MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it Leukocyte cell-derived chemotaxin 2 is a zinc-binding protein. Leukocyte cell-derived chemotaxin 2 is a zinc-binding protein. FEBS Lett. (0014-5793) 2013 Okumura A., Suzuki T., Miyatake H., Okabe T., Hashimoto Y., Miyakawa T., Zheng H., Unoki-Kubota H., Ohno H., Dohmae N., Kaburagi Y., Miyazaki Y., Tanokura M., Yamagoe S. in vitro In vitro comigration in gel comigration in gel electrophoresis comigration in gel western blot western blot Immuno blot Immuno blot Okumura A., Suzuki T., Miyatake H., Okabe T., Hashimoto Y., Miyakawa T., Zheng H., Unoki-Kubota H., Ohno H., Dohmae N., Kaburagi Y., Miyazaki Y., Tanokura M., Yamagoe S. FEBS Lett. (0014-5793) 2013 Leukocyte cell-derived chemotaxin 2 is a zinc-binding protein. Leukocyte cell-derived chemotaxin 2 is a zinc-binding protein. FEBS Lett. (0014-5793) 2013 Okumura A., Suzuki T., Miyatake H., Okabe T., Hashimoto Y., Miyakawa T., Zheng H., Unoki-Kubota H., Ohno H., Dohmae N., Kaburagi Y., Miyazaki Y., Tanokura M., Yamagoe S. in vitro In vitro crosslink cross-linking study crosslink western blot western blot Immuno blot Immuno blot Okumura A., Suzuki T., Miyatake H., Okabe T., Hashimoto Y., Miyakawa T., Zheng H., Unoki-Kubota H., Ohno H., Dohmae N., Kaburagi Y., Miyazaki Y., Tanokura M., Yamagoe S. FEBS Lett. (0014-5793) 2013 lect2_mouse Leukocyte cell-derived chemotaxin-2 Lect2 Chondromodulin II protein protein mouse Mus musculus Mouse MIPTTILISAALLSSALAGPWANICASKSSNEIRTCDSYGCGQYSAQRTQRHHPGVDVLCSDGSVVYAPFTGKIVGQEKPYRNKNAINDGIRLSGRGFCVKIFYIKPIKYKGSIKKGEKLGTLLPLQKIYPGIQSHVHVENCDSSDPTAYL mint 18AF444046B7AE8E lect2_human Leukocyte cell-derived chemotaxin-2 LECT2 protein protein human Homo sapiens Human MFSTKALLLAGLISTALAGPWANICAGKSSNEIRTCDRHGCGQYSAQRSQRPHQGVDILCSAGSTVYAPFTGMIVGQEKPYQNKNAINNGVRISGRGFCVKMFYIKPIKYKGPIKKGEKLGTLLPLQKVYPGIQSHVHIENCDSSDPTAYL mint 3C1DFCA1B4F8792F lect2-lect2 1 LECT2 3 western blot western blot Immuno blot Immuno blot experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified LECT2 3 western blot western blot Immuno blot Immuno blot experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction mint SDS-PAGE was then performed under non-reducing conditions, and LECT2 protein was detected by western blotting using an anti-mouse LECT2 polyclonal antibody. Fig. 3A shows that the oligomerization occurred in a temperature-dependent manner. As shown in supplemetal Fig. 1, the oligomerization occurred in a time-dependent manner. SDS-PAGE carried out under reducing conditions showed a distinct pattern of oligomerization. Strangely, ladder bands migrating at 100 250 kDa and smear bands around the expected dimer position were detected in reduced SDS-PAGE. As shown in supplemental Fig. 2, DTT treatment enhanced the oligomerization of LECT2 in a concentration-dependent manner. Furthermore, the intensity of the ladder bands migrating between 100 250 kDa increased over time in the experiments carried out at the high concentration of 200 mM DTT (supplemental Fig. 3). Moreover, the state of the dimer in reduced SDS-PAGE was different from those observed in non-reduced SDS-PAGE. On the other hand, iodoacetate is known to be an alkylating agent, which irreversibly reacts with cysteine to block disulfide bond formation. As shown in supplemental Fig. 4, iodoacetate treatment inhibited higher-order oligomerization except dimers and trimers. f3a sf1 lect2-1 1 LECT2 3 western blot western blot Immuno blot Immuno blot experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 2.0 direct interaction direct interaction mint SDS-PAGE was then performed under non-reducing conditions, and LECT2 protein was detected by western blotting using an anti-mouse LECT2 polyclonal antibody. Fig. 3A shows that the oligomerization occurred in a temperature-dependent manner. As shown in supplemetal Fig. 1, the oligomerization occurred in a time-dependent manner. SDS-PAGE carried out under reducing conditions showed a distinct pattern of oligomerization. Strangely, ladder bands migrating at 100 250 kDa and smear bands around the expected dimer position were detected in reduced SDS-PAGE. As shown in supplemental Fig. 2, DTT treatment enhanced the oligomerization of LECT2 in a concentration-dependent manner. Furthermore, the intensity of the ladder bands migrating between 100 250 kDa increased over time in the experiments carried out at the high concentration of 200 mM DTT (supplemental Fig. 3). Moreover, the state of the dimer in reduced SDS-PAGE was different from those observed in non-reduced SDS-PAGE. On the other hand, iodoacetate is known to be an alkylating agent, which irreversibly reacts with cysteine to block disulfide bond formation. As shown in supplemental Fig. 4, iodoacetate treatment inhibited higher-order oligomerization except dimers and trimers. f3a sf1 lect2-1 1 LECT2 3 