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rhmmp13 pro form  (R&D Systems)


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    Structured Review

    R&D Systems rhmmp13 pro form
    A-D. Molecular docking study showing the interaction of proMMP13 (A) and mature MMP13 (C) with DCLK1-S. B. Ser 73 and Ser 114 highlighted in green in proMMP13, represent the phosphorylation sites for DCLK1-S. D. Arg207 and Gln211 are donor sites from MMP13 in mature protein close to Thr197 (circled). E. Both <t>rhMMP13</t> and rhDCLK1 were incubated in kinase buffer in presence or absence of ATP at 30 °C for 1 hr. rhMMP13 didn’t show any autophosphorylation in the same condition. Phosphorylation was detected by pan phospho-Serine/Threonine antibody. F. rhMMP13 was incubated with rhDCLK1 in presence of ATP at 30 °C for 1 hr. Phosphorylated rhMMP13 was detected with immunoblotting using pan phospho-Serine/Threonine antibody. Representative immunoblots showing the levels of phosphorylation of rhMMP13. Right panel represents the Coomassie staining (n = 3 independent experiments). G, H. Protein band intensity ratios, pMMP13/pDCLK1 and pMMP13/Total MMP13, showing rhMMP13 phosphorylation by rhDCLK1.
    Rhmmp13 Pro Form, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 30 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/human+recombinant+pro+mmp+13/pmc12370143-267-22-26?v=R%26D+Systems
    Average 94 stars, based on 30 article reviews
    rhmmp13 pro form - by Bioz Stars, 2026-07
    94/100 stars

    Images

    1) Product Images from "DCLK1 isoform (DCLK1-S) as a critical player in promoting inflammation, tissue remodeling, and EMT in mouse models of colitis"

    Article Title: DCLK1 isoform (DCLK1-S) as a critical player in promoting inflammation, tissue remodeling, and EMT in mouse models of colitis

    Journal: PLOS Pathogens

    doi: 10.1371/journal.ppat.1013360

    A-D. Molecular docking study showing the interaction of proMMP13 (A) and mature MMP13 (C) with DCLK1-S. B. Ser 73 and Ser 114 highlighted in green in proMMP13, represent the phosphorylation sites for DCLK1-S. D. Arg207 and Gln211 are donor sites from MMP13 in mature protein close to Thr197 (circled). E. Both rhMMP13 and rhDCLK1 were incubated in kinase buffer in presence or absence of ATP at 30 °C for 1 hr. rhMMP13 didn’t show any autophosphorylation in the same condition. Phosphorylation was detected by pan phospho-Serine/Threonine antibody. F. rhMMP13 was incubated with rhDCLK1 in presence of ATP at 30 °C for 1 hr. Phosphorylated rhMMP13 was detected with immunoblotting using pan phospho-Serine/Threonine antibody. Representative immunoblots showing the levels of phosphorylation of rhMMP13. Right panel represents the Coomassie staining (n = 3 independent experiments). G, H. Protein band intensity ratios, pMMP13/pDCLK1 and pMMP13/Total MMP13, showing rhMMP13 phosphorylation by rhDCLK1.
    Figure Legend Snippet: A-D. Molecular docking study showing the interaction of proMMP13 (A) and mature MMP13 (C) with DCLK1-S. B. Ser 73 and Ser 114 highlighted in green in proMMP13, represent the phosphorylation sites for DCLK1-S. D. Arg207 and Gln211 are donor sites from MMP13 in mature protein close to Thr197 (circled). E. Both rhMMP13 and rhDCLK1 were incubated in kinase buffer in presence or absence of ATP at 30 °C for 1 hr. rhMMP13 didn’t show any autophosphorylation in the same condition. Phosphorylation was detected by pan phospho-Serine/Threonine antibody. F. rhMMP13 was incubated with rhDCLK1 in presence of ATP at 30 °C for 1 hr. Phosphorylated rhMMP13 was detected with immunoblotting using pan phospho-Serine/Threonine antibody. Representative immunoblots showing the levels of phosphorylation of rhMMP13. Right panel represents the Coomassie staining (n = 3 independent experiments). G, H. Protein band intensity ratios, pMMP13/pDCLK1 and pMMP13/Total MMP13, showing rhMMP13 phosphorylation by rhDCLK1.

