type 2 collagenase  (Millipore)


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    Name:
    Collagenase II
    Description:
    This product is provided as delivered and specified by the issuing Pharmacopoeia All information provided in support of this product including MSDS and any product information leaflets have been developed and issued under the Authority of the issuing Pharmacopoeia For further information and support please go to the website of the issuing Pharmacopoeia
    Catalog Number:
    1148090
    Price:
    None
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    Structured Review

    Millipore type 2 collagenase
    Collagenase II
    This product is provided as delivered and specified by the issuing Pharmacopoeia All information provided in support of this product including MSDS and any product information leaflets have been developed and issued under the Authority of the issuing Pharmacopoeia For further information and support please go to the website of the issuing Pharmacopoeia
    https://www.bioz.com/result/type 2 collagenase/product/Millipore
    Average 99 stars, based on 20 article reviews
    Price from $9.99 to $1999.99
    type 2 collagenase - by Bioz Stars, 2020-05
    99/100 stars

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    Related Articles

    Isolation:

    Article Title: Optimization and qualification of a memory B-cell ELISpot for the detection of vaccine-induced memory responses in HIV vaccine trials
    Article Snippet: .. GMMC from biopsies obtained by flexible sigmoidoscopy were isolated by two rounds of digestion with collagenase II (Sigma-Aldrich, St. Louis, MO) followed by gradient centrifugation using Histopaque (Sigma, St. Louis, MO). .. GMMC were counted on a Guava Counter using αCD45-FITC, αCD19-PE and 7AAD (BD Biosciences, San Jose, CA) for enumeration of live B cells, and were used after overnight rest at 37°C.

    Incubation:

    Article Title: Vascular smooth muscle cell proliferation depends on caveolin-1-regulated polyamine uptake
    Article Snippet: .. The adventitia was then pulled off using forceps and the aorta was incubated for another 2 h in DMEM with 2 mg/ml collagenase type 2 and 0.2 mg/ml elastase (Sigma). .. The primary ASMCs were cultured in the DMEM medium with addition of antibiotics (50 units/ml penicillin and 50 μg/ml streptomycin) and 10% (v/v)FBS and trypsinized [0.25% (w/v) trypsin] upon reaching confluence.

    Article Title: Role of voltage-dependent calcium channels in stimulus-secretion coupling in rabbit carotid body chemoreceptor cells
    Article Snippet: .. The CBs (usually two) were incubated for 30 min in nominally Ca2+ and Mg2+ -free Tyrode solution (pH 7.2) containing collagenase (2.5 mg ml−1 , type IV, Sigma) and bovine serum albumin (6 mg ml−1 , Fraction V, Sigma). .. After centrifugation (800 g , 5 min), the pellet was placed in new solution containing collagenase (1 mg ml−1 ), trypsin (1 mg ml−1 , type