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  • 99
    Millipore pepstatin a
    Pepstatin A, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pepstatin a/product/Millipore
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    pepstatin a - by Bioz Stars, 2021-05
    99/100 stars
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    86
    Roche pepstatin
    PMN cell released proteases cleave decorin in vitro . PMN cells were isolated from peripheral human blood and treated with vehicle or PMA. Conditioned media were collected and incubated with bovine decorin with or without protease inhibitors for 30 minutes. (A) Representative Western blot of decorin: Lane 1: partially degraded decorin in human skin 24 hours post UV irradiation. Lane 2: Bovine decorin-treated with conditioned media obtained from vehicle-treated PMN cells. Lanes 3–7: bovine decorin incubated with conditioned media obtained from PMA-treated cells with or without various protease inhibitors as indicated. EDTA is an inhibitor of metalloproteinase; Aprotinin (Apr) is an inhibitor of serine protease; E-64 is an inhibitor of cysteine protease; <t>Pepstatin</t> (PEP) is an inhibitor of aspartate protease. Four major decorin fragments are indicated by arrow heads. (b) Quantification of Western blots by ImageQuant software. Data are Western blots lanes 3–7. Results are mean ± SEM, (N = 3; * p
    Pepstatin, supplied by Roche, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pepstatin/product/Roche
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    pepstatin - by Bioz Stars, 2021-05
    86/100 stars
      Buy from Supplier

    99
    Thermo Fisher pepstatin a
    PMN cell released proteases cleave decorin in vitro . PMN cells were isolated from peripheral human blood and treated with vehicle or PMA. Conditioned media were collected and incubated with bovine decorin with or without protease inhibitors for 30 minutes. (A) Representative Western blot of decorin: Lane 1: partially degraded decorin in human skin 24 hours post UV irradiation. Lane 2: Bovine decorin-treated with conditioned media obtained from vehicle-treated PMN cells. Lanes 3–7: bovine decorin incubated with conditioned media obtained from PMA-treated cells with or without various protease inhibitors as indicated. EDTA is an inhibitor of metalloproteinase; Aprotinin (Apr) is an inhibitor of serine protease; E-64 is an inhibitor of cysteine protease; <t>Pepstatin</t> (PEP) is an inhibitor of aspartate protease. Four major decorin fragments are indicated by arrow heads. (b) Quantification of Western blots by ImageQuant software. Data are Western blots lanes 3–7. Results are mean ± SEM, (N = 3; * p
    Pepstatin A, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pepstatin a/product/Thermo Fisher
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    pepstatin a - by Bioz Stars, 2021-05
    99/100 stars
      Buy from Supplier

    86
    Peptide Institute pepstatin a
    Degradation of invariant chain (Ii) molecules in cathepsin inhibitor-treated A20 cells (a) and BALB/c mice (b). (a) Cells (10 8 ) were incubated for 4 hr in the absence (lane 1) or in the presence of CA074 (lane 2), <t>pepstatin</t> A (lane 3), or leupeptin (lane 4) (each at 100 μg/ml). The cells were then lysed and immunoprecipitated with In-1 (anti-Ii) monoclonal antibody (mAb), as described in the Materials and methods. Immunoprecipitates were separated by sodium dodecyl sulphate–polyacrylamide gel electrophoresis (SDS–PAGE) and stained using silver-staining reagents. In-1 mAb only is shown in lane 5. IgH is the H chain of immunoglobulin, and IgL is the L chain of immunoglobulin. (b) BALB/c mice were treated with CA074 or pepstatin A for 10 days. Splenocytes were collected and blocked with normal mouse serum for 30 min at 37° and then stained with fluorescein isothiocyanate (FITC)-conjugated anti-mouse Ii mAb (solid lines) Dotted lines indicate the unstained control.
    Pepstatin A, supplied by Peptide Institute, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pepstatin a/product/Peptide Institute
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    pepstatin a - by Bioz Stars, 2021-05
    86/100 stars
      Buy from Supplier