    Techniques Used: Phospho-proteomics, Incubation, Western Blot, Staining



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    A-D. Molecular docking study showing the interaction of proMMP13 (A) and mature MMP13 (C) with DCLK1-S. B. Ser 73 and Ser 114 highlighted in green in proMMP13, represent the phosphorylation sites for DCLK1-S. D. Arg207 and Gln211 are donor sites from MMP13 in mature protein close to Thr197 (circled). E. Both <t>rhMMP13</t> and rhDCLK1 were incubated in kinase buffer in presence or absence of ATP at 30 °C for 1 hr. rhMMP13 didn’t show any autophosphorylation in the same condition. Phosphorylation was detected by pan phospho-Serine/Threonine antibody. F. rhMMP13 was incubated with rhDCLK1 in presence of ATP at 30 °C for 1 hr. Phosphorylated rhMMP13 was detected with immunoblotting using pan phospho-Serine/Threonine antibody. Representative immunoblots showing the levels of phosphorylation of rhMMP13. Right panel represents the Coomassie staining (n = 3 independent experiments). G, H. Protein band intensity ratios, pMMP13/pDCLK1 and pMMP13/Total MMP13, showing rhMMP13 phosphorylation by rhDCLK1.
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    A-D. Molecular docking study showing the interaction of proMMP13 (A) and mature MMP13 (C) with DCLK1-S. B. Ser 73 and Ser 114 highlighted in green in proMMP13, represent the phosphorylation sites for DCLK1-S. D. Arg207 and Gln211 are donor sites from MMP13 in mature protein close to Thr197 (circled). E. Both <t>rhMMP13</t> and rhDCLK1 were incubated in kinase buffer in presence or absence of ATP at 30 °C for 1 hr. rhMMP13 didn’t show any autophosphorylation in the same condition. Phosphorylation was detected by pan phospho-Serine/Threonine antibody. F. rhMMP13 was incubated with rhDCLK1 in presence of ATP at 30 °C for 1 hr. Phosphorylated rhMMP13 was detected with immunoblotting using pan phospho-Serine/Threonine antibody. Representative immunoblots showing the levels of phosphorylation of rhMMP13. Right panel represents the Coomassie staining (n = 3 independent experiments). G, H. Protein band intensity ratios, pMMP13/pDCLK1 and pMMP13/Total MMP13, showing rhMMP13 phosphorylation by rhDCLK1.
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    A-D. Molecular docking study showing the interaction of proMMP13 (A) and mature MMP13 (C) with DCLK1-S. B. Ser 73 and Ser 114 highlighted in green in proMMP13, represent the phosphorylation sites for DCLK1-S. D. Arg207 and Gln211 are donor sites from MMP13 in mature protein close to Thr197 (circled). E. Both <t>rhMMP13</t> and rhDCLK1 were incubated in kinase buffer in presence or absence of ATP at 30 °C for 1 hr. rhMMP13 didn’t show any autophosphorylation in the same condition. Phosphorylation was detected by pan phospho-Serine/Threonine antibody. F. rhMMP13 was incubated with rhDCLK1 in presence of ATP at 30 °C for 1 hr. Phosphorylated rhMMP13 was detected with immunoblotting using pan phospho-Serine/Threonine antibody. Representative immunoblots showing the levels of phosphorylation of rhMMP13. Right panel represents the Coomassie staining (n = 3 independent experiments). G, H. Protein band intensity ratios, pMMP13/pDCLK1 and pMMP13/Total MMP13, showing rhMMP13 phosphorylation by rhDCLK1.
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    Image Search Results


    A-D. Molecular docking study showing the interaction of proMMP13 (A) and mature MMP13 (C) with DCLK1-S. B. Ser 73 and Ser 114 highlighted in green in proMMP13, represent the phosphorylation sites for DCLK1-S. D. Arg207 and Gln211 are donor sites from MMP13 in mature protein close to Thr197 (circled). E. Both rhMMP13 and rhDCLK1 were incubated in kinase buffer in presence or absence of ATP at 30 °C for 1 hr. rhMMP13 didn’t show any autophosphorylation in the same condition. Phosphorylation was detected by pan phospho-Serine/Threonine antibody. F. rhMMP13 was incubated with rhDCLK1 in presence of ATP at 30 °C for 1 hr. Phosphorylated rhMMP13 was detected with immunoblotting using pan phospho-Serine/Threonine antibody. Representative immunoblots showing the levels of phosphorylation of rhMMP13. Right panel represents the Coomassie staining (n = 3 independent experiments). G, H. Protein band intensity ratios, pMMP13/pDCLK1 and pMMP13/Total MMP13, showing rhMMP13 phosphorylation by rhDCLK1.

    Journal: PLOS Pathogens

    Article Title: DCLK1 isoform (DCLK1-S) as a critical player in promoting inflammation, tissue remodeling, and EMT in mouse models of colitis

    doi: 10.1371/journal.ppat.1013360

    Figure Lengend Snippet: A-D. Molecular docking study showing the interaction of proMMP13 (A) and mature MMP13 (C) with DCLK1-S. B. Ser 73 and Ser 114 highlighted in green in proMMP13, represent the phosphorylation sites for DCLK1-S. D. Arg207 and Gln211 are donor sites from MMP13 in mature protein close to Thr197 (circled). E. Both rhMMP13 and rhDCLK1 were incubated in kinase buffer in presence or absence of ATP at 30 °C for 1 hr. rhMMP13 didn’t show any autophosphorylation in the same condition. Phosphorylation was detected by pan phospho-Serine/Threonine antibody. F. rhMMP13 was incubated with rhDCLK1 in presence of ATP at 30 °C for 1 hr. Phosphorylated rhMMP13 was detected with immunoblotting using pan phospho-Serine/Threonine antibody. Representative immunoblots showing the levels of phosphorylation of rhMMP13. Right panel represents the Coomassie staining (n = 3 independent experiments). G, H. Protein band intensity ratios, pMMP13/pDCLK1 and pMMP13/Total MMP13, showing rhMMP13 phosphorylation by rhDCLK1.

    Article Snippet: To examine DCLK1 binding/kinase activity, we used recombinant human DCLK1 protein (full length, rhDCLK1 (D14-10H, Sino Biologicals) and recombinant human MMP13 protein, rhMMP13 Pro form (511-MM-010, R&D Systems).

    Techniques: Phospho-proteomics, Incubation, Western Blot, Staining