Review



sheep anti matriptase  (R&D Systems)


Bioz Verified Symbol R&D Systems is a verified supplier
Bioz Manufacturer Symbol R&D Systems manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
    • 92
      Buy from Supplier

    Structured Review

    R&D Systems sheep anti matriptase
    (A) Schematic structure of the biotin-RQRR-CMK peptide inhibitor. (B) The reactivity of biotin-RQRR-CMK was tested after 180 min of pre-incubation at 37°C (diamonds) or without preincubation (crosses). 0.2 µM <t>matriptase</t> SPD was incubated for 10 min at 37°C with (diamonds and crosses) or without (squares) 50 µM biotin-RQRR-CMK before addition of the chromogenic substrate to a final concentration of 300 µM. (C) The stability of 5 nM biotin-RQRR-CMK was further tested after the time points 0 (crosses), 60 (circles), 120 (stars), and 180 min (diamonds) of pre-incubation at 37°C and compared to a control not containing biotin-RQRR-CMK (squares). As described above, 0.2 nM matriptase SPD was added to each sample and incubated for 10 min at 37°C followed by addition of the chromogenic substrate to a final concentration of 300 µM. In all cases, the enzymatic activity of SPD was monitored by conversion of the chromogenic substrate (S2288). Each plot shows the change in optical density at 405 nm of the reaction mixture as a function of reaction time. The presence of active protease results in a continued release of a yellow cleavage product resulting in a linear color development in agreement with a pseudo 1 st order reaction due to the high molar excess of substrate to protease. Results shown are representative of 3 independent experiments.
    Sheep Anti Matriptase, supplied by R&D Systems, used in various techniques. Bioz Stars score: 92/100, based on 39 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/sheep anti matriptase/product/R&D Systems
    Average 92 stars, based on 39 article reviews
    sheep anti matriptase - by Bioz Stars, 2026-03
    92/100 stars

    Images

    1) Product Images from "Detection of Active Matriptase Using a Biotinylated Chloromethyl Ketone Peptide"

    Article Title: Detection of Active Matriptase Using a Biotinylated Chloromethyl Ketone Peptide

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0077146

    (A) Schematic structure of the biotin-RQRR-CMK peptide inhibitor. (B) The reactivity of biotin-RQRR-CMK was tested after 180 min of pre-incubation at 37°C (diamonds) or without preincubation (crosses). 0.2 µM matriptase SPD was incubated for 10 min at 37°C with (diamonds and crosses) or without (squares) 50 µM biotin-RQRR-CMK before addition of the chromogenic substrate to a final concentration of 300 µM. (C) The stability of 5 nM biotin-RQRR-CMK was further tested after the time points 0 (crosses), 60 (circles), 120 (stars), and 180 min (diamonds) of pre-incubation at 37°C and compared to a control not containing biotin-RQRR-CMK (squares). As described above, 0.2 nM matriptase SPD was added to each sample and incubated for 10 min at 37°C followed by addition of the chromogenic substrate to a final concentration of 300 µM. In all cases, the enzymatic activity of SPD was monitored by conversion of the chromogenic substrate (S2288). Each plot shows the change in optical density at 405 nm of the reaction mixture as a function of reaction time. The presence of active protease results in a continued release of a yellow cleavage product resulting in a linear color development in agreement with a pseudo 1 st order reaction due to the high molar excess of substrate to protease. Results shown are representative of 3 independent experiments.
    Figure Legend Snippet: (A) Schematic structure of the biotin-RQRR-CMK peptide inhibitor. (B) The reactivity of biotin-RQRR-CMK was tested after 180 min of pre-incubation at 37°C (diamonds) or without preincubation (crosses). 0.2 µM matriptase SPD was incubated for 10 min at 37°C with (diamonds and crosses) or without (squares) 50 µM biotin-RQRR-CMK before addition of the chromogenic substrate to a final concentration of 300 µM. (C) The stability of 5 nM biotin-RQRR-CMK was further tested after the time points 0 (crosses), 60 (circles), 120 (stars), and 180 min (diamonds) of pre-incubation at 37°C and compared to a control not containing biotin-RQRR-CMK (squares). As described above, 0.2 nM matriptase SPD was added to each sample and incubated for 10 min at 37°C followed by addition of the chromogenic substrate to a final concentration of 300 µM. In all cases, the enzymatic activity of SPD was monitored by conversion of the chromogenic substrate (S2288). Each plot shows the change in optical density at 405 nm of the reaction mixture as a function of reaction time. The presence of active protease results in a continued release of a yellow cleavage product resulting in a linear color development in agreement with a pseudo 1 st order reaction due to the high molar excess of substrate to protease. Results shown are representative of 3 independent experiments.