    N/A
    Aspartic protease inhibitor
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    N/A
    Pepstatin A is a bacterial derived chemotactic pentapeptide that irreversibly inhibits aspartic proteases including pepsin gastricsin renin cathepsin E and cathepsin D Pepstatin A has been reported to stimulate human
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    N/A
    A cell permeable methyl ester derivative of Pepstatin A that acts as a potent non competitive transition state analog inhibitor of γ secretase
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    Image Search Results


    PMN cell released proteases cleave decorin in vitro . PMN cells were isolated from peripheral human blood and treated with vehicle or PMA. Conditioned media were collected and incubated with bovine decorin with or without protease inhibitors for 30 minutes. (A) Representative Western blot of decorin: Lane 1: partially degraded decorin in human skin 24 hours post UV irradiation. Lane 2: Bovine decorin-treated with conditioned media obtained from vehicle-treated PMN cells. Lanes 3–7: bovine decorin incubated with conditioned media obtained from PMA-treated cells with or without various protease inhibitors as indicated. EDTA is an inhibitor of metalloproteinase; Aprotinin (Apr) is an inhibitor of serine protease; E-64 is an inhibitor of cysteine protease; Pepstatin (PEP) is an inhibitor of aspartate protease. Four major decorin fragments are indicated by arrow heads. (b) Quantification of Western blots by ImageQuant software. Data are Western blots lanes 3–7. Results are mean ± SEM, (N = 3; * p

    Journal: PLoS ONE

    Article Title: Solar Ultraviolet Irradiation Induces Decorin Degradation in Human Skin Likely via Neutrophil Elastase

    doi: 10.1371/journal.pone.0072563

    Figure Lengend Snippet: PMN cell released proteases cleave decorin in vitro . PMN cells were isolated from peripheral human blood and treated with vehicle or PMA. Conditioned media were collected and incubated with bovine decorin with or without protease inhibitors for 30 minutes. (A) Representative Western blot of decorin: Lane 1: partially degraded decorin in human skin 24 hours post UV irradiation. Lane 2: Bovine decorin-treated with conditioned media obtained from vehicle-treated PMN cells. Lanes 3–7: bovine decorin incubated with conditioned media obtained from PMA-treated cells with or without various protease inhibitors as indicated. EDTA is an inhibitor of metalloproteinase; Aprotinin (Apr) is an inhibitor of serine protease; E-64 is an inhibitor of cysteine protease; Pepstatin (PEP) is an inhibitor of aspartate protease. Four major decorin fragments are indicated by arrow heads. (b) Quantification of Western blots by ImageQuant software. Data are Western blots lanes 3–7. Results are mean ± SEM, (N = 3; * p

    Article Snippet: Proteinase inhibitors E-64, pepstatin, and aprotinin were purchased from Roche Applied Science (Indianapolis, IN).

    Techniques: In Vitro, Isolation, Incubation, Western Blot, Irradiation, Software

    Degradation of invariant chain (Ii) molecules in cathepsin inhibitor-treated A20 cells (a) and BALB/c mice (b). (a) Cells (10 8 ) were incubated for 4 hr in the absence (lane 1) or in the presence of CA074 (lane 2), pepstatin A (lane 3), or leupeptin (lane 4) (each at 100 μg/ml). The cells were then lysed and immunoprecipitated with In-1 (anti-Ii) monoclonal antibody (mAb), as described in the Materials and methods. Immunoprecipitates were separated by sodium dodecyl sulphate–polyacrylamide gel electrophoresis (SDS–PAGE) and stained using silver-staining reagents. In-1 mAb only is shown in lane 5. IgH is the H chain of immunoglobulin, and IgL is the L chain of immunoglobulin. (b) BALB/c mice were treated with CA074 or pepstatin A for 10 days. Splenocytes were collected and blocked with normal mouse serum for 30 min at 37° and then stained with fluorescein isothiocyanate (FITC)-conjugated anti-mouse Ii mAb (solid lines) Dotted lines indicate the unstained control.

