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prommp16  (R&D Systems)


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    R&D Systems prommp16
    Identification of the KLK14 hydrolysis sites within the CleavEx proMMP protein. CleavEx proMMP fusion proteins were separated using SDS-PAGE and electrotransferred for N-terminal sequencing. Identified sequences are represented in the bold font and the underscore denotes where the location of the expected activation cleavage P1-P1′ in the proMMP-derived sequence.
    Prommp16, supplied by R&D Systems, used in various techniques. Bioz Stars score: 90/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/prommp16/Recombinant+Human+MMP-16%2FMT3-MMP+Protein%2C+CF/pmc07352328-290-33-37
    Average 90 stars, based on 4 article reviews
    prommp16 - by Bioz Stars, 2026-10
    90/100 stars

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    1) Product Images from "Kallikrein-Related Peptidase 14 Activates Zymogens of Membrane Type Matrix Metalloproteinases (MT-MMPs)—A CleavEx Based Analysis"

    Article Title: Kallikrein-Related Peptidase 14 Activates Zymogens of Membrane Type Matrix Metalloproteinases (MT-MMPs)—A CleavEx Based Analysis

    Journal: International Journal of Molecular Sciences

    doi: 10.3390/ijms21124383

    Identification of the KLK14 hydrolysis sites within the CleavEx proMMP protein. CleavEx proMMP fusion proteins were separated using SDS-PAGE and electrotransferred for N-terminal sequencing. Identified sequences are represented in the bold font and the underscore denotes where the location of the expected activation cleavage P1-P1′ in the proMMP-derived sequence.
    Figure Legend Snippet: Identification of the KLK14 hydrolysis sites within the CleavEx proMMP protein. CleavEx proMMP fusion proteins were separated using SDS-PAGE and electrotransferred for N-terminal sequencing. Identified sequences are represented in the bold font and the underscore denotes where the location of the expected activation cleavage P1-P1′ in the proMMP-derived sequence.

    Techniques Used: Sequencing, Activation Assay

    N-terminal identification of KLK14-mediated processing of recombinant proMMPs. The KLK14 hydrolysis product sequences were analyzed by N-terminal sequencing using Edman degradation. The bold font denotes the amino acid sequences identified. The underscored residues represent changes to the native protein sequence, as reported by the manufacturer (R&D Systems, Abingdon, United Kingdom). KLK14 recognized the sequence 3-aa upstream of the native MMP17 activation site, likely because the native site was modified by the manufacturer. All residues are numbered according to the Uniprot reported sequence of the full-length proteins. Bands are labeled according to the notation explained at <xref ref-type= Figure 2 ." title="N-terminal identification of KLK14-mediated processing of recombinant proMMPs. The KLK14 hydrolysis product sequences ... " property="contentUrl" width="100%" height="100%"/>
    Figure Legend Snippet: N-terminal identification of KLK14-mediated processing of recombinant proMMPs. The KLK14 hydrolysis product sequences were analyzed by N-terminal sequencing using Edman degradation. The bold font denotes the amino acid sequences identified. The underscored residues represent changes to the native protein sequence, as reported by the manufacturer (R&D Systems, Abingdon, United Kingdom). KLK14 recognized the sequence 3-aa upstream of the native MMP17 activation site, likely because the native site was modified by the manufacturer. All residues are numbered according to the Uniprot reported sequence of the full-length proteins. Bands are labeled according to the notation explained at Figure 2 .

    Techniques Used: Recombinant, Sequencing, Activation Assay, Modification, Labeling