western blot western blot Immuno blot Immuno blot experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 3.0 direct interaction direct interaction mint SDS-PAGE was then performed under non-reducing conditions, and LECT2 protein was detected by western blotting using an anti-mouse LECT2 polyclonal antibody. Fig. 3A shows that the oligomerization occurred in a temperature-dependent manner. As shown in supplemetal Fig. 1, the oligomerization occurred in a time-dependent manner. SDS-PAGE carried out under reducing conditions showed a distinct pattern of oligomerization. Strangely, ladder bands migrating at 100 250 kDa and smear bands around the expected dimer position were detected in reduced SDS-PAGE. As shown in supplemental Fig. 2, DTT treatment enhanced the oligomerization of LECT2 in a concentration-dependent manner. Furthermore, the intensity of the ladder bands migrating between 100 250 kDa increased over time in the experiments carried out at the high concentration of 200 mM DTT (supplemental Fig. 3). Moreover, the state of the dimer in reduced SDS-PAGE was different from those observed in non-reduced SDS-PAGE. On the other hand, iodoacetate is known to be an alkylating agent, which irreversibly reacts with cysteine to block disulfide bond formation. As shown in supplemental Fig. 4, iodoacetate treatment inhibited higher-order oligomerization except dimers and trimers. f3a sf1 lect2-1 1 LECT2 3 western blot western blot Immuno blot Immuno blot experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 4.0 direct interaction direct interaction mint SDS-PAGE was then performed under non-reducing conditions, and LECT2 protein was detected by western blotting using an anti-mouse LECT2 polyclonal antibody. Fig. 3A shows that the oligomerization occurred in a temperature-dependent manner. As shown in supplemetal Fig. 1, the oligomerization occurred in a time-dependent manner. SDS-PAGE carried out under reducing conditions showed a distinct pattern of oligomerization. Strangely, ladder bands migrating at 100 250 kDa and smear bands around the expected dimer position were detected in reduced SDS-PAGE. As shown in supplemental Fig. 2, DTT treatment enhanced the oligomerization of LECT2 in a concentration-dependent manner. Furthermore, the intensity of the ladder bands migrating between 100 250 kDa increased over time in the experiments carried out at the high concentration of 200 mM DTT (supplemental Fig. 3). Moreover, the state of the dimer in reduced SDS-PAGE was different from those observed in non-reduced SDS-PAGE. On the other hand, iodoacetate is known to be an alkylating agent, which irreversibly reacts with cysteine to block disulfide bond formation. As shown in supplemental Fig. 4, iodoacetate treatment inhibited higher-order oligomerization except dimers and trimers. f3a sf1 lect2-1 1 LECT2 4 western blot western blot Immuno blot Immuno blot experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 2.0 direct interaction direct interaction f3b mint Oligomerization of recombinant human LECT2 produced by an animal cell line has also been 2 observed, indicating that the oligomerization was not unique to mouse LECT2 (Fig. 3B). lect2-1 1 LECT2 4 western blot western blot Immuno blot Immuno blot experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 3.0 direct interaction direct interaction f3b mint Oligomerization of recombinant human LECT2 produced by an animal cell line has also been 2 observed, indicating that the oligomerization was not unique to mouse LECT2 (Fig. 3B). lect2-1 1 LECT2 4 western blot western blot Immuno blot Immuno blot experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 4.0 direct interaction direct interaction f3b mint Oligomerization of recombinant human LECT2 produced by an animal cell line has also been 2 observed, indicating that the oligomerization was not unique to mouse LECT2 (Fig. 3B). lect2-1 2 LECT2 3 western blot western blot Immuno blot Immuno blot experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 2.0 direct interaction direct interaction mint SDS-PAGE was then performed under non-reducing conditions, and LECT2 protein was detected by western blotting using an anti-mouse LECT2 polyclonal antibody. Fig. 3A shows that the oligomerization occurred in a temperature-dependent manner. As shown in supplemetal Fig. 1, the oligomerization occurred in a time-dependent manner. SDS-PAGE carried out under reducing conditions showed a distinct pattern of oligomerization. Strangely, ladder bands migrating at 100 250 kDa and smear bands around the expected dimer position were detected in reduced SDS-PAGE. As shown in supplemental Fig. 2, DTT treatment enhanced the oligomerization of LECT2 in a concentration-dependent manner. Furthermore, the intensity of the ladder bands migrating between 100 250 kDa increased over time in the