    Techniques Used: Incubation, Concentration Assay, Activity Assay

    (A) Eleven days post-confluent Caco-2 cells grown on Transwell filters were labeled with 50 µM biotin-RQRR-CMK from the basolateral side for the times indicated (2–180 min) at 37°C (lanes 3–6) or for 180 min at 4°C (lane 7). As a measure of the steady state level of matriptase, membrane proteins on the basolateral plasma membrane of filter-grown Caco-2 cells were labeled by incubation with S-NHS-SS-biotin at 4°C for 30 min (lane 1). As a negative control, cells were labeled from the basolateral side with 50 µM control peptide; biotin-RQRR (lane 2). All cells were lysed and biotinylated proteins were precipitated using streptavidin-coated resin and were analyzed by non-reducing SDS-PAGE and Western blotting using the monoclonal matriptase antibody; M32. A tenth of the surface biotinylated sample was loaded (lane 1); whereas total sample volume was loaded for the other samples (lanes 2-7). (B) Caco-2 cells grown on Transwell filters were labeled with the biotin-RQRR-CMK peptide inhibitor from either the apical (lanes 1, 4, and 7) or the basolateral (lanes 2, 5, and 8) side for 180 min at either 4°C or 37°C. An overexposure of lanes 1–3 is shown in lanes 7–9. As a negative control, cells were labeled from the basolateral side with a peptide corresponding to the inhibitory peptide but lacking the CMK moiety (CTRL, lanes 3, 6, and 9). Cells were lysed and the lysates of multiple filters were pooled. Biotinylated proteins were precipitated using streptavidin-coated resin and the streptavidin pull downs were released by boiling in SDS-PAGE samples buffer and analyzed by SDS-PAGE and Western blotting using the monoclonal M32 antibody. Positions of the molecular weight markers (kDa) are indicated on the left. Results shown are representative of 3 independent experiments.
    Figure Legend Snippet: (A) Eleven days post-confluent Caco-2 cells grown on Transwell filters were labeled with 50 µM biotin-RQRR-CMK from the basolateral side for the times indicated (2–180 min) at 37°C (lanes 3–6) or for 180 min at 4°C (lane 7). As a measure of the steady state level of matriptase, membrane proteins on the basolateral plasma membrane of filter-grown Caco-2 cells were labeled by incubation with S-NHS-SS-biotin at 4°C for 30 min (lane 1). As a negative control, cells were labeled from the basolateral side with 50 µM control peptide; biotin-RQRR (lane 2). All cells were lysed and biotinylated proteins were precipitated using streptavidin-coated resin and were analyzed by non-reducing SDS-PAGE and Western blotting using the monoclonal matriptase antibody; M32. A tenth of the surface biotinylated sample was loaded (lane 1); whereas total sample volume was loaded for the other samples (lanes 2-7). (B) Caco-2 cells grown on Transwell filters were labeled with the biotin-RQRR-CMK peptide inhibitor from either the apical (lanes 1, 4, and 7) or the basolateral (lanes 2, 5, and 8) side for 180 min at either 4°C or 37°C. An overexposure of lanes 1–3 is shown in lanes 7–9. As a negative control, cells were labeled from the basolateral side with a peptide corresponding to the inhibitory peptide but lacking the CMK moiety (CTRL, lanes 3, 6, and 9). Cells were lysed and the lysates of multiple filters were pooled. Biotinylated proteins were precipitated using streptavidin-coated resin and the streptavidin pull downs were released by boiling in SDS-PAGE samples buffer and analyzed by SDS-PAGE and Western blotting using the monoclonal M32 antibody. Positions of the molecular weight markers (kDa) are indicated on the left. Results shown are representative of 3 independent experiments.

    Techniques Used: Labeling, Incubation, Negative Control, SDS Page, Western Blot, Molecular Weight

    (A) Eleven days post-confluent filter-grown Caco-2 cells were treated with either a physiologically phosphate buffer pH 6.0 for 20 min (lanes 2, 4, 6, and 8) from both the apical and the basolateral side or left untreated (lanes 1, 3, 5, and 7). Cells were lysed and lysates were analyzed by Western blotting using antibodies against total matriptase (M24; lanes 1 and 2), matriptase SPD (IM1014; lanes 5 and 6), matriptase-HAI-1 complex (M69; lanes 3 and 4) and HAI-1 (lanes 7 and 8). Samples in lanes 1–4, 7, and 8 were not boiled to avoid dissociation of matriptase-HAI-1 complexes, while samples in lanes 5 and 6 were boiled and reduced to dissociate the S-S bridged SPD from the stem domain of activated matriptase in order to distinguish between the SEA domain-cleaved form (70 kDa) and the Arg614 cleaved form (25–30 kDa). Treatment with phosphate buffer pH 6.0 and DTT is indicated by +/−. Positions of the molecular weight markers (kDa) are indicated on the left. (B) A solution of 0.2 µM SPD was incubated for 10 min at 37°C with (crosses) or without (squares) 50 µM biotin-RQRR-CMK before addition the chromogenic substrate to a final concentration of 300 µM. All experiments were performed in 20 mM citric acid buffer pH 6.0, 140 mM NaCl and 0.1% BSA at 37°C. Results shown are representative of 3 independent experiments.
    Figure Legend Snippet: (A) Eleven days post-confluent filter-grown Caco-2 cells were treated with either a physiologically phosphate buffer pH 6.0 for 20 min (lanes 2, 4, 6, and 8) from both the apical and the basolateral side or left untreated (lanes 1, 3, 5, and 7). Cells were lysed and lysates were analyzed by Western blotting using antibodies against total matriptase (M24; lanes 1 and 2), matriptase SPD (IM1014; lanes 5 and 6), matriptase-HAI-1 complex (M69; lanes 3 and 4) and HAI-1 (lanes 7 and 8). Samples in lanes 1–4, 7, and 8 were not boiled to avoid dissociation of matriptase-HAI-1 complexes, while samples in lanes 5 and 6 were boiled and reduced to dissociate the S-S bridged SPD from the stem domain of activated matriptase in order to distinguish between the SEA domain-cleaved form (70 kDa) and the Arg614 cleaved form (25–30 kDa). Treatment with phosphate buffer pH 6.0 and DTT is indicated by +/−. Positions of the molecular weight markers (kDa) are indicated on the left. (B) A solution of 0.2 µM SPD was incubated for 10 min at 37°C with (crosses) or without (squares) 50 µM biotin-RQRR-CMK before addition the chromogenic substrate to a final concentration of 300 µM. All experiments were performed in 20 mM citric acid buffer pH 6.0, 140 mM NaCl and 0.1% BSA at 37°C. Results shown are representative of 3 independent experiments.

    Techniques Used: Western Blot, Molecular Weight, Incubation, Concentration Assay

    Eleven days post-confluent Caco-2 cells grown on Transwell filters were labeled with 50 µM biotin-RQRR-CMK from the basolateral side for 180 min at 37°C. As a negative control, cells were labeled from the basolateral side with 50 µM control peptide; biotin-RQRR (CTRL), under the same conditions. Labeled proteases were precipitated using streptavidin-coated resin and the streptavidin pull downs were analyzed by reducing SDS-PAGE and Western blotting using the IM1014 antibody raised against matriptase SPD. Positions of the molecular weight markers (kDa) are indicated on the left and position of SEA domain-cleaved zymogen matriptase and matriptase SPD is indicated on the right. Results shown are representative of 3 independent experiments.
    Figure Legend Snippet: Eleven days post-confluent Caco-2 cells grown on Transwell filters were labeled with 50 µM biotin-RQRR-CMK from the basolateral side for 180 min at 37°C. As a negative control, cells were labeled from the basolateral side with 50 µM control peptide; biotin-RQRR (CTRL), under the same conditions. Labeled proteases were precipitated using streptavidin-coated resin and the streptavidin pull downs were analyzed by reducing SDS-PAGE and Western blotting using the IM1014 antibody raised against matriptase SPD. Positions of the molecular weight markers (kDa) are indicated on the left and position of SEA domain-cleaved zymogen matriptase and matriptase SPD is indicated on the right. Results shown are representative of 3 independent experiments.

