sheep anti human matriptase pab (R&D Systems)
R&D Systems is a verified supplier 
R&D Systems manufactures this product 
93
Structured Review
R&D Systems
sheep anti human matriptase pab
Sheep Anti Human Matriptase Pab, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 25 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/sheep+anti-matriptase+antibody/Human+Matriptase%2FST14+Catalytic+Domain+Antibody/pm35020274-224-23-28
Average 93 stars, based on 25 article reviews
Sheep Anti Human Matriptase Pab, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 25 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/sheep+anti-matriptase+antibody/Human+Matriptase%2FST14+Catalytic+Domain+Antibody/pm35020274-224-23-28
Average 93 stars, based on 25 article reviews
sheep anti human matriptase pab - by Bioz Stars,
2026-10
93/100 stars
Images
Related Articles
Staining:Article Title: Inflammatory cytokines down-regulate the barrier-protective prostasin-matriptase proteolytic cascade early in experimental colitis Article Snippet: Sections were stained with 0.5 μg/ml Article Title: Inflammatory cytokines down-regulate the barrier-protective prostasin-matriptase proteolytic cascade early in experimental colitis Article Snippet: Sections were stained with 0.5 μg/ml Immunostaining:Article Title: Inflammatory cytokines down-regulate the barrier-protective prostasin-matriptase proteolytic cascade early in experimental colitis Article Snippet: Sections were stained with 0.5 μg/ml Article Title: Inflammatory cytokines down-regulate the barrier-protective prostasin-matriptase proteolytic cascade early in experimental colitis Article Snippet: Sections were stained with 0.5 μg/ml Expressing:Article Title: Inflammatory cytokines down-regulate the barrier-protective prostasin-matriptase proteolytic cascade early in experimental colitis Article Snippet: Sections were stained with 0.5 μg/ml Article Title: Inflammatory cytokines down-regulate the barrier-protective prostasin-matriptase proteolytic cascade early in experimental colitis Article Snippet: Sections were stained with 0.5 μg/ml Quantitation Assay:Article Title: Inflammatory cytokines down-regulate the barrier-protective prostasin-matriptase proteolytic cascade early in experimental colitis Article Snippet: Sections were stained with 0.5 μg/ml Article Title: Inflammatory cytokines down-regulate the barrier-protective prostasin-matriptase proteolytic cascade early in experimental colitis Article Snippet: Sections were stained with 0.5 μg/ml Isolation:Article Title: Inflammatory cytokines down-regulate the barrier-protective prostasin-matriptase proteolytic cascade early in experimental colitis Article Snippet: Sections were stained with 0.5 μg/ml Article Title: Inflammatory cytokines down-regulate the barrier-protective prostasin-matriptase proteolytic cascade early in experimental colitis Article Snippet: Sections were stained with 0.5 μg/ml Marker:Article Title: Inflammatory cytokines down-regulate the barrier-protective prostasin-matriptase proteolytic cascade early in experimental colitis Article Snippet: Sections were stained with 0.5 μg/ml Article Title: Inflammatory cytokines down-regulate the barrier-protective prostasin-matriptase proteolytic cascade early in experimental colitis Article Snippet: Sections were stained with 0.5 μg/ml Disruption:Article Title: Inflammatory cytokines down-regulate the barrier-protective prostasin-matriptase proteolytic cascade early in experimental colitis Article Snippet: Sections were stained with 0.5 μg/ml Article Title: Inflammatory cytokines down-regulate the barrier-protective prostasin-matriptase proteolytic cascade early in experimental colitis Article Snippet: Sections were stained with 0.5 μg/ml Permeability:Article Title: Inflammatory cytokines down-regulate the barrier-protective prostasin-matriptase proteolytic cascade early in experimental colitis Article Snippet: Sections were stained with 0.5 μg/ml Article Title: Inflammatory cytokines down-regulate the barrier-protective prostasin-matriptase proteolytic cascade early in experimental colitis Article Snippet: Sections were stained with 0.5 μg/ml Western Blot:Article Title: Inflammatory cytokines down-regulate the barrier-protective prostasin-matriptase proteolytic cascade early in experimental colitis Article Snippet: Sections were stained with 0.5 μg/ml Article Title: Inflammatory cytokines down-regulate the barrier-protective prostasin-matriptase proteolytic cascade early in experimental colitis Article Snippet: Sections were stained with 0.5 μg/ml Activation Assay:Article Title: Inflammatory cytokines down-regulate the barrier-protective prostasin-matriptase proteolytic cascade early in experimental colitis Article Snippet: Sections were stained with 0.5 μg/ml Article Title: Inflammatory cytokines down-regulate the barrier-protective prostasin-matriptase proteolytic cascade early in experimental colitis Article Snippet: Sections were stained with 0.5 μg/ml |
![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).](https://pub-med-unpaywalled-images-cdn.bioz.com/pub_med_ids_ending_with_1920/pm32761920/pm32761920__page6_image1.jpg)
![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.](https://pub-med-unpaywalled-images-cdn.bioz.com/pub_med_ids_ending_with_1920/pm32761920/pm32761920__page7_image1.jpg)