    Gelatin zymography of proMMPs by KLK14-mediated processing. Activation of proMMPs by KLK14 results in a fully functional mature enzyme. Each proMMP was incubated with the indicated concentrations of KLK14 for 1 h at 37 °C. The reaction was stopped by the addition of KLK14-specific inhibitors, and the reaction mixture was analyzed by SDS-PAGE, followed by a zymogram with gelatin as a substrate. The proMMP2 ( A ) negative control was not activated. ProMMP14 ( B ), proMMP15 ( C ), and proMMP16 ( D ) were activated, whereas proMMP17 ( E ) did not show hydrolysis of gelatin; yet a shift corresponding to the loss of the profragment was observed (note that an amino acid substitution was introduced in proMMP17 by the manufacturer (R&D Systems, Abingdon, United Kingdom)). KLK = kallikrein-related peptidase; MMP = matrix metalloproteinase.
    Figure Legend Snippet: Gelatin zymography of proMMPs by KLK14-mediated processing. Activation of proMMPs by KLK14 results in a fully functional mature enzyme. Each proMMP was incubated with the indicated concentrations of KLK14 for 1 h at 37 °C. The reaction was stopped by the addition of KLK14-specific inhibitors, and the reaction mixture was analyzed by SDS-PAGE, followed by a zymogram with gelatin as a substrate. The proMMP2 ( A ) negative control was not activated. ProMMP14 ( B ), proMMP15 ( C ), and proMMP16 ( D ) were activated, whereas proMMP17 ( E ) did not show hydrolysis of gelatin; yet a shift corresponding to the loss of the profragment was observed (note that an amino acid substitution was introduced in proMMP17 by the manufacturer (R&D Systems, Abingdon, United Kingdom)). KLK = kallikrein-related peptidase; MMP = matrix metalloproteinase.

    Techniques Used: Zymography, Activation Assay, Functional Assay, Incubation, SDS Page, Negative Control

    Primers used for generating the proMMP CleavEx fusion proteins using mutagenesis.
    Figure Legend Snippet: Primers used for generating the proMMP CleavEx fusion proteins using mutagenesis.

    Techniques Used: Mutagenesis, Sequencing

    Related Articles

    Incubation:

    Article Title: Kallikrein-related peptidase 14 activates zymogens of membrane type matrix metalloproteinases (MT-MMPs) - a CleavEx library-based analysis
    Article Snippet: Data was recorded using proprietary software (Shimadzu Biotech) and the sequence was determined by visual inspection of the UV 269 nm chromatograms. .. A total of 0.5 μg native proMMP2 (catalog no. 902-MP-010, R&D systems), 0.5 μg proMMP14 (catalog no. 918-MP-010, R&D systems), 1 μg proMMP15 (catalog no. 916-MP-010, R&D systems), 0.5 μg ProMMP16 (catalog no. 1785-MP-010, R&D systems) and 1 μg ProMMP17 (catalog no. 7796-MP-010, R&D systems) were separately incubated in 10 μl with a range of KLK14 concentrations (25-250 nM, with molar ratios from around 1:65 to 1:10 KLK14:MMP) in the presence of 5 μM batimastat (Sigma) for 1 hour at 37°C in PBS. .. As a positive control, a total of 1 μg native proMMP2 and 0.5 μg proMMP14 were separately incubated in 10 μl with a range of furin (catalog no. 1503-SE-010, R&D systems) concentrations (0 – 250 nM, molar ratios from around 1:65 to 1:6).

    Article Title: Kallikrein-Related Peptidase 14 Activates Zymogens of Membrane Type Matrix Metalloproteinases (MT-MMPs)—A CleavEx Based Analysis
    Article Snippet: Data was recorded using proprietary software (Shimadzu Biotech), and the sequence was determined by visual inspection of the UV 269 nm chromatograms. .. A total of 0.5 μg native proMMP2 (catalog no. 902-MP-010, R&D Systems, Abingdon, United Kingdom), 0.5 μg proMMP14 (catalog no. 918-MP-010, R&D Systems), 1 μg proMMP15 (catalog no. 916-MP-010, R&D Systems), 0.5 μg proMMP16 (catalog no. 1785-MP-010, R&D Systems), and 1 μg proMMP17 (catalog no. 7796-MP-010, R&D Systems) were separately incubated in 10 μL with a range of KLK14 concentrations (25–250 nM, with molar ratios from around 1:65 to 1:10 KLK14:MMP) in the presence of 5 μM batimastat (Sigma-Aldrich, St. Louis, MO, USA) for 1 h at 37 °C in PBS. .. As a positive control, a total of 1 μg native proMMP2 and 0.5 μg proMMP14 were separately incubated in 10 μL with a range of furin (catalog no. 1503-SE-010, R&D Systems) concentrations (0–250 nM, molar ratios from around 1:65 to 1:6).