    Techniques Used: Labeling, Negative Control, SDS Page, Western Blot, Molecular Weight

    Murine keratinocytes were isolated from newborn wildtype (WT) or matriptase-deficient pups (KO) and cultured on collagen-coated plastic. The cells were grown until sub-confluent and then labeled with S-NHS-SS-biotin (lanes 1, 4, 7, and 10), or with 50 µM biotin-RQRR-CMK (lanes 2, 5, 8, and 11), or with 50 µM control peptide; biotin-RQRR (lanes 3, 6, 9, and 12). Cells were lysed and analyzed on Western blot (lanes 7–12). The remaining lysates were precipitated using streptavidin-coated resin, released from the beads by boiling under non-reducing conditions and lysates were analyzed by SDS-PAGE and Western blotting using the matriptase antibody AF3946. Results shown are representative of 2 independent experiments.
    Figure Legend Snippet: Murine keratinocytes were isolated from newborn wildtype (WT) or matriptase-deficient pups (KO) and cultured on collagen-coated plastic. The cells were grown until sub-confluent and then labeled with S-NHS-SS-biotin (lanes 1, 4, 7, and 10), or with 50 µM biotin-RQRR-CMK (lanes 2, 5, 8, and 11), or with 50 µM control peptide; biotin-RQRR (lanes 3, 6, 9, and 12). Cells were lysed and analyzed on Western blot (lanes 7–12). The remaining lysates were precipitated using streptavidin-coated resin, released from the beads by boiling under non-reducing conditions and lysates were analyzed by SDS-PAGE and Western blotting using the matriptase antibody AF3946. Results shown are representative of 2 independent experiments.