    Journal: Immunology

    Article Title: Lysosomal cathepsin B plays an important role in antigen processing, while cathepsin D is involved in degradation of the invariant chain in ovalbumin-immunized mice

    doi: 10.1046/j.1365-2567.2000.00000.x

    Figure Lengend Snippet: Degradation of invariant chain (Ii) molecules in cathepsin inhibitor-treated A20 cells (a) and BALB/c mice (b). (a) Cells (10 8 ) were incubated for 4 hr in the absence (lane 1) or in the presence of CA074 (lane 2), pepstatin A (lane 3), or leupeptin (lane 4) (each at 100 μg/ml). The cells were then lysed and immunoprecipitated with In-1 (anti-Ii) monoclonal antibody (mAb), as described in the Materials and methods. Immunoprecipitates were separated by sodium dodecyl sulphate–polyacrylamide gel electrophoresis (SDS–PAGE) and stained using silver-staining reagents. In-1 mAb only is shown in lane 5. IgH is the H chain of immunoglobulin, and IgL is the L chain of immunoglobulin. (b) BALB/c mice were treated with CA074 or pepstatin A for 10 days. Splenocytes were collected and blocked with normal mouse serum for 30 min at 37° and then stained with fluorescein isothiocyanate (FITC)-conjugated anti-mouse Ii mAb (solid lines) Dotted lines indicate the unstained control.

    Article Snippet: On the other hand, pepstatin A did not influence the digestion of OVA, suggesting that immune suppression resulting from treatment with pepstatin A is not caused by digestion of OVA in the lysosome.

    Techniques: Mouse Assay, Incubation, Immunoprecipitation, Polyacrylamide Gel Electrophoresis, SDS Page, Staining, Silver Staining

    In vitro digestion of ovalbumin (OVA) by lysosomal proteases. Five micrograms of OVA was digested with 10 μg of mitochondria/lysosome (ML) fraction in the absence (lane 3) or in the presence of CA074 (lanes 4 and 5) or pepstatin A (lanes 6 and 7) (each at 1 μg/ml) for 3 hr at 37°. The OVA digests were then stained with Coomassie Brilliant Blue following separation by sodium dodecyl sulphate–polyacrylamide gel electrophoresis (SDS–PAGE). The untreated OVA control is shown in lane 1, and control lysosomes in lane 2. Filled arrowheads indicate the lysosomal band, and the open arrowhead indicates the band of digested OVA.

    Journal: Immunology

    Article Title: Lysosomal cathepsin B plays an important role in antigen processing, while cathepsin D is involved in degradation of the invariant chain in ovalbumin-immunized mice

    doi: 10.1046/j.1365-2567.2000.00000.x

    Figure Lengend Snippet: In vitro digestion of ovalbumin (OVA) by lysosomal proteases. Five micrograms of OVA was digested with 10 μg of mitochondria/lysosome (ML) fraction in the absence (lane 3) or in the presence of CA074 (lanes 4 and 5) or pepstatin A (lanes 6 and 7) (each at 1 μg/ml) for 3 hr at 37°. The OVA digests were then stained with Coomassie Brilliant Blue following separation by sodium dodecyl sulphate–polyacrylamide gel electrophoresis (SDS–PAGE). The untreated OVA control is shown in lane 1, and control lysosomes in lane 2. Filled arrowheads indicate the lysosomal band, and the open arrowhead indicates the band of digested OVA.

    Article Snippet: On the other hand, pepstatin A did not influence the digestion of OVA, suggesting that immune suppression resulting from treatment with pepstatin A is not caused by digestion of OVA in the lysosome.

    Techniques: In Vitro, Staining, Polyacrylamide Gel Electrophoresis, SDS Page

    T helper (Th) phenotype in mice treated with cathepsin inhibitors. Mice were immunized intraperitoneally (i.p.) with ovalbumin (OVA) adsorbed with alum. CA074 or pepstatin A (0·25 mg of each/mouse) was injected i.p. 2 hr before and after immunization and every 12 hr thereafter for 10 days. Frequencies of splenic interleukin (IL)-4, IL-5 and interferon-γ (IFN-γ)-secreting cells from naive, untreated, CA074- or pepstatin A-treated mice were determined by using an enzyme-linked immunospot (ELISPOT) assay. Spots were counted, and the results are expressed per 10 6 cells. Standard deviations (SD) were

