, Jean-Christophe; Groshenry, Guillaume; Le
Cordier, HélÚne; Charron, Christophe; Quinternet, Marc; Mazon, Hortense; Talfournier, François; Boschi-Muller, Sandrine; Jouzeau, Jean-Yves; Reboul, Pascal (Oct 2018).
229:
CapTagâą is controlled by pH change (typically pH 8.5 to pH 6.2). Therefore, this technology can be adapted to a wide range of buffers adjusted to the target pH values of 8.5 and 6.2. The expected purity of target proteins or peptides is between 95-99%. The
596:. It is an 11-amino-acid peptide tag, and it can be fused to the N- or C-terminus or internal locations of proteins. Its small size leads to a rapid knock-in of this tag with other proteins through CRISPR/Cas9 technology.
830:
Götzke, Hansjörg; Kilisch, Markus; MartĂnez-Carranza, Markel; Sograte-Idrissi, Shama; Rajavel, Abirami; Schlichthaerle, Thomas; Engels, Niklas; Jungmann, Ralf; Stenmark, PĂ„l; Opazo, Felipe; Frey, Steffen (2019).
475:
degrader AGB1 to form a ternary complex between the "BromoTagged" protein and the E3 ligase VHL, leading to ubiquitination of the tagged protein and its subsequent rapid and effective proteasomal degradation in
69:
Chromatography tags are used to alter chromatographic properties of the protein to afford different resolution across a particular separation technique. Often, these consist of polyanionic amino acids, such as
438:, a peptide which binds covalently to SnoopCatcher protein (KLGDIEFIKVNK). A second generation, SnoopTagJr, was also developed to bind to either SnoopCatcher or DogTag (mediated by SnoopLigase) (KLGSIEFIKVNK)
302:
Gly-His-tags are N-terminal His-Tag variants (e.g. GHHHH, or GHHHHHH, or GSSHHHHHH) that still bind to immobilised metal cations but can also be activated via azidogluconoylation to enable click-chemistry
1286:
Keefe, Anthony D.; Wilson, David S.; Seelig, Burckhard; Szostak, Jack W. (2001). "One-Step
Purification of Recombinant Proteins Using a Nanomolar-Affinity Streptavidin-Binding Peptide, the SBP-Tag".
1930:
Schwinn, Marie K.; Machleidt, Thomas; Zimmerman, Kris; Eggers, Christopher T.; Dixon, Andrew S.; Hurst, Robin; Hall, Mary P.; Encell, Lance P.; Binkowski, Brock F.; Wood, Keith V. (2018-02-16).
127:(GFP) and its variants are the most commonly used fluorescence tags. More advanced applications of GFP include using it as a folding reporter (fluorescent if folded, colorless if not).
33:
Affinity tags are appended to proteins so that they can be purified from their crude biological source using an affinity technique. Affinity tags include chitin binding protein (CBP),
1229:"Assessment of cellular estrogenic activity based on estrogen receptor-mediated reduction of soluble-form catechol-O-methyltransferase (COMT) expression in an ELISA-based system"
184:
ALFA-tag, a de novo designed helical peptide tag (SRLEEELRRRLTE) for biochemical and microscopy applications. The tag is recognized by a repertoire of single-domain antibodies
697:
Schmidt, Thomas G.M.; Koepke, JĂŒrgen; Frank, Ronald; Skerra, Arne (1996). "Molecular
Interaction Between the Strep-tag Affinity Peptide and its Cognate Target, Streptavidin".
479:
84:
can be reliably produced in many different species. These are usually derived from viral genes, which explain their high immunoreactivity. Epitope tags include ALFA-tag,
1791:"Production in Escherichia coli and one-step purification of bifunctional hybrid proteins which bind maltose. Export of the Klenow polymerase into the periplasmic space"
327:, refers to the last 9 amino acids of the intracellular C-terminus of bovine rhodopsin (TETSQVAPA). It is a very specific tag that can be used for purification of
1120:
Prakriya, Murali; Feske, Stefan; Gwack, Yousang; Srikanth, Sonal; Rao, Anjana; Hogan, Patrick G. (2006). "Orai1 is an essential pore subunit of the CRAC channel".
444:
SdyTag, a peptide which binds covalently to SdyCatcher protein (DPIVMIDNDKPIT). SdyTag/SdyCatcher has a kinetic-dependent cross-reactivity with SpyTag/SpyCatcher.
1583:
Keeble, Anthony H.; Yadav, Vikash K.; Ferla, Matteo P.; Bauer, Claudia C.; Chuntharpursat-Bon, Eulashini; Huang, Jin; Bon, Robin S.; Howarth, Mark (July 2021).
30:
specific or are both C-terminus and N-terminus specific. Some tags are also inserted at sites within the protein of interest; they are known as internal tags.