    Techniques Used: Isolation, Cell Culture, Labeling, Western Blot, SDS Page



    Similar Products

    sheep anti matriptase  (R&D Systems)
    92
    R&D Systems sheep anti matriptase
    (A) Schematic structure of the biotin-RQRR-CMK peptide inhibitor. (B) The reactivity of biotin-RQRR-CMK was tested after 180 min of pre-incubation at 37°C (diamonds) or without preincubation (crosses). 0.2 µM <t>matriptase</t> SPD was incubated for 10 min at 37°C with (diamonds and crosses) or without (squares) 50 µM biotin-RQRR-CMK before addition of the chromogenic substrate to a final concentration of 300 µM. (C) The stability of 5 nM biotin-RQRR-CMK was further tested after the time points 0 (crosses), 60 (circles), 120 (stars), and 180 min (diamonds) of pre-incubation at 37°C and compared to a control not containing biotin-RQRR-CMK (squares). As described above, 0.2 nM matriptase SPD was added to each sample and incubated for 10 min at 37°C followed by addition of the chromogenic substrate to a final concentration of 300 µM. In all cases, the enzymatic activity of SPD was monitored by conversion of the chromogenic substrate (S2288). Each plot shows the change in optical density at 405 nm of the reaction mixture as a function of reaction time. The presence of active protease results in a continued release of a yellow cleavage product resulting in a linear color development in agreement with a pseudo 1 st order reaction due to the high molar excess of substrate to protease. Results shown are representative of 3 independent experiments.
    Sheep Anti Matriptase, supplied by R&D Systems, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/sheep anti matriptase/product/R&D Systems
    Average 92 stars, based on 1 article reviews
    sheep anti matriptase - by Bioz Stars, 2026-03
    92/100 stars
    		  Buy from Supplier
    sheep anti human matriptase pab  (R&D Systems)
    96
    R&D Systems sheep anti human matriptase pab
    (A) Schematic structure of the biotin-RQRR-CMK peptide inhibitor. (B) The reactivity of biotin-RQRR-CMK was tested after 180 min of pre-incubation at 37°C (diamonds) or without preincubation (crosses). 0.2 µM <t>matriptase</t> SPD was incubated for 10 min at 37°C with (diamonds and crosses) or without (squares) 50 µM biotin-RQRR-CMK before addition of the chromogenic substrate to a final concentration of 300 µM. (C) The stability of 5 nM biotin-RQRR-CMK was further tested after the time points 0 (crosses), 60 (circles), 120 (stars), and 180 min (diamonds) of pre-incubation at 37°C and compared to a control not containing biotin-RQRR-CMK (squares). As described above, 0.2 nM matriptase SPD was added to each sample and incubated for 10 min at 37°C followed by addition of the chromogenic substrate to a final concentration of 300 µM. In all cases, the enzymatic activity of SPD was monitored by conversion of the chromogenic substrate (S2288). Each plot shows the change in optical density at 405 nm of the reaction mixture as a function of reaction time. The presence of active protease results in a continued release of a yellow cleavage product resulting in a linear color development in agreement with a pseudo 1 st order reaction due to the high molar excess of substrate to protease. Results shown are representative of 3 independent experiments.
    Sheep Anti Human Matriptase Pab, supplied by R&D Systems, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/sheep anti human matriptase pab/product/R&D Systems
    Average 96 stars, based on 1 article reviews
    sheep anti human matriptase pab - by Bioz Stars, 2026-03
    96/100 stars
    		  Buy from Supplier
    sheep polyclonal anti matriptase catalytic domain antibody  (R&D Systems)
    96
    R&D Systems sheep polyclonal anti matriptase catalytic domain antibody
    Fig. 2. Identification of Trop2 as a target for <t>matriptase.</t> (A) Sequence alignment of a part of human EpCAM and human Trop2 protein sequences. Scissors denote reported N-terminal cleavage site in human EpCAM between Arg80 and Arg81 [19]. It corresponds to Arg87 and Thr88 (boxed) in human Trop2 which were selected for generating alanine substitution mutants. (The conserved residues between the two proteins are indicated by asterisks below the sequence.) Amino acid numbering is including the signal peptide. (B) Expression of WT Trop2-HA and the indicated alanine substitution mutants. Total cell lysate from HEK293 cells transiently transfected with either WT Trop2- HA or R87A Trop2-HA or T88A Trop2-HA was immunoblotted before (left) and after PNGase treatment (right) using anti-HA antibody (upper panel) and anti-GAPDH antibody (lower panel) (C) Cell surface localization of Trop2 (green) in nonpermeabilized HEK293 cells transiently expressing the indicated Trop2-HA constructs visualized by indirect immunofluorescence using anti-Trop2 ECD antibody. DAPI (blue) was used as a nuclear stain. Bar = 10 µm. HEK293 cells transfected with an EV served as a negative control. (D) HEK293 cells were cotransfected with the indicated amount of WT Trop2-HA and either WT matriptase (Mat-HA) or inactive matriptase (Mat-M-HA) constructs. Cell lysates were prepared 48 h post-transfection followed by immunoblotting with anti-HA antibody to detect matriptase as well as Trop2 protein. GAPDH is the loading control (lower panel). Filled triangle and hollow triangle represents full-length Trop2 and DN-Trop2, respectively. (E) Immunoblot showing matriptase expression in the total cell lysates of the indicated cell lines using anti-matriptase antibody (upper panel). Expression of GAPDH in each cell line serves as the loading control (lower panel).
    Sheep Polyclonal Anti Matriptase Catalytic Domain Antibody, supplied by R&D Systems, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/sheep polyclonal anti matriptase catalytic domain antibody/product/R&D Systems
    Average 96 stars, based on 1 article reviews
    sheep polyclonal anti matriptase catalytic domain antibody - by Bioz Stars, 2026-03
    96/100 stars
    		  Buy from Supplier
    polyclonal sheep anti human matriptase st14 antibody  (R&D Systems)
    96
    R&D Systems polyclonal sheep anti human matriptase st14 antibody
    Fig. 2. Identification of Trop2 as a target for <t>matriptase.</t> (A) Sequence alignment of a part of human EpCAM and human Trop2 protein sequences. Scissors denote reported N-terminal cleavage site in human EpCAM between Arg80 and Arg81 [19]. It corresponds to Arg87 and Thr88 (boxed) in human Trop2 which were selected for generating alanine substitution mutants. (The conserved residues between the two proteins are indicated by asterisks below the sequence.) Amino acid numbering is including the signal peptide. (B) Expression of WT Trop2-HA and the indicated alanine substitution mutants. Total cell lysate from HEK293 cells transiently transfected with either WT Trop2- HA or R87A Trop2-HA or T88A Trop2-HA was immunoblotted before (left) and after PNGase treatment (right) using anti-HA antibody (upper panel) and anti-GAPDH antibody (lower panel) (C) Cell surface localization of Trop2 (green) in nonpermeabilized HEK293 cells transiently expressing the indicated Trop2-HA constructs visualized by indirect immunofluorescence using anti-Trop2 ECD antibody. DAPI (blue) was used as a nuclear stain. Bar = 10 µm. HEK293 cells transfected with an EV served as a negative control. (D) HEK293 cells were cotransfected with the indicated amount of WT Trop2-HA and either WT matriptase (Mat-HA) or inactive matriptase (Mat-M-HA) constructs. Cell lysates were prepared 48 h post-transfection followed by immunoblotting with anti-HA antibody to detect matriptase as well as Trop2 protein. GAPDH is the loading control (lower panel). Filled triangle and hollow triangle represents full-length Trop2 and DN-Trop2, respectively. (E) Immunoblot showing matriptase expression in the total cell lysates of the indicated cell lines using anti-matriptase antibody (upper panel). Expression of GAPDH in each cell line serves as the loading control (lower panel).
    Polyclonal Sheep Anti Human Matriptase St14 Antibody, supplied by R&D Systems, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/polyclonal sheep anti human matriptase st14 antibody/product/R&D Systems
    Average 96 stars, based on 1 article reviews
    polyclonal sheep anti human matriptase st14 antibody - by Bioz Stars, 2026-03
    96/100 stars
    		  Buy from Supplier
    polyclonal sheep anti human matriptase antibody  (R&D Systems)
    96
    R&D Systems polyclonal sheep anti human matriptase antibody
    Figure 2. HAI-2 SCSD-associated variants Phe161Val, Tyr163Cys and Gly168Ser stabilize <t>matriptase</t> and display unaffected inhibitory effect toward matriptase. (A) Each column represents the rate of turnover of the chromogenic substrate S-2288 without antibody (PBS, light grey column), with antibody aZ-mAb-6 inhibiting matriptase activity (aZ-mAb-6, black column) or with a control antibody (control, dark grey column) in extracts obtained by lysis of HEK293 cells transiently transfected
    Polyclonal Sheep Anti Human Matriptase Antibody, supplied by R&D Systems, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/polyclonal sheep anti human matriptase antibody/product/R&D Systems
    Average 96 stars, based on 1 article reviews
    polyclonal sheep anti human matriptase antibody - by Bioz Stars, 2026-03
    96/100 stars
    		  Buy from Supplier
    sheep anti human matriptase  (R&D Systems)
    93
    R&D Systems sheep anti human matriptase
    Figure 2. HAI-2 SCSD-associated variants Phe161Val, Tyr163Cys and Gly168Ser stabilize <t>matriptase</t> and display unaffected inhibitory effect toward matriptase. (A) Each column represents the rate of turnover of the chromogenic substrate S-2288 without antibody (PBS, light grey column), with antibody aZ-mAb-6 inhibiting matriptase activity (aZ-mAb-6, black column) or with a control antibody (control, dark grey column) in extracts obtained by lysis of HEK293 cells transiently transfected
    Sheep Anti Human Matriptase, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/sheep anti human matriptase/product/R&D Systems
    Average 93 stars, based on 1 article reviews
    sheep anti human matriptase - by Bioz Stars, 2026-03
    93/100 stars
    		  Buy from Supplier

    Image Search Results


    (A) Schematic structure of the biotin-RQRR-CMK peptide inhibitor. (B) The reactivity of biotin-RQRR-CMK was tested after 180 min of pre-incubation at 37°C (diamonds) or without preincubation (crosses). 0.2 µM matriptase SPD was incubated for 10 min at 37°C with (diamonds and crosses) or without (squares) 50 µM biotin-RQRR-CMK before addition of the chromogenic substrate to a final concentration of 300 µM. (C) The stability of 5 nM biotin-RQRR-CMK was further tested after the time points 0 (crosses), 60 (circles), 120 (stars), and 180 min (diamonds) of pre-incubation at 37°C and compared to a control not containing biotin-RQRR-CMK (squares). As described above, 0.2 nM matriptase SPD was added to each sample and incubated for 10 min at 37°C followed by addition of the chromogenic substrate to a final concentration of 300 µM. In all cases, the enzymatic activity of SPD was monitored by conversion of the chromogenic substrate (S2288). Each plot shows the change in optical density at 405 nm of the reaction mixture as a function of reaction time. The presence of active protease results in a continued release of a yellow cleavage product resulting in a linear color development in agreement with a pseudo 1 st order reaction due to the high molar excess of substrate to protease. Results shown are representative of 3 independent experiments.