    Journal: Immunology

    Article Title: Lysosomal cathepsin B plays an important role in antigen processing, while cathepsin D is involved in degradation of the invariant chain in ovalbumin-immunized mice

    doi: 10.1046/j.1365-2567.2000.00000.x

    Figure Lengend Snippet: T helper (Th) phenotype in mice treated with cathepsin inhibitors. Mice were immunized intraperitoneally (i.p.) with ovalbumin (OVA) adsorbed with alum. CA074 or pepstatin A (0·25 mg of each/mouse) was injected i.p. 2 hr before and after immunization and every 12 hr thereafter for 10 days. Frequencies of splenic interleukin (IL)-4, IL-5 and interferon-γ (IFN-γ)-secreting cells from naive, untreated, CA074- or pepstatin A-treated mice were determined by using an enzyme-linked immunospot (ELISPOT) assay. Spots were counted, and the results are expressed per 10 6 cells. Standard deviations (SD) were

    Article Snippet: On the other hand, pepstatin A did not influence the digestion of OVA, suggesting that immune suppression resulting from treatment with pepstatin A is not caused by digestion of OVA in the lysosome.

    Techniques: Mouse Assay, Injection, Enzyme-linked Immunospot

    The delayed-type hypersensitivity (DTH) response in mice treated with cathepsin inhibitors. Mice ( n  = 3–5) were challenged subcutaneously (s.c.) with 10 μg of ovalbumin (OVA) in alum in the left hind footpad 10 days after immunization with OVA. The size of the footpad swelling in naive, untreated, CA074- or pepstatin A-treated mice was measured by comparing the swollen footpad with the non-swollen footpad 24 hr after challenge. The results of the DTH reaction are representative of three individual experiments.

    Journal: Immunology

    Article Title: Lysosomal cathepsin B plays an important role in antigen processing, while cathepsin D is involved in degradation of the invariant chain in ovalbumin-immunized mice

    doi: 10.1046/j.1365-2567.2000.00000.x

    Figure Lengend Snippet: The delayed-type hypersensitivity (DTH) response in mice treated with cathepsin inhibitors. Mice ( n = 3–5) were challenged subcutaneously (s.c.) with 10 μg of ovalbumin (OVA) in alum in the left hind footpad 10 days after immunization with OVA. The size of the footpad swelling in naive, untreated, CA074- or pepstatin A-treated mice was measured by comparing the swollen footpad with the non-swollen footpad 24 hr after challenge. The results of the DTH reaction are representative of three individual experiments.

    Article Snippet: On the other hand, pepstatin A did not influence the digestion of OVA, suggesting that immune suppression resulting from treatment with pepstatin A is not caused by digestion of OVA in the lysosome.

    Techniques: Mouse Assay

    Levels of ovalbumin (OVA)-specific antibodies in mice treated with cathepsin inhibitors. Mice were treated as indicated in the Materials and methods, and serum titres of antigen-specific immunoglobulin G2a (IgG2a) and immunoglobulin E (IgE) from untreated, CA074- or pepstatin A-treated animals ( n  = 6) were assessed by using enzyme-linked immunosorbent assay (ELISA) 10 days after immunization. Results are representative of five separate experiments.

    Journal: Immunology

    Article Title: Lysosomal cathepsin B plays an important role in antigen processing, while cathepsin D is involved in degradation of the invariant chain in ovalbumin-immunized mice

    doi: 10.1046/j.1365-2567.2000.00000.x

    Figure Lengend Snippet: Levels of ovalbumin (OVA)-specific antibodies in mice treated with cathepsin inhibitors. Mice were treated as indicated in the Materials and methods, and serum titres of antigen-specific immunoglobulin G2a (IgG2a) and immunoglobulin E (IgE) from untreated, CA074- or pepstatin A-treated animals ( n = 6) were assessed by using enzyme-linked immunosorbent assay (ELISA) 10 days after immunization. Results are representative of five separate experiments.

    Article Snippet: On the other hand, pepstatin A did not influence the digestion of OVA, suggesting that immune suppression resulting from treatment with pepstatin A is not caused by digestion of OVA in the lysosome.

    Techniques: Mouse Assay, Enzyme-linked Immunosorbent Assay