248:
and its fragments. It can be used in research labs and it is intended for large-scale purification during downstream manufacturing process as well. The
2173:
441:
DogTag, a peptide which covalently binds to DogCatcher (DIPATYEFTDGKHYITNEPIPPK), and can also covalently bind to SnoopTagJr, mediated by SnoopLigase
639:
Mahmoudi Gomari, Mohammad; Saraygord-Afshari, Neda; Farsimadan, Marziye; Rostami, Neda; Aghamiri, Shahin; Farajollahi, Mohammad M. (December 2020).
482:(Fluorescence-Activating and absorption-Shifting Tag), a mutated photoactive yellow protein (PYP) that reversibly binds cognate fluorogenic ligands
2178:
1063:
1380:
Zakeri, Bijan; Howarth, Mark (2010). "Spontaneous
Intermolecular Amide Bond Formation between Side Chains for Irreversible Peptide Targeting".
26:. Tags are attached to proteins for various purposes. They can be added to either end of the target protein, so they are either C-terminus or
2188:
1996:
1773:
1703:"Development of BromoTag: A "Bump-and-Hole"âPROTAC System to Induce Potent, Rapid, and Selective Degradation of Tagged Target Proteins"
571:-tag, derived from immunoglobulin Fc domain, allow dimerization and solubilization. Can be used for purification on Protein-A Sepharose
488:-tag, an engineered variant of Colicin E7 that has a strong binding affinity and specificity for immobilized Immunity Protein 7 (Im7).
1882:"CRDSAT Generated by pCARGHO: A New Efficient Lectin-Based Affinity Tag Method for Safe, Simple, and Low-Cost Protein Purification"
381:, an epitope tag derived from the T7 major capsid protein of the T7 gene (MASMTGGQQMG). Used in different immunoassays as well as
1415:
Zakeri, Bijan; Fierer, Jacob O.; Celik, Emrah; Chittock, Emily C.; Schwarz-Linek, Ulrich; Moy, Vincent T.; Howarth, Mark (2012).
2112:
641:"Opportunities and challenges of the tag-assisted protein purification techniques: Applications in the pharmaceutical industry"
577:
1085:
Einhauer, A.; Jungbauer, A. (2001). "The FLAGâą peptide, a versatile fusion tag for the purification of recombinant proteins".
2183:
568:
1474:
Veggiani, Gianluca; Nakamura, Tomohiko; Brenner, Michael; Gayet, Raphael; Yan, Jun; Robinson, Carol; Howarth, Mark (2016).
1227:
Ho, Philip WL.; Tse, Zero HM.; Liu, HF.; Lu, S.; Ho, Jessica WM.; Kung, Michelle HW.; Ramsden, David B.; Ho, SL. (2013).
615:
787:
Zhang, Jin; Campbell, Robert; Ting, Alice; Tsien, Roger (2002). "Creating new fluorescent probes for cell biology".
2193:
256:
1341:"Catalytic Activity is Not Required for Secreted PCSK9 to Reduce Low Density Lipoprotein Receptors in HepG2 Cells"
2122:
2117:
1989:
497:
491:
369:(PDRVRAVSHWSS) for immunoprecipitation, affinity purification, immunofluorescence and super resolution microscopy
290:
124:
42:
1321:
375:, a peptide which binds to streptavidin or the modified streptavidin called streptactin (Strep-tag II: WSHPQFEK)
2198:
172:
2147:
551:
507:
34:
66:(TRX) and poly(NANP). Some affinity tags have a dual role as a solubilization agent, such as MBP and GST.
640:
1537:
605:
535:
521:
382:
1754:"Application of a Novel CL7/Im7 Affinity System in Purification of Complex and Pharmaceutical Proteins"
539:
548:, a sequence-specific single-stranded DNA binding protein that covalently binds to its target sequence
1982:
1655:
1487:
1428:
1240:
1129:
844:
245:
274:
polyarginine tag, a peptide binding efficiently to cation-exchange resin (from 5 to 9 consecutive R)
205:
574:
Designed
Intrinsically Disordered tags containing disorder promoting amino acids (P,E,S,T,A,Q,G,..)
117:
23:
1909:
1753:
1565:
1417:"Peptide tag forming a rapid covalent bond to a protein, through engineering a bacterial adhesin"
1209:
1173:
1153:
986:
812:
676:
271:
polyglutamate tag, a peptide binding efficiently to anion-exchange resin such as Mono-Q (EEEEEE)
236:
113:
931:
52:
Solubilization tags are used, especially for recombinant proteins expressed in species such as
1961:
1953:
1901:
1861:
1812:
1769:
1734:
1683:
1624:
1606:
1557:
1515:
1456:
1397:
1362:
1303:
1268:
1201:
1193:
1145:
1102:
1045:
1027:
978:
970:
913:
890:
870:
804:
766:
714:
668:
660:
435:
356:
350:
46:
2066:
557:
1943:
1893:
1851:
1843:
1802:
1761:
1724:
1714:
1673:
1663:
1614:
1596:
1549:
1505:
1495:
1446:
1436:
1389:
1352:
1295:
1258:
1248:
1185:
1137:
1094:
1035:
1017:
962:
905:
860:
852:
796:
756:
748:
706:
652:
620:
525:
400:
394:
378:
328:
261:
241:
109:
101:
85:
59:
1538:"SnoopLigase Catalyzes PeptideâPeptide Locking and Enables Solid-Phase Conjugate Isolation"
1006:"The Evolution of Intein-Based Affinity Methods as Reflected in 30 years of Patent History"
891:"Structure and Properties of a Complex of α-Synuclein and a Single-Domain Camelid Antibody"
458:
391:, a tetracysteine tag that is recognized by FlAsH and ReAsH biarsenical compounds (CCPGCC)
156:
485:
1659:
1491:
1432:
1244:
1133:
848:
1856:
1831:
1807:
1790:
1729:
1702:
1678:
1643:
1619:
1584:
1536:
Buldun, Can M.; Jean, Jisoo X.; Bedford, Michael R.; Howarth, Mark (14 February 2018).