    Journal: PLoS ONE

    Article Title: Detection of Active Matriptase Using a Biotinylated Chloromethyl Ketone Peptide

    doi: 10.1371/journal.pone.0077146

    Figure Lengend Snippet: (A) Schematic structure of the biotin-RQRR-CMK peptide inhibitor. (B) The reactivity of biotin-RQRR-CMK was tested after 180 min of pre-incubation at 37°C (diamonds) or without preincubation (crosses). 0.2 µM matriptase SPD was incubated for 10 min at 37°C with (diamonds and crosses) or without (squares) 50 µM biotin-RQRR-CMK before addition of the chromogenic substrate to a final concentration of 300 µM. (C) The stability of 5 nM biotin-RQRR-CMK was further tested after the time points 0 (crosses), 60 (circles), 120 (stars), and 180 min (diamonds) of pre-incubation at 37°C and compared to a control not containing biotin-RQRR-CMK (squares). As described above, 0.2 nM matriptase SPD was added to each sample and incubated for 10 min at 37°C followed by addition of the chromogenic substrate to a final concentration of 300 µM. In all cases, the enzymatic activity of SPD was monitored by conversion of the chromogenic substrate (S2288). Each plot shows the change in optical density at 405 nm of the reaction mixture as a function of reaction time. The presence of active protease results in a continued release of a yellow cleavage product resulting in a linear color development in agreement with a pseudo 1 st order reaction due to the high molar excess of substrate to protease. Results shown are representative of 3 independent experiments.

    Article Snippet: For detection of matriptase in murine cells, sheep anti-matriptase was used (AF3946 diluted 1∶1000, R&D).

    Techniques: Incubation, Concentration Assay, Activity Assay

    (A) Eleven days post-confluent Caco-2 cells grown on Transwell filters were labeled with 50 µM biotin-RQRR-CMK from the basolateral side for the times indicated (2–180 min) at 37°C (lanes 3–6) or for 180 min at 4°C (lane 7). As a measure of the steady state level of matriptase, membrane proteins on the basolateral plasma membrane of filter-grown Caco-2 cells were labeled by incubation with S-NHS-SS-biotin at 4°C for 30 min (lane 1). As a negative control, cells were labeled from the basolateral side with 50 µM control peptide; biotin-RQRR (lane 2). All cells were lysed and biotinylated proteins were precipitated using streptavidin-coated resin and were analyzed by non-reducing SDS-PAGE and Western blotting using the monoclonal matriptase antibody; M32. A tenth of the surface biotinylated sample was loaded (lane 1); whereas total sample volume was loaded for the other samples (lanes 2-7). (B) Caco-2 cells grown on Transwell filters were labeled with the biotin-RQRR-CMK peptide inhibitor from either the apical (lanes 1, 4, and 7) or the basolateral (lanes 2, 5, and 8) side for 180 min at either 4°C or 37°C. An overexposure of lanes 1–3 is shown in lanes 7–9. As a negative control, cells were labeled from the basolateral side with a peptide corresponding to the inhibitory peptide but lacking the CMK moiety (CTRL, lanes 3, 6, and 9). Cells were lysed and the lysates of multiple filters were pooled. Biotinylated proteins were precipitated using streptavidin-coated resin and the streptavidin pull downs were released by boiling in SDS-PAGE samples buffer and analyzed by SDS-PAGE and Western blotting using the monoclonal M32 antibody. Positions of the molecular weight markers (kDa) are indicated on the left. Results shown are representative of 3 independent experiments.

    Journal: PLoS ONE

    Article Title: Detection of Active Matriptase Using a Biotinylated Chloromethyl Ketone Peptide

    doi: 10.1371/journal.pone.0077146

    Figure Lengend Snippet: (A) Eleven days post-confluent Caco-2 cells grown on Transwell filters were labeled with 50 µM biotin-RQRR-CMK from the basolateral side for the times indicated (2–180 min) at 37°C (lanes 3–6) or for 180 min at 4°C (lane 7). As a measure of the steady state level of matriptase, membrane proteins on the basolateral plasma membrane of filter-grown Caco-2 cells were labeled by incubation with S-NHS-SS-biotin at 4°C for 30 min (lane 1). As a negative control, cells were labeled from the basolateral side with 50 µM control peptide; biotin-RQRR (lane 2). All cells were lysed and biotinylated proteins were precipitated using streptavidin-coated resin and were analyzed by non-reducing SDS-PAGE and Western blotting using the monoclonal matriptase antibody; M32. A tenth of the surface biotinylated sample was loaded (lane 1); whereas total sample volume was loaded for the other samples (lanes 2-7). (B) Caco-2 cells grown on Transwell filters were labeled with the biotin-RQRR-CMK peptide inhibitor from either the apical (lanes 1, 4, and 7) or the basolateral (lanes 2, 5, and 8) side for 180 min at either 4°C or 37°C. An overexposure of lanes 1–3 is shown in lanes 7–9. As a negative control, cells were labeled from the basolateral side with a peptide corresponding to the inhibitory peptide but lacking the CMK moiety (CTRL, lanes 3, 6, and 9). Cells were lysed and the lysates of multiple filters were pooled. Biotinylated proteins were precipitated using streptavidin-coated resin and the streptavidin pull downs were released by boiling in SDS-PAGE samples buffer and analyzed by SDS-PAGE and Western blotting using the monoclonal M32 antibody. Positions of the molecular weight markers (kDa) are indicated on the left. Results shown are representative of 3 independent experiments.

    Article Snippet: For detection of matriptase in murine cells, sheep anti-matriptase was used (AF3946 diluted 1∶1000, R&D).

    Techniques: Labeling, Incubation, Negative Control, SDS Page, Western Blot, Molecular Weight

    (A) Eleven days post-confluent filter-grown Caco-2 cells were treated with either a physiologically phosphate buffer pH 6.0 for 20 min (lanes 2, 4, 6, and 8) from both the apical and the basolateral side or left untreated (lanes 1, 3, 5, and 7). Cells were lysed and lysates were analyzed by Western blotting using antibodies against total matriptase (M24; lanes 1 and 2), matriptase SPD (IM1014; lanes 5 and 6), matriptase-HAI-1 complex (M69; lanes 3 and 4) and HAI-1 (lanes 7 and 8). Samples in lanes 1–4, 7, and 8 were not boiled to avoid dissociation of matriptase-HAI-1 complexes, while samples in lanes 5 and 6 were boiled and reduced to dissociate the S-S bridged SPD from the stem domain of activated matriptase in order to distinguish between the SEA domain-cleaved form (70 kDa) and the Arg614 cleaved form (25–30 kDa). Treatment with phosphate buffer pH 6.0 and DTT is indicated by +/−. Positions of the molecular weight markers (kDa) are indicated on the left. (B) A solution of 0.2 µM SPD was incubated for 10 min at 37°C with (crosses) or without (squares) 50 µM biotin-RQRR-CMK before addition the chromogenic substrate to a final concentration of 300 µM. All experiments were performed in 20 mM citric acid buffer pH 6.0, 140 mM NaCl and 0.1% BSA at 37°C. Results shown are representative of 3 independent experiments.

