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Abnormal sulfatase activity is strongly connected to various diseases such as hormone\u2010dependent cancers, infectious diseases like tuberculosis, lysosomal storage disorders, and bacterial virulence, making these enzymes emerge as crucial biomarkers and therapeutic targets. This review highlights the advances in small\u2010molecule probes for selectively detecting sulfatase activity through various imaging modalities, such as fluorescence, photoacoustic, in\u2010gel fluorogenic assays, and bioluminescence imaging. Additionally, the enzyme\u2010activatable probes that exploit mechanisms via self\u2010immolative linkers, intramolecular charge transfer (ICT), photoinduced electron transfer (PET), ratiometric sensing, followed by aggregation\u2010induced emission (AIE), to achieve high specificity and sensitivity. Along similar lines, we explored substrate\u2010based and affinity\u2010based designs, covering turn\u2010on, ratiometric, and dual\u2010modal near\u2010infrared fluorescence, chemiluminescence, and photoacoustic (NIRF\/PA) probes that enable real\u2010time, noninvasive, and deep\u2010tissue imaging. A special focus is given to activity\u2010based sensing of steroid sulfatases (STS) in hormone\u2010related cancers and on profiling bacterial sulfatases for rapid mycobacterial strain differentiation. Furthermore, emerging strategies using nanoprobes and AIEgens demonstrate potential for image\u2010guided surgery, inhalable diagnostics, and high\u2010throughput screening of enzyme inhibitors. Together, these innovations establish a strong framework for sulfatase activity profiling and offer powerful capabilities for disease diagnostics, inhibitor screening, and therapeutic monitoring by enabling spatiotemporal visualization of sulfatase activity both in\u2009vitro and in\u2009vivo. This review may inspire the development of novel activatable sensors suited for practical biomedical applications by consolidating recent advances in sulfatase\u2010targeted probe design and imaging strategies.<\/jats:p>","DOI":"10.1002\/cbic.202500980","type":"journal-article","created":{"date-parts":[[2026,3,23]],"date-time":"2026-03-23T12:35:16Z","timestamp":1774269316000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Molecular Probes for Sulfatase Detection and Bio\u2010Imaging"],"prefix":"10.1002","volume":"27","author":[{"given":"Subba Rao","family":"Cheekatla","sequence":"first","affiliation":[{"name":"School of Transdisciplinary Innovations &amp; Department of Chemistry Seoul National University  Seoul Republic of Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Seong Cheol","family":"Hong","sequence":"additional","affiliation":[{"name":"Thermo Fisher Scientific  Seoul Republic of Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Muresan Anca","family":"Raluca","sequence":"additional","affiliation":[{"name":"School of Transdisciplinary Innovations &amp; Department of Chemistry Seoul National University  Seoul Republic of Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3641-1728","authenticated-orcid":false,"given":"Jun\u2010Seok","family":"Lee","sequence":"additional","affiliation":[{"name":"School of Transdisciplinary Innovations &amp; Department of Chemistry Seoul National University  Seoul Republic of Korea"},{"name":"National Research Laboratory for Convergence Degradation Biology Korea University  Seoul Republic of Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2026,3,23]]},"reference":[{"key":"e_1_2_12_2_1","doi-asserted-by":"publisher","DOI":"10.1530\/JME-18-0086"},{"key":"e_1_2_12_3_1","doi-asserted-by":"publisher","DOI":"10.1146\/annurev-bioeng-071516-044610"},{"key":"e_1_2_12_4_1","doi-asserted-by":"publisher","DOI":"10.1210\/er.2001-0040"},{"key":"e_1_2_12_5_1","doi-asserted-by":"publisher","DOI":"10.1002\/anie.200300632"},{"key":"e_1_2_12_6_1","doi-asserted-by":"publisher","DOI":"10.1093\/hmg\/ddi351"},{"key":"e_1_2_12_7_1","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/gkac977"},{"key":"e_1_2_12_8_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.biotechadv.2023.108207"},{"key":"e_1_2_12_9_1","doi-asserted-by":"publisher","DOI":"10.1007\/s00018-007-7175-y"},{"key":"e_1_2_12_10_1","doi-asserted-by":"publisher","DOI":"10.1016\/0092-8674(95)90314-3"},{"key":"e_1_2_12_11_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.steroids.2023.109335"},{"key":"e_1_2_12_12_1","doi-asserted-by":"publisher","DOI":"10.1042\/EBC20230096"},{"key":"e_1_2_12_13_1","doi-asserted-by":"publisher","DOI":"10.1210\/er.2004-0003"},{"key":"e_1_2_12_14_1","doi-asserted-by":"publisher","DOI":"10.1021\/acs.jmedchem.5b00386"},{"key":"e_1_2_12_15_1","doi-asserted-by":"publisher","DOI":"10.1039\/D4MD00795F"},{"key":"e_1_2_12_16_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2414331122"},{"key":"e_1_2_12_17_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.ejmech.2016.02.054"},{"key":"e_1_2_12_18_1","doi-asserted-by":"publisher","DOI":"10.1080\/14756366.2025.2483818"},{"key":"e_1_2_12_19_1","doi-asserted-by":"publisher","DOI":"10.1002\/med.20008"},{"key":"e_1_2_12_20_1","volume-title":"In Chemistry and Biological Activity of Steroids (Eds.:","author":"Shavva A. 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