1510:
1475:
1451:
1416:
1263:
1228:
1040:
1005:
865:
832:
761:
736:
134:
by biotin ligase) or chemical modification (such as coupling to other proteins through
1098:
951:"A Convenient Split-Intein Tag Method for the Purification of Tagless Target Proteins"
950:
49:
is a widely used protein tag, which binds to matrices bearing immobilized metal ions.
2167:
1569:
1213:
680:
656:
610:
252:
CapTagâą-target protein complex can be expressed in a wide range of expression hosts (
199:
188:
131:
1913:
1644:"Kinetic Controlled Tag-Catcher Interactions for Directed Covalent Protein Assembly"
833:"The ALFA-tag is a highly versatile tool for nanobody-based bioscience applications"
816:
1601:
1157:
990:
462:
344:
192:
144:
1642:
Tan, Lee Ling; Hoon, Shawn S.; Wong, Fong T.; Ahmed, S. Ashraf (26 October 2016).
198:
C-tag, a peptide that binds to a single-domain camelid antibody developed through
1719:
1668:
1253:
500:-tag, a protein which is spontaneously fluorescent and can be bound by nanobodies
225:), a self-removing peptide-based tag (MIKIATRKYLGKQNVYGIGVERDHNFALKNGFIAHN). The
2152:
1881:
1765:
562:
468:
63:
58:, to assist in the proper folding in proteins and keep them from aggregating in
1948:
1931:
856:
2096:
2049:
1022:
909:
752:
511:
471:
of Brd4, Brd4-BD2 L387A, that can be highly selectively bound by tag-specific
429:
425:
388:
139:
135:
81:
27:
1957:
1610:
1197:
1174:"N-Terminal Modification of Gly-His-Tagged Proteins with Azidogluconolactone"
1031:
974:
949:
Cooper, Merideth A.; Taris, Joseph E.; Shi, Changhua; Wood, David W. (2018).
664:
2091:
2043:
1500:
1441:
419:
372:
152:
38:
1965:
1932:"CRISPR-Mediated Tagging of Endogenous Proteins with a Luminescent Peptide"
1905:
1897:
1865:
1738:
1687:
1628:
1561:
1519:
1460:
1401:
1366:
1357:
1340:
1307:
1299:
1272:
1205:
1189:
1149:
1106:
1049:
982:
917:
874:
808:
770:
710:
672:
1816:
718:
324:
2137:
2132:
2086:
2019:
1553:
545:
531:
517:
366:
362:
280:
148:
97:
71:
1141:
422:, a peptide which binds covalently to pilin-C protein (TDKDMTITFTNKKDAE)
208:, a peptide bound by the protein calmodulin (KRRWKKNFIAVSAANRFKKISSSGAL)
80:
tags are short peptide sequences which are chosen because high-affinity
2142:
2127:
2081:
2037:
2031:
593:
503:
340:
308:
296:
89:
77:
54:
1847:
1393:
2071:
2025:
782:
780:
730:
728:
472:
318:
286:
160:
105:
93:
966:
457:(Biotin Carboxyl Carrier Protein), a protein domain biotinylated by
800:
120:
experiments, although they also find use in antibody purification.
2076:
334:
123:
Fluorescence tags are used to give visual readout on a protein.
1760:. Methods in Molecular Biology. Vol. 2466. pp. 61â82.
932:"CaptureSelect C-tag Affinity Matrix - Thermo Fisher Scientific"
454:
266:
130:
Protein tags may allow specific enzymatic modification (such as
1978:
1476:"Programmable polyproteams built using twin peptide superglues"
299:, 5-10 histidines bound by a nickel or cobalt chelate (HHHHHH)
1974:
1004:
Prabhala, Sai Vivek; Gierach, Izabela; Wood, David W. (2022).
312:
1339:
McNutt, Markey C.; Lagace, Thomas A.; Horton, Jay D. (2007).
580:-tag, a protein which binds to lactose agarose or Sepharose
1585:"DogCatcher allows loop-friendly protein-protein ligation"
737:"Plug-and-play pairing via defined divalent streptavidins"
735:
Fairhead M, Krndija D, Lowe ED, Howarth M (January 2014).
467:
BromoTag, a "bump-and-hole" mutated version of the second
409:
Xpress tag (DLYDDDDK), a peptide recognized by an antibody
406:
VSV-tag, a peptide recognized by an antibody (YTDIEMNRLGK)
277:
E-tag, a peptide recognized by an antibody (GAPVPYPDPLEPR)
16:
Artificial peptide attached to protein for marking purpose
337:, a peptide derived from Ribonuclease A (KETAAAKFERQHMDS)
191:
by the enzyme BirA and so the protein can be isolated by
1322:"Epitope Tags & Fusion Proteins â antibodies-online"
494:-tag, a protein which binds to immobilized glutathione
403:, a peptide recognized by an antibody (GKPIPNPLLGLDST)
2105:
2059:
2012:
1832:"Designing disorder: Tales of the unexpected tails"
1830:Minde, David P; Halff, Els F; Tans, Sander (2013).
143:sometimes removed by specific proteolysis (e.g. by
1925:
1923:
234:CapTagâą contains patented component derived from
22:are peptide sequences genetically grafted onto a
283:, a peptide recognized by an antibody (DYKDDDDK)
1789:Bedouelle, Hugues; Duplay, Pascale (Feb 1988).
1531:
1529:
1480:Proceedings of the National Academy of Sciences
1421:Proceedings of the National Academy of Sciences
265:cells). It is not intended for fully expressed
244:. This tag is used for protein purification of
1752:Chow, Louise T.; Vassylyev, Dmitry G. (2022).
1087:Journal of Biochemical and Biophysical Methods
554:-tag, a protein which binds to amylose agarose
1990:
1068:CapTagâą Technology - Protein Capture Science"
8:
173:Proteinogenic amino acid#Chemical properties
1997:
1983:
1975:
1701:Ciulli, Bond; Alessi, Craigon (Oct 2021).
353:, for mammalian expression (SLAELLNAGLGGS)
1947:
1855:
1806:
1728:
1718:
1677:
1667:
1618:
1600:
1509:
1499:
1450:
1440:
1356:
1262:
1252:
1039:
1021:
864:
760:
578:Carbohydrate Recognition Domain or CRDSAT
108:. These tags are particularly useful for
1542:Journal of the American Chemical Society
1382:Journal of the American Chemical Society
347:(MDEKTTGWRGGHVVEGLAGELEQLRARLEHHPQGQREP)
631:
359:, for prokaryotic expression (TQDPSRVG)
428:, a peptide which binds covalently to
315:recognized by an antibody (EQKLISEEDL)
293:recognized by an antibody (YPYDVPDYA)
7:
955:Current Protocols in Protein Science
692:
690:
1288:Protein Expression and Purification
1808:10.1111/j.1432-1033.1988.tb13823.x
1010:Frontiers in Molecular Biosciences
14:
1836:Intrinsically Disordered Proteins
2174:Biochemical separation processes
657:10.1016/j.biotechadv.2020.107653
1345:Journal of Biological Chemistry
592:was developed by Scientists at
2179:Biochemistry detection methods
1602:10.1016/j.chembiol.2021.07.005
175:for the A-Z amino-acid codes)
1:
1099:10.1016/S0165-022X(01)00213-5
1072:www.proteincapturescience.com
2189:Molecular biology techniques
1720:10.1021/acs.jmedchem.1c01532
1669:10.1371/journal.pone.0165074
1254:10.1371/journal.pone.0074065
1172:TÄrs, Kaspars (2021-11-16).
898:Journal of Molecular Biology
741:Journal of Molecular Biology
699:Journal of Molecular Biology
538:that covalently attaches to
524:that covalently attaches to
510:that covalently attaches to
365:, a peptide recognized by a
1766:10.1007/978-1-0716-2176-9_5
616:TimeSTAMP protein labelling
343:, a peptide which binds to
311:, a peptide derived from c-
187:AviTag, a peptide allowing
2215:
1949:10.1021/acschembio.7b00549
857:10.1038/s41467-019-12301-7
1326:www.antibodies-online.com
1023:10.3389/fmolb.2022.857566
910:10.1016/j.jmb.2010.07.001
753:10.1016/j.jmb.2013.09.016
498:Green fluorescent protein
492:Glutathione-S-transferase
125:Green fluorescent protein
43:glutathione-S-transferase
461:enabling recognition by
1758:Affinity Chromatography
1501:10.1073/pnas.1519214113
1442:10.1073/pnas.1115485109
552:Maltose binding protein
534:, a mutated eukaryotic
520:, a mutated eukaryotic
508:haloalkane dehalogenase
432:protein (AHIVMVDAYKPTK)
35:maltose binding protein
2060:10aa<length<50aa
1898:10.1002/biot.201800214
1358:10.1074/jbc.C700095200
1300:10.1006/prep.2001.1515
1190:10.1002/cbic.202100381
711:10.1006/jmbi.1996.0061
645:Biotechnology Advances
506:, a mutated bacterial
74:or polyglutamate tag.
62:. These tags include
2184:Laboratory techniques
1589:Cell Chemical Biology
961:(1): 5.29.1â5.29.23.
837:Nature Communications
789:Nat Rev Mol Cell Biol
606:Affinity purification
536:DNA methyltransferase
522:DNA methyltransferase
414:Covalent peptide tags
383:affinity purification
1936:ACS Chemical Biology
1554:10.1021/jacs.7b13237
936:www.thermofisher.com
246:recombinant proteins
167:List of protein tags
1713:(20): 15477â15502.
1660:2016PLoSO..1165074T
1492:2016PNAS..113.1202V
1433:2012PNAS..109E.690Z
1245:2013PLoSO...874065H
1142:10.1038/nature05122
1134:2006Natur.443..230P
849:2019NatCo..10.4403G
118:immunoprecipitation
24:recombinant protein
1595:(2): 339â350.e10.
237:Nostoc punctiforme
114:immunofluorescence
2194:Peptide sequences
2161:
2160:
1848:10.4161/idp.26790
1775:978-1-0716-2175-2
1394:10.1021/ja910795a
1351:(29): 20799â803.
1184:(22): 3199â3207.
329:membrane proteins
289:, a peptide from
195:(GLNDIFEAQKIEWHE)
138:or reaction with
2206:
1999:
1992:
1985:
1976:
1970:
1969:
1951:
1927:
1918:
1917:
1876:
1870:
1869:
1859:
1827:
1821:
1820:
1810:
1786:
1780:
1779:
1749:
1743:
1742:
1732:
1722:
1698:
1692:
1691:
1681:
1671:
1654:(10): e0165074.
1639:
1633:
1632:
1622:
1604:
1580:
1574:
1573:
1548:(8): 3008â3018.
1533:
1524:
1523:
1513:
1503:
1471:
1465:
1464:
1454:
1444:
1412:
1406:
1405:
1377:
1371:
1370:
1360:
1336:
1330:
1329:
1318:
1312:
1311:
1283:
1277:
1276:
1266:
1256:
1224:
1218:
1217:
1168:
1162:
1161:
1117:
1111:
1110:
1082:
1076:
1075:
1060:
1054:
1053:
1043:
1025:
1001:
995:
994:
946:
940:
939:
928:
922:
921:
895:
885:
879:
878:
868:
827:
821:
820:
784:
775:
774:
764:
732:
723:
722:
694:
685:
684:
636:
621:Western blotting
110:western blotting
60:inclusion bodies
2214:
2213:
2209:
2208:
2207:
2205:
2204:
2203:
2199:Protein methods
2164:
2163:
2162:
2157:
2101:
2055:
2008:
2003:
1973:
1929:
1928:
1921:
1878:
1877:
1873:
1829:
1828:
1824:
1788:
1787:
1783:
1776:
1751:
1750:
1746:
1700:
1699:
1695:
1641:
1640:
1636:
1582:
1581:
1577:
1535:
1534:
1527:
1473:
1472:
1468:
1414:
1413:
1409:
1379:
1378:
1374:
1338:
1337:
1333:
1320:
1319:
1315:
1285:
1284:
1280:
1226:
1225:
1221:
1170:
1169:
1165:
1128:(7108): 230â3.
1119:
1118:
1114:
1093:(1â3): 455â65.
1084:
1083:
1079:
1062:
1061:
1057:
1003:
1002:
998:
967:10.1002/cpps.46
948:
947:
943:
930:
929:
925:
893:
887:
886:
882:
829:
828:
824:
795:(12): 906â918.
786:
785:
778:
734:
733:
726:
696:
695:
688:
638:
637:
633:
629:
602:
587:
451:
416:
181:
169:
157:Enteropeptidase
17:
12:
11:
5:
2212:
2210:
2202:
2201:
2196:
2191:
2186:
2181:
2176:
2166:
2165:
2159:
2158:
2156:
2155:
2150:
2145:
2140:
2135:
2130:
2125:
2120:
2115:
2109:
2107:
2106:length>50aa
2103:
2102:
2100:
2099:
2094:
2089:
2084:
2079:
2074:
2069:
2063:
2061:
2057:
2056:
2054:
2053:
2047:
2041:
2035:
2029:
2023:
2016:
2014:
2013:length<10aa
2010:
2009:
2004:
2002:
2001:
1994:
1987:
1979:
1972:
1971:
1942:(2): 467â474.
1919:
1892:(4): 1800214.
1871:
1822:
1801:(3): 541â549.
1781:
1774:
1744:
1693:
1634:
1575:
1525:
1466:
1427:(12): E690â7.
1407:
1388:(13): 4526â7.
1372:
1331:
1313:
1278:
1219:
1163:
1112:
1077:
1055:
996:
941:
923:
904:(2): 326â343.
880:
822:
801:10.1038/nrm976
776:
747:(1): 199â214.
724:
686:
630:
628:
625:
624:
623:
618:
613:
608:
601:
598:
586:
583:
582:
581:
575:
572:
566:
560:
555:
549:
543:
540:benzylcytosine
529:
515:
501:
495:
489:
483:
477:
465:
450:
447:
446:
445:
442:
439:
433:
423:
415:
412:
411:
410:
407:
404:
398:
392:
386:
376:
370:
360:
354:
348:
338:
332:
322:
316:
306:
305:
304:
294:
284:
278:
275:
272:
269:
209:
206:Calmodulin-tag
203:
196:
185:
180:
177:
168:
165:
15:
13:
10:
9:
6:
4:
3:
2:
2211:
2200:
2197:
2195:
2192:
2190:
2187:
2185:
2182:
2180:
2177:
2175:
2172:
2171:
2169:
2154:
2151:
2149:
2146:
2144:
2141:
2139:
2136:
2134:
2131:
2129:
2126:
2124:
2121:
2119:
2116:
2114:
2111:
2110:
2108:
2104:
2098:
2095:
2093:
2090:
2088:
2085:
2083:
2080:
2078:
2075:
2073:
2070:
2068:
2065:
2064:
2062:
2058:
2051:
2048:
2045:
2042:
2039:
2036:
2033:
2030:
2027:
2024:
2021:
2018:
2017:
2015:
2011:
2007:
2000:
1995:
1993:
1988:
1986:
1981:
1980:
1977:
1967:
1963:
1959:
1955:
1950:
1945:
1941:
1937:
1933:
1926:
1924:
1920:
1915:
1911:
1907:
1903:
1899:
1895:
1891:
1887:
1883:
1875:
1872:
1867:
1863:
1858:
1853:
1849:
1845:
1841:
1837:
1833:
1826:
1823:
1818:
1814:
1809:
1804:
1800:
1796:
1795:Eur J Biochem
1792:
1785:
1782:
1777:
1771:
1767:
1763:
1759:
1755:
1748:
1745:
1740:
1736:
1731:
1726:
1721:
1716:
1712:
1708:
1704:
1697:
1694:
1689:
1685:
1680:
1675:
1670:
1665:
1661:
1657:
1653:
1649:
1645:
1638:
1635:
1630:
1626:
1621:
1616:
1612:
1608:
1603:
1598:
1594:
1590:
1586:
1579:
1576:
1571:
1567:
1563:
1559:
1555:
1551:
1547:
1543:
1539:
1532:
1530:
1526:
1521:
1517:
1512:
1507:
1502:
1497:
1493:
1489:
1486:(5): 1202â7.
1485:
1481:
1477:
1470:
1467:
1462:
1458:
1453:
1448:
1443:
1438:
1434:
1430:
1426:
1422:
1418:
1411:
1408:
1403:
1399:
1395:
1391:
1387:
1383:
1376:
1373:
1368:
1364:
1359:
1354:
1350:
1346:
1342:
1335:
1332:
1327:
1323:
1317:
1314:
1309:
1305:
1301:
1297:
1293:
1289:
1282:
1279:
1274:
1270:
1265:
1260:
1255:
1250:
1246:
1242:
1239:(9): e74065.
1238:
1234:
1230:
1223:
1220:
1215:
1211:
1207:
1203:
1199:
1195:
1191:
1187:
1183:
1179:
1175:
1167:
1164:
1159:
1155:
1151:
1147:
1143:
1139:
1135:
1131:
1127:
1123:
1116:
1113:
1108:
1104:
1100:
1096:
1092:
1088:
1081:
1078:
1073:
1069:
1067:
1059:
1056:
1051:
1047:
1042:
1037:
1033:
1029:
1024:
1019:
1015:
1011:
1007:
1000:
997:
992:
988:
984:
980:
976:
972:
968:
964:
960:
956:
952:
945:
942:
937:
933:
927:
924:
919:
915:
911:
907:
903:
899:
892:
884:
881:
876:
872:
867:
862:
858:
854:
850:
846:
842:
838:
834:
826:
823:
818:
814:
810:
806:
802:
798:
794:
790:
783:
781:
777:
772:
768:
763:
758:
754:
750:
746:
742:
738:
731:
729:
725:
720:
716:
712:
708:
705:(5): 753â66.
704:
700:
693:
691:
687:
682:
678:
674:
670:
666:
662:
658:
654:
650:
646:
642:
635:
632:
626:
622:
619:
617:
614:
612:
611:Protein array
609:
607:
604:
603:
599:
597:
595:
591:
584:
579:
576:
573:
570:
567:
564:
561:
559:
556:
553:
550:
547:
544:
541:
537:
533:
530:
527:
526:benzylguanine
523:
519:
516:
513:
509:
505:
502:
499:
496:
493:
490:
487:
484:
481:
478:
474:
470:
466:
464:
460:
456:
453:
452:
448:
443:
440:
437:
434:
431:
427:
424:
421:
418:
417:
413:
408:
405:
402:
399:
396:
393:
390:
387:
384:
380:
377:
374:
371:
368:
364:
361:
358:
355:
352:
349:
346:
342:
339:
336:
333:
330:
326:
323:
320:
317:
314:
310:
307:
301:
300:
298:
295:
292:
291:hemagglutinin
288:
285:
282:
279:
276:
273:
270:
268:
264:
263:
258:
255:
251:
247:
243:
239:
238:
233:
228:
224:
220:
217:
213:
210:
207:
204:
201:
200:phage display
197:
194:
190:
189:biotinylation
186:
183:
182:
178:
176:
174:
166:
164:
162:
158:
154:
150:
146:
141:
137:
133:
132:biotinylation
128:
126:
121:
119:
115:
111:
107:
103:
99:
95:
91:
87:
83:
79:
75:
73:
67:
65:
61:
57:
56:
50:
48:
47:poly(His) tag
44:
40:
36:
31:
29:
25:
21:
2040:(EQKLISEEDL)
2005:
1939:
1935:
1889:
1886:Biotechnol J
1885:
1874:
1839:
1835:
1825:
1798:
1794:
1784:
1757:
1747:
1710:
1706:
1696:
1651:
1647:
1637:
1592:
1588:
1578:
1545:
1541:
1483:
1479:
1469:
1424:
1420:
1410:
1385:
1381:
1375:
1348:
1344:
1334:
1325:
1316:
1294:(3): 440â6.
1291:
1287:
1281:
1236:
1232:
1222:
1181:
1177:
1166:
1125:
1121:
1115:
1090:
1086:
1080:
1071:
1065:
1058:
1013:
1009:
999:
958:
954:
944:
935:
926:
901:
897:
883:
840:
836:
825:
792:
788:
744:
740:
702:
698:
648:
644:
634:
600:Applications
589:
588:
463:streptavidin
449:Protein tags
397:(EVHTNQDPLD)
385:Mainly used
345:streptavidin
303:applications
260:
253:
249:
235:
231:
226:
222:
218:
215:
211:
193:streptavidin
179:Peptide tags
170:
145:TEV protease
129:
122:
76:
68:
53:
51:
45:(GST). The
32:
20:Protein tags
19:
18:
2028:(YPYDVPDYA)
2006:Protein tag
1842:(1): 5â15.
1178:ChemBioChem
843:(1): 4403.
563:Thioredoxin
542:derivatives
528:derivatives
469:bromodomain
64:thioredoxin
2168:Categories
2046:(WSHPQFEK)
2022:(DYKDDDDK)
1707:J Med Chem
1016:: 857566.
651:: 107653.
627:References
514:substrates
512:haloalkane
430:SpyCatcher
325:Rho1D4-tag
163:splicing.
140:FlAsH-EDT2
136:SpyCatcher
82:antibodies
28:N-terminus
2092:Isopeptag
2044:Strep-tag
1958:1554-8929
1611:2451-9456
1570:207189163
1214:237515136
1198:1439-7633
1032:2296-889X
975:1934-3655
681:226276355
665:0734-9750
590:HiBiT-tag
420:Isopeptag
373:Strep-tag
214:CapTagâą (
153:Factor Xa
39:Strep-tag
2138:CLIP-tag
2133:SNAP-tag
2113:BCCP-tag
2087:Spot-tag
2052:(CCPGCC)
2034:(HHHHHH)
2020:FLAG-tag
1966:28892606
1914:52942568
1906:30298550
1866:28516025
1739:34652918
1688:27783674
1648:PLOS ONE
1629:34324879
1562:29402082
1520:26787909
1461:22366317
1402:20235501
1367:17537735
1308:11722181
1273:24040167
1233:PLOS ONE
1206:34520613
1150:16921383
1107:11694294
1050:35463948
983:29516483
918:20620148
875:31562305
817:11588100
809:12461557
771:24056174
673:33157154
532:CLIP-tag
518:SNAP-tag
436:SnoopTag
367:nanobody
363:Spot-tag
357:Softag 3
351:Softag 1
281:FLAG-tag
149:Thrombin
98:Spot-tag
72:FLAG-tag
2153:TXN-tag
2148:MBP-tag
2143:HUH-tag
2128:HaloTag
2123:GFP-tag
2118:GST-tag
2082:SBP-tag
2067:iCapTag
2038:Myc-tag
2032:His-tag
1857:5424805
1817:3278900
1730:8558867
1679:5082641
1656:Bibcode
1620:8878318
1511:4747704
1488:Bibcode
1452:3311370
1429:Bibcode
1264:3765251
1241:Bibcode
1158:4310221
1130:Bibcode
1041:9033041
991:3749506
866:6764986
845:Bibcode
762:4047826
719:8636976
594:Promega
558:Nus-tag
546:HUH-tag
504:HaloTag
341:SBP-tag
309:Myc-tag
297:His-tag
90:Myc-tag
78:Epitope
55:E. coli
37:(MBP),
2097:SpyTag
2072:NE-tag
2050:TC tag
2026:HA-tag
1964:
1956:
1912:
1904:
1864:
1854:
1815:
1772:
1737:
1727:
1686:
1676:
1627:
1617:
1609:
1568:
1560:
1518:
1508:
1459:
1449:
1400:
1365:
1306:
1271:
1261:
1212:
1204:
1196:
1156:
1148:
1122:Nature
1105:
1048:
1038:
1030:
989:
981:
973:
916:
873:
863:
815:
807:
769:
759:
717:
679:
671:
663:
585:Others
476:cells.
473:PROTAC
426:SpyTag
401:V5 tag
395:Ty tag
389:TC tag
379:T7-tag
319:NE-tag
287:HA-tag
262:E.coli
242:intein
240:(Npu)
216:intein
202:(EPEA)
161:intein
106:NE-tag
102:T7-tag
94:HA-tag
86:V5-tag
2077:S-tag
1910:S2CID
1566:S2CID
1210:S2CID
1154:S2CID
987:S2CID
894:(PDF)
813:S2CID
677:S2CID
335:S-tag
221:ture
171:(See
159:) or
1962:PMID
1954:ISSN
1902:PMID
1862:PMID
1813:PMID
1770:ISBN
1735:PMID
1684:PMID
1625:PMID
1607:ISSN
1558:PMID
1516:PMID
1457:PMID
1398:PMID
1363:PMID
1304:PMID
1269:PMID
1202:PMID
1194:ISSN
1146:PMID
1103:PMID
1046:PMID
1028:ISSN
979:PMID
971:ISSN
914:PMID
871:PMID
805:PMID
767:PMID
715:PMID
669:PMID
661:ISSN
565:-tag
480:FAST
459:BirA
455:BCCP
267:mAbs
259:and
254:e.g.
116:and
104:and
41:and
1944:doi
1894:doi
1852:PMC
1844:doi
1803:doi
1799:171
1762:doi
1725:PMC
1715:doi
1674:PMC
1664:doi
1615:PMC
1597:doi
1550:doi
1546:140
1506:PMC
1496:doi
1484:113
1447:PMC
1437:doi
1425:109
1390:doi
1386:132
1353:doi
1349:282
1296:doi
1259:PMC
1249:doi
1186:doi
1138:doi
1126:443
1095:doi
1036:PMC
1018:doi
963:doi
906:doi
902:402
861:PMC
853:doi
797:doi
757:PMC
749:doi
745:426
707:doi
703:255
653:doi
486:CL7
313:myc
257:CHO
223:Tag
219:Cap
155:or
2170::
1960:.
1952:.
1940:13
1938:.
1934:.
1922:^
1908:.
1900:.
1890:14
1888:.
1884:.
1860:.
1850:.
1838:.
1834:.
1811:.
1797:.
1793:.
1768:.
1756:.
1733:.
1723:.
1711:64
1709:.
1705:.
1682:.
1672:.
1662:.
1652:11
1650:.
1646:.
1623:.
1613:.
1605:.
1593:29
1591:.
1587:.
1564:.
1556:.
1544:.
1540:.
1528:^
1514:.
1504:.
1494:.
1482:.
1478:.
1455:.
1445:.
1435:.
1423:.
1419:.
1396:.
1384:.
1361:.
1347:.
1343:.
1324:.
1302:.
1292:23
1290:.
1267:.
1257:.
1247:.
1235:.
1231:.
1208:.
1200:.
1192:.
1182:22
1180:.
1176:.
1152:.
1144:.
1136:.
1124:.
1101:.
1091:49
1089:.
1070:.
1044:.
1034:.
1026:.
1012:.
1008:.
985:.
977:.
969:.
959:91
957:.
953:.
934:.
912:.
900:.
896:.
869:.
859:.
851:.
841:10
839:.
835:.
811:.
803:.
791:.
779:^
765:.
755:.
743:.
739:.
727:^
713:.
701:.
689:^
675:.
667:.
659:.
649:45
647:.
643:.
569:Fc
151:,
147:,
112:,
100:,
96:,
92:,
88:,
1998:e
1991:t
1984:v
1968:.
1946::
1916:.
1896::
1868:.
1846::
1840:1
1819:.
1805::
1778:.
1764::
1741:.
1717::
1690:.
1666::
1658::
1631:.
1599::
1572:.
1552::
1522:.
1498::
1490::
1463:.
1439::
1431::
1404:.
1392::
1369:.
1355::
1328:.
1310:.
1298::
1275:.
1251::
1243::
1237:8
1216:.
1188::
1160:.
1140::
1132::
1109:.
1097::
1074:.
1066:i
1064:"
1052:.
1020::
1014:9
993:.
965::
938:.
920:.
908::
877:.
855::
847::
819:.
799::
793:3
773:.
751::
721:.
709::
683:.
655::
331:.
250:i
232:i
227:i
212:i
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