    Journal: PLoS ONE

    Article Title: Detection of Active Matriptase Using a Biotinylated Chloromethyl Ketone Peptide

    doi: 10.1371/journal.pone.0077146

    Figure Lengend Snippet: (A) Eleven days post-confluent filter-grown Caco-2 cells were treated with either a physiologically phosphate buffer pH 6.0 for 20 min (lanes 2, 4, 6, and 8) from both the apical and the basolateral side or left untreated (lanes 1, 3, 5, and 7). Cells were lysed and lysates were analyzed by Western blotting using antibodies against total matriptase (M24; lanes 1 and 2), matriptase SPD (IM1014; lanes 5 and 6), matriptase-HAI-1 complex (M69; lanes 3 and 4) and HAI-1 (lanes 7 and 8). Samples in lanes 1–4, 7, and 8 were not boiled to avoid dissociation of matriptase-HAI-1 complexes, while samples in lanes 5 and 6 were boiled and reduced to dissociate the S-S bridged SPD from the stem domain of activated matriptase in order to distinguish between the SEA domain-cleaved form (70 kDa) and the Arg614 cleaved form (25–30 kDa). Treatment with phosphate buffer pH 6.0 and DTT is indicated by +/−. Positions of the molecular weight markers (kDa) are indicated on the left. (B) A solution of 0.2 µM SPD was incubated for 10 min at 37°C with (crosses) or without (squares) 50 µM biotin-RQRR-CMK before addition the chromogenic substrate to a final concentration of 300 µM. All experiments were performed in 20 mM citric acid buffer pH 6.0, 140 mM NaCl and 0.1% BSA at 37°C. Results shown are representative of 3 independent experiments.

    Article Snippet: For detection of matriptase in murine cells, sheep anti-matriptase was used (AF3946 diluted 1∶1000, R&D).

    Techniques: Western Blot, Molecular Weight, Incubation, Concentration Assay

    Eleven days post-confluent Caco-2 cells grown on Transwell filters were labeled with 50 µM biotin-RQRR-CMK from the basolateral side for 180 min at 37°C. As a negative control, cells were labeled from the basolateral side with 50 µM control peptide; biotin-RQRR (CTRL), under the same conditions. Labeled proteases were precipitated using streptavidin-coated resin and the streptavidin pull downs were analyzed by reducing SDS-PAGE and Western blotting using the IM1014 antibody raised against matriptase SPD. Positions of the molecular weight markers (kDa) are indicated on the left and position of SEA domain-cleaved zymogen matriptase and matriptase SPD is indicated on the right. Results shown are representative of 3 independent experiments.

    Journal: PLoS ONE

    Article Title: Detection of Active Matriptase Using a Biotinylated Chloromethyl Ketone Peptide

    doi: 10.1371/journal.pone.0077146

    Figure Lengend Snippet: Eleven days post-confluent Caco-2 cells grown on Transwell filters were labeled with 50 µM biotin-RQRR-CMK from the basolateral side for 180 min at 37°C. As a negative control, cells were labeled from the basolateral side with 50 µM control peptide; biotin-RQRR (CTRL), under the same conditions. Labeled proteases were precipitated using streptavidin-coated resin and the streptavidin pull downs were analyzed by reducing SDS-PAGE and Western blotting using the IM1014 antibody raised against matriptase SPD. Positions of the molecular weight markers (kDa) are indicated on the left and position of SEA domain-cleaved zymogen matriptase and matriptase SPD is indicated on the right. Results shown are representative of 3 independent experiments.

    Article Snippet: For detection of matriptase in murine cells, sheep anti-matriptase was used (AF3946 diluted 1∶1000, R&D).

    Techniques: Labeling, Negative Control, SDS Page, Western Blot, Molecular Weight

    Murine keratinocytes were isolated from newborn wildtype (WT) or matriptase-deficient pups (KO) and cultured on collagen-coated plastic. The cells were grown until sub-confluent and then labeled with S-NHS-SS-biotin (lanes 1, 4, 7, and 10), or with 50 µM biotin-RQRR-CMK (lanes 2, 5, 8, and 11), or with 50 µM control peptide; biotin-RQRR (lanes 3, 6, 9, and 12). Cells were lysed and analyzed on Western blot (lanes 7–12). The remaining lysates were precipitated using streptavidin-coated resin, released from the beads by boiling under non-reducing conditions and lysates were analyzed by SDS-PAGE and Western blotting using the matriptase antibody AF3946. Results shown are representative of 2 independent experiments.

    Journal: PLoS ONE

    Article Title: Detection of Active Matriptase Using a Biotinylated Chloromethyl Ketone Peptide

    doi: 10.1371/journal.pone.0077146

    Figure Lengend Snippet: Murine keratinocytes were isolated from newborn wildtype (WT) or matriptase-deficient pups (KO) and cultured on collagen-coated plastic. The cells were grown until sub-confluent and then labeled with S-NHS-SS-biotin (lanes 1, 4, 7, and 10), or with 50 µM biotin-RQRR-CMK (lanes 2, 5, 8, and 11), or with 50 µM control peptide; biotin-RQRR (lanes 3, 6, 9, and 12). Cells were lysed and analyzed on Western blot (lanes 7–12). The remaining lysates were precipitated using streptavidin-coated resin, released from the beads by boiling under non-reducing conditions and lysates were analyzed by SDS-PAGE and Western blotting using the matriptase antibody AF3946. Results shown are representative of 2 independent experiments.

    Article Snippet: For detection of matriptase in murine cells, sheep anti-matriptase was used (AF3946 diluted 1∶1000, R&D).