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    prommp16  (R&D Systems)
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    R&D Systems prommp16
    Identification of the KLK14 hydrolysis sites within the CleavEx proMMP protein. CleavEx proMMP fusion proteins were separated using SDS-PAGE and electrotransferred for N-terminal sequencing. Identified sequences are represented in the bold font and the underscore denotes where the location of the expected activation cleavage P1-P1′ in the proMMP-derived sequence.
    Prommp16, supplied by R&D Systems, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/prommp16/Recombinant+Human+MMP-16%2FMT3-MMP+Protein%2C+CF/pmc07352328-290-33-37
    Average 90 stars, based on 1 article reviews
    prommp16 - by Bioz Stars, 2026-10
    90/100 stars
    		  Buy from Supplier

    Image Search Results


    Identification of the KLK14 hydrolysis sites within the CleavEx proMMP protein. CleavEx proMMP fusion proteins were separated using SDS-PAGE and electrotransferred for N-terminal sequencing. Identified sequences are represented in the bold font and the underscore denotes where the location of the expected activation cleavage P1-P1′ in the proMMP-derived sequence.

    Journal: International Journal of Molecular Sciences

    Article Title: Kallikrein-Related Peptidase 14 Activates Zymogens of Membrane Type Matrix Metalloproteinases (MT-MMPs)—A CleavEx Based Analysis

    doi: 10.3390/ijms21124383

    Figure Lengend Snippet: Identification of the KLK14 hydrolysis sites within the CleavEx proMMP protein. CleavEx proMMP fusion proteins were separated using SDS-PAGE and electrotransferred for N-terminal sequencing. Identified sequences are represented in the bold font and the underscore denotes where the location of the expected activation cleavage P1-P1′ in the proMMP-derived sequence.

    Article Snippet: A total of 0.5 μg native proMMP2 (catalog no. 902-MP-010, R&D Systems, Abingdon, United Kingdom), 0.5 μg proMMP14 (catalog no. 918-MP-010, R&D Systems), 1 μg proMMP15 (catalog no. 916-MP-010, R&D Systems), 0.5 μg proMMP16 (catalog no. 1785-MP-010, R&D Systems), and 1 μg proMMP17 (catalog no. 7796-MP-010, R&D Systems) were separately incubated in 10 μL with a range of KLK14 concentrations (25–250 nM, with molar ratios from around 1:65 to 1:10 KLK14:MMP) in the presence of 5 μM batimastat (Sigma-Aldrich, St. Louis, MO, USA) for 1 h at 37 °C in PBS.

    Techniques: Sequencing, Activation Assay

    N-terminal identification of KLK14-mediated processing of recombinant proMMPs. The KLK14 hydrolysis product sequences were analyzed by N-terminal sequencing using Edman degradation. The bold font denotes the amino acid sequences identified. The underscored residues represent changes to the native protein sequence, as reported by the manufacturer (R&D Systems, Abingdon, United Kingdom). KLK14 recognized the sequence 3-aa upstream of the native MMP17 activation site, likely because the native site was modified by the manufacturer. All residues are numbered according to the Uniprot reported sequence of the full-length proteins. Bands are labeled according to the notation explained at <xref ref-type= Figure 2 ." width="100%" height="100%">

    Journal: International Journal of Molecular Sciences

    Article Title: Kallikrein-Related Peptidase 14 Activates Zymogens of Membrane Type Matrix Metalloproteinases (MT-MMPs)—A CleavEx Based Analysis

    doi: 10.3390/ijms21124383

    Figure Lengend Snippet: N-terminal identification of KLK14-mediated processing of recombinant proMMPs. The KLK14 hydrolysis product sequences were analyzed by N-terminal sequencing using Edman degradation. The bold font denotes the amino acid sequences identified. The underscored residues represent changes to the native protein sequence, as reported by the manufacturer (R&D Systems, Abingdon, United Kingdom). KLK14 recognized the sequence 3-aa upstream of the native MMP17 activation site, likely because the native site was modified by the manufacturer. All residues are numbered according to the Uniprot reported sequence of the full-length proteins. Bands are labeled according to the notation explained at Figure 2 .

    Article Snippet: A total of 0.5 μg native proMMP2 (catalog no. 902-MP-010, R&D Systems, Abingdon, United Kingdom), 0.5 μg proMMP14 (catalog no. 918-MP-010, R&D Systems), 1 μg proMMP15 (catalog no. 916-MP-010, R&D Systems), 0.5 μg proMMP16 (catalog no. 1785-MP-010, R&D Systems), and 1 μg proMMP17 (catalog no. 7796-MP-010, R&D Systems) were separately incubated in 10 μL with a range of KLK14 concentrations (25–250 nM, with molar ratios from around 1:65 to 1:10 KLK14:MMP) in the presence of 5 μM batimastat (Sigma-Aldrich, St. Louis, MO, USA) for 1 h at 37 °C in PBS.