experiments carried out at the high concentration of 200 mM DTT (supplemental Fig. 3). Moreover, the state of the dimer in reduced SDS-PAGE was different from those observed in non-reduced SDS-PAGE. On the other hand, iodoacetate is known to be an alkylating agent, which irreversibly reacts with cysteine to block disulfide bond formation. As shown in supplemental Fig. 4, iodoacetate treatment inhibited higher-order oligomerization except dimers and trimers. f3a sf2 sf3 sf4 lect2-1 2 LECT2 3 western blot western blot Immuno blot Immuno blot experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 3.0 direct interaction direct interaction mint SDS-PAGE was then performed under non-reducing conditions, and LECT2 protein was detected by western blotting using an anti-mouse LECT2 polyclonal antibody. Fig. 3A shows that the oligomerization occurred in a temperature-dependent manner. As shown in supplemetal Fig. 1, the oligomerization occurred in a time-dependent manner. SDS-PAGE carried out under reducing conditions showed a distinct pattern of oligomerization. Strangely, ladder bands migrating at 100 250 kDa and smear bands around the expected dimer position were detected in reduced SDS-PAGE. As shown in supplemental Fig. 2, DTT treatment enhanced the oligomerization of LECT2 in a concentration-dependent manner. Furthermore, the intensity of the ladder bands migrating between 100 250 kDa increased over time in the experiments carried out at the high concentration of 200 mM DTT (supplemental Fig. 3). Moreover, the state of the dimer in reduced SDS-PAGE was different from those observed in non-reduced SDS-PAGE. On the other hand, iodoacetate is known to be an alkylating agent, which irreversibly reacts with cysteine to block disulfide bond formation. As shown in supplemental Fig. 4, iodoacetate treatment inhibited higher-order oligomerization except dimers and trimers. f3a sf2 sf3 sf4 lect2-1 2 LECT2 3 western blot western blot Immuno blot Immuno blot experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 4.0 direct interaction direct interaction mint SDS-PAGE was then performed under non-reducing conditions, and LECT2 protein was detected by western blotting using an anti-mouse LECT2 polyclonal antibody. Fig. 3A shows that the oligomerization occurred in a temperature-dependent manner. As shown in supplemetal Fig. 1, the oligomerization occurred in a time-dependent manner. SDS-PAGE carried out under reducing conditions showed a distinct pattern of oligomerization. Strangely, ladder bands migrating at 100 250 kDa and smear bands around the expected dimer position were detected in reduced SDS-PAGE. As shown in supplemental Fig. 2, DTT treatment enhanced the oligomerization of LECT2 in a concentration-dependent manner. Furthermore, the intensity of the ladder bands migrating between 100 250 kDa increased over time in the experiments carried out at the high concentration of 200 mM DTT (supplemental Fig. 3). Moreover, the state of the dimer in reduced SDS-PAGE was different from those observed in non-reduced SDS-PAGE. On the other hand, iodoacetate is known to be an alkylating agent, which irreversibly reacts with cysteine to block disulfide bond formation. As shown in supplemental Fig. 4, iodoacetate treatment inhibited higher-order oligomerization except dimers and trimers. f3a sf2 sf3 sf4 lect2-lect2-1 2 LECT2 3 western blot western blot Immuno blot Immuno blot experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified LECT2 3 western blot western blot Immuno blot Immuno blot experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction mint SDS-PAGE was then performed under non-reducing conditions, and LECT2 protein was detected by western blotting using an anti-mouse LECT2 polyclonal antibody. Fig. 3A shows that the oligomerization occurred in a temperature-dependent manner. As shown in supplemetal Fig. 1, the oligomerization occurred in a time-dependent manner. SDS-PAGE carried out under reducing conditions showed a distinct pattern of oligomerization. Strangely, ladder bands migrating at 100 250 kDa and smear bands around the expected dimer position were detected in reduced SDS-PAGE. As shown in supplemental Fig. 2, DTT treatment enhanced the oligomerization of LECT2 in a concentration-dependent manner. Furthermore, the intensity of the ladder bands migrating between 100 250 kDa increased over time in the experiments carried out at the high concentration of 200 mM DTT (supplemental Fig. 3). Moreover, the state of the dimer in reduced SDS-PAGE was different from those observed in non-reduced SDS-PAGE. On the other hand, iodoacetate is known to be an alkylating agent, which irreversibly reacts with cysteine to block disulfide bond formation. As shown in supplemental Fig. 4, iodoacetate treatment inhibited higher-order oligomerization except dimers and trimers. f3a sf2 sf3 sf4