    Techniques: Isolation, Cell Culture, Labeling, Western Blot, SDS Page

    Fig. 2. Identification of Trop2 as a target for matriptase. (A) Sequence alignment of a part of human EpCAM and human Trop2 protein sequences. Scissors denote reported N-terminal cleavage site in human EpCAM between Arg80 and Arg81 [19]. It corresponds to Arg87 and Thr88 (boxed) in human Trop2 which were selected for generating alanine substitution mutants. (The conserved residues between the two proteins are indicated by asterisks below the sequence.) Amino acid numbering is including the signal peptide. (B) Expression of WT Trop2-HA and the indicated alanine substitution mutants. Total cell lysate from HEK293 cells transiently transfected with either WT Trop2- HA or R87A Trop2-HA or T88A Trop2-HA was immunoblotted before (left) and after PNGase treatment (right) using anti-HA antibody (upper panel) and anti-GAPDH antibody (lower panel) (C) Cell surface localization of Trop2 (green) in nonpermeabilized HEK293 cells transiently expressing the indicated Trop2-HA constructs visualized by indirect immunofluorescence using anti-Trop2 ECD antibody. DAPI (blue) was used as a nuclear stain. Bar = 10 µm. HEK293 cells transfected with an EV served as a negative control. (D) HEK293 cells were cotransfected with the indicated amount of WT Trop2-HA and either WT matriptase (Mat-HA) or inactive matriptase (Mat-M-HA) constructs. Cell lysates were prepared 48 h post-transfection followed by immunoblotting with anti-HA antibody to detect matriptase as well as Trop2 protein. GAPDH is the loading control (lower panel). Filled triangle and hollow triangle represents full-length Trop2 and DN-Trop2, respectively. (E) Immunoblot showing matriptase expression in the total cell lysates of the indicated cell lines using anti-matriptase antibody (upper panel). Expression of GAPDH in each cell line serves as the loading control (lower panel).

    Journal: FEBS letters

    Article Title: Proteolytic cleavage of Trop2 at Arg87 is mediated by matriptase and regulated by Val194.

    doi: 10.1002/1873-3468.13899

    Figure Lengend Snippet: Fig. 2. Identification of Trop2 as a target for matriptase. (A) Sequence alignment of a part of human EpCAM and human Trop2 protein sequences. Scissors denote reported N-terminal cleavage site in human EpCAM between Arg80 and Arg81 [19]. It corresponds to Arg87 and Thr88 (boxed) in human Trop2 which were selected for generating alanine substitution mutants. (The conserved residues between the two proteins are indicated by asterisks below the sequence.) Amino acid numbering is including the signal peptide. (B) Expression of WT Trop2-HA and the indicated alanine substitution mutants. Total cell lysate from HEK293 cells transiently transfected with either WT Trop2- HA or R87A Trop2-HA or T88A Trop2-HA was immunoblotted before (left) and after PNGase treatment (right) using anti-HA antibody (upper panel) and anti-GAPDH antibody (lower panel) (C) Cell surface localization of Trop2 (green) in nonpermeabilized HEK293 cells transiently expressing the indicated Trop2-HA constructs visualized by indirect immunofluorescence using anti-Trop2 ECD antibody. DAPI (blue) was used as a nuclear stain. Bar = 10 µm. HEK293 cells transfected with an EV served as a negative control. (D) HEK293 cells were cotransfected with the indicated amount of WT Trop2-HA and either WT matriptase (Mat-HA) or inactive matriptase (Mat-M-HA) constructs. Cell lysates were prepared 48 h post-transfection followed by immunoblotting with anti-HA antibody to detect matriptase as well as Trop2 protein. GAPDH is the loading control (lower panel). Filled triangle and hollow triangle represents full-length Trop2 and DN-Trop2, respectively. (E) Immunoblot showing matriptase expression in the total cell lysates of the indicated cell lines using anti-matriptase antibody (upper panel). Expression of GAPDH in each cell line serves as the loading control (lower panel).

    Article Snippet: Antibodies used in this study include a goat polyclonal anti-Trop2 antibody directed against ECD of Trop2 (1 : 3000, AF650; R & D Systems, Minneapolis, MN, USA), rabbit monoclonal antibody targeted against C-terminal region of Trop2 (1 : 2000, ab214 488; abcam, Cambridge, MA, USA), mouse monoclonal anti-HA (1 : 1000, ab18 181; abcam), anti-CD63 (1 : 500, ab59 479; abcam), sheep polyclonal anti-matriptase catalytic domain antibody (1 : 1000, AF3946; R & D Systems), mouse monoclonal antibody against GAPDH (1 : 10 000, MA5-15738; Thermo Fisher Scientific), and mouse monoclonal anti-Flag antibody (1 : 1000, F1804; Sigma-Aldrich, St. Louis, MO, USA).

    Techniques: Sequencing, Expressing, Transfection, Construct, Staining, Negative Control, Western Blot, Control

    Fig. 3. Homology modeling of Trop2 ECD dimer. (A) Modeled structure of Trop2 ECD (1–275) dimer. Monomeric subunits are color coded (cyan and golden yellow). Positions of matriptase cleavage site between Arg87 and Thr88 and the predicted ADAM17 cleavage site Val194 is highlighted as red sticks for one monomer and as indigo sticks for another monomer. Zoomed-in image shows that the Arg87 and Thr88 of one monomer are in the same plane as that of Val194 of another monomer. (B) Sequence alignment of a part of mouse and human Trop2 protein sequences. Val188, which is a reported ADAM17 cleavage site in mTrop2, is denoted by scissors [16]. It corresponds to Val194 (boxed) in human Trop2. The conserved residues are indicated by asterisks below the sequence. Red arrows denote the amino acids (Lys189, Val194, and His195) selected for site-directed mutagenesis.

    Journal: FEBS letters

    Article Title: Proteolytic cleavage of Trop2 at Arg87 is mediated by matriptase and regulated by Val194.

    doi: 10.1002/1873-3468.13899

    Figure Lengend Snippet: Fig. 3. Homology modeling of Trop2 ECD dimer. (A) Modeled structure of Trop2 ECD (1–275) dimer. Monomeric subunits are color coded (cyan and golden yellow). Positions of matriptase cleavage site between Arg87 and Thr88 and the predicted ADAM17 cleavage site Val194 is highlighted as red sticks for one monomer and as indigo sticks for another monomer. Zoomed-in image shows that the Arg87 and Thr88 of one monomer are in the same plane as that of Val194 of another monomer. (B) Sequence alignment of a part of mouse and human Trop2 protein sequences. Val188, which is a reported ADAM17 cleavage site in mTrop2, is denoted by scissors [16]. It corresponds to Val194 (boxed) in human Trop2. The conserved residues are indicated by asterisks below the sequence. Red arrows denote the amino acids (Lys189, Val194, and His195) selected for site-directed mutagenesis.