    Techniques: Recombinant, Sequencing, Activation Assay, Modification, Labeling

    Gelatin zymography of proMMPs by KLK14-mediated processing. Activation of proMMPs by KLK14 results in a fully functional mature enzyme. Each proMMP was incubated with the indicated concentrations of KLK14 for 1 h at 37 °C. The reaction was stopped by the addition of KLK14-specific inhibitors, and the reaction mixture was analyzed by SDS-PAGE, followed by a zymogram with gelatin as a substrate. The proMMP2 ( A ) negative control was not activated. ProMMP14 ( B ), proMMP15 ( C ), and proMMP16 ( D ) were activated, whereas proMMP17 ( E ) did not show hydrolysis of gelatin; yet a shift corresponding to the loss of the profragment was observed (note that an amino acid substitution was introduced in proMMP17 by the manufacturer (R&D Systems, Abingdon, United Kingdom)). KLK = kallikrein-related peptidase; MMP = matrix metalloproteinase.

    Journal: International Journal of Molecular Sciences

    Article Title: Kallikrein-Related Peptidase 14 Activates Zymogens of Membrane Type Matrix Metalloproteinases (MT-MMPs)—A CleavEx Based Analysis

    doi: 10.3390/ijms21124383

    Figure Lengend Snippet: Gelatin zymography of proMMPs by KLK14-mediated processing. Activation of proMMPs by KLK14 results in a fully functional mature enzyme. Each proMMP was incubated with the indicated concentrations of KLK14 for 1 h at 37 °C. The reaction was stopped by the addition of KLK14-specific inhibitors, and the reaction mixture was analyzed by SDS-PAGE, followed by a zymogram with gelatin as a substrate. The proMMP2 ( A ) negative control was not activated. ProMMP14 ( B ), proMMP15 ( C ), and proMMP16 ( D ) were activated, whereas proMMP17 ( E ) did not show hydrolysis of gelatin; yet a shift corresponding to the loss of the profragment was observed (note that an amino acid substitution was introduced in proMMP17 by the manufacturer (R&D Systems, Abingdon, United Kingdom)). KLK = kallikrein-related peptidase; MMP = matrix metalloproteinase.

    Article Snippet: A total of 0.5 μg native proMMP2 (catalog no. 902-MP-010, R&D Systems, Abingdon, United Kingdom), 0.5 μg proMMP14 (catalog no. 918-MP-010, R&D Systems), 1 μg proMMP15 (catalog no. 916-MP-010, R&D Systems), 0.5 μg proMMP16 (catalog no. 1785-MP-010, R&D Systems), and 1 μg proMMP17 (catalog no. 7796-MP-010, R&D Systems) were separately incubated in 10 μL with a range of KLK14 concentrations (25–250 nM, with molar ratios from around 1:65 to 1:10 KLK14:MMP) in the presence of 5 μM batimastat (Sigma-Aldrich, St. Louis, MO, USA) for 1 h at 37 °C in PBS.

    Techniques: Zymography, Activation Assay, Functional Assay, Incubation, SDS Page, Negative Control

    Primers used for generating the proMMP CleavEx fusion proteins using mutagenesis.

    Journal: International Journal of Molecular Sciences

    Article Title: Kallikrein-Related Peptidase 14 Activates Zymogens of Membrane Type Matrix Metalloproteinases (MT-MMPs)—A CleavEx Based Analysis

    doi: 10.3390/ijms21124383

    Figure Lengend Snippet: Primers used for generating the proMMP CleavEx fusion proteins using mutagenesis.

    Article Snippet: A total of 0.5 μg native proMMP2 (catalog no. 902-MP-010, R&D Systems, Abingdon, United Kingdom), 0.5 μg proMMP14 (catalog no. 918-MP-010, R&D Systems), 1 μg proMMP15 (catalog no. 916-MP-010, R&D Systems), 0.5 μg proMMP16 (catalog no. 1785-MP-010, R&D Systems), and 1 μg proMMP17 (catalog no. 7796-MP-010, R&D Systems) were separately incubated in 10 μL with a range of KLK14 concentrations (25–250 nM, with molar ratios from around 1:65 to 1:10 KLK14:MMP) in the presence of 5 μM batimastat (Sigma-Aldrich, St. Louis, MO, USA) for 1 h at 37 °C in PBS.

    Techniques: Mutagenesis, Sequencing