    Article Snippet: Antibodies used in this study include a goat polyclonal anti-Trop2 antibody directed against ECD of Trop2 (1 : 3000, AF650; R & D Systems, Minneapolis, MN, USA), rabbit monoclonal antibody targeted against C-terminal region of Trop2 (1 : 2000, ab214 488; abcam, Cambridge, MA, USA), mouse monoclonal anti-HA (1 : 1000, ab18 181; abcam), anti-CD63 (1 : 500, ab59 479; abcam), sheep polyclonal anti-matriptase catalytic domain antibody (1 : 1000, AF3946; R & D Systems), mouse monoclonal antibody against GAPDH (1 : 10 000, MA5-15738; Thermo Fisher Scientific), and mouse monoclonal anti-Flag antibody (1 : 1000, F1804; Sigma-Aldrich, St. Louis, MO, USA).

    Techniques: Sequencing, Mutagenesis

    Figure 2. HAI-2 SCSD-associated variants Phe161Val, Tyr163Cys and Gly168Ser stabilize matriptase and display unaffected inhibitory effect toward matriptase. (A) Each column represents the rate of turnover of the chromogenic substrate S-2288 without antibody (PBS, light grey column), with antibody aZ-mAb-6 inhibiting matriptase activity (aZ-mAb-6, black column) or with a control antibody (control, dark grey column) in extracts obtained by lysis of HEK293 cells transiently transfected

    Journal: Human molecular genetics

    Article Title: SPINT2 (HAI-2) missense variants identified in congenital sodium diarrhea/tufting enteropathy affect the ability of HAI-2 to inhibit prostasin but not matriptase.

    doi: 10.1093/hmg/ddy394

    Figure Lengend Snippet: Figure 2. HAI-2 SCSD-associated variants Phe161Val, Tyr163Cys and Gly168Ser stabilize matriptase and display unaffected inhibitory effect toward matriptase. (A) Each column represents the rate of turnover of the chromogenic substrate S-2288 without antibody (PBS, light grey column), with antibody aZ-mAb-6 inhibiting matriptase activity (aZ-mAb-6, black column) or with a control antibody (control, dark grey column) in extracts obtained by lysis of HEK293 cells transiently transfected

    Article Snippet: All samples for WB were boiled under reducing conditions and blots were probed with primary polyclonal sheep anti-human matriptase antibody (cat. no. AF3946, R&D systems, Abington, United Kingdom) (1:1000), polyclonal rabbit anti-human HAI2 antibody (cat. no. HPA011101, Sigma) (1:1000), monoclonal mouse anti-human prostasin (cat. no. 612173, BD Transduction LaboratoriesTM, Albertslund, Denmark) recognizing prostasin and with GAPDH antibody (cat. no. ZG003, Thermo Fischer Scientific, Hvidovre, Denmark) (1:2000) as control.

    Techniques: Activity Assay, Control, Lysis, Transfection

    Figure 3. HAI-2 SCSD-associated variants Phe161Val, Tyr163Cys and Gly168Ser display reduced ability to inhibit prostasin-catalyzed cleavage. Extracts obtained by lysis of HEK293 cells transiently transfected with matriptase Ser805Ala (mat Ser805Ala) alone, matriptase Ser805Ala with prostasin (pro), matriptase Ser805Ala and prostasin together with HAI-2 WT or mutated HAI-2 variants (Cys47Phe/Arg48Leu, Arg143Leu, Phe161Val, Tyr163Cys or Gly168Ser), as indicated above the figure,

    Journal: Human molecular genetics

    Article Title: SPINT2 (HAI-2) missense variants identified in congenital sodium diarrhea/tufting enteropathy affect the ability of HAI-2 to inhibit prostasin but not matriptase.

    doi: 10.1093/hmg/ddy394

    Figure Lengend Snippet: Figure 3. HAI-2 SCSD-associated variants Phe161Val, Tyr163Cys and Gly168Ser display reduced ability to inhibit prostasin-catalyzed cleavage. Extracts obtained by lysis of HEK293 cells transiently transfected with matriptase Ser805Ala (mat Ser805Ala) alone, matriptase Ser805Ala with prostasin (pro), matriptase Ser805Ala and prostasin together with HAI-2 WT or mutated HAI-2 variants (Cys47Phe/Arg48Leu, Arg143Leu, Phe161Val, Tyr163Cys or Gly168Ser), as indicated above the figure,

    Article Snippet: All samples for WB were boiled under reducing conditions and blots were probed with primary polyclonal sheep anti-human matriptase antibody (cat. no. AF3946, R&D systems, Abington, United Kingdom) (1:1000), polyclonal rabbit anti-human HAI2 antibody (cat. no. HPA011101, Sigma) (1:1000), monoclonal mouse anti-human prostasin (cat. no. 612173, BD Transduction LaboratoriesTM, Albertslund, Denmark) recognizing prostasin and with GAPDH antibody (cat. no. ZG003, Thermo Fischer Scientific, Hvidovre, Denmark) (1:2000) as control.

    Techniques: Lysis, Transfection

    Figure 5. Proposed schematic structure of inhibitory complexes between prostasin or matriptase and HAI-2 WT or SCSD-mutated HAI-2. A schematic overview of suggested HAI-2 inhibitory complexes between (A) prostasin (green) and WT HAI-2, (B) prostasin and SCSD-associated HAI-2 mutants, (C) matriptase (red) and WT HAI-2

    Journal: Human molecular genetics

    Article Title: SPINT2 (HAI-2) missense variants identified in congenital sodium diarrhea/tufting enteropathy affect the ability of HAI-2 to inhibit prostasin but not matriptase.

    doi: 10.1093/hmg/ddy394

    Figure Lengend Snippet: Figure 5. Proposed schematic structure of inhibitory complexes between prostasin or matriptase and HAI-2 WT or SCSD-mutated HAI-2. A schematic overview of suggested HAI-2 inhibitory complexes between (A) prostasin (green) and WT HAI-2, (B) prostasin and SCSD-associated HAI-2 mutants, (C) matriptase (red) and WT HAI-2

    Article Snippet: All samples for WB were boiled under reducing conditions and blots were probed with primary polyclonal sheep anti-human matriptase antibody (cat. no. AF3946, R&D systems, Abington, United Kingdom) (1:1000), polyclonal rabbit anti-human HAI2 antibody (cat. no. HPA011101, Sigma) (1:1000), monoclonal mouse anti-human prostasin (cat. no. 612173, BD Transduction LaboratoriesTM, Albertslund, Denmark) recognizing prostasin and with GAPDH antibody (cat. no. ZG003, Thermo Fischer Scientific, Hvidovre, Denmark) (1:2000) as control.

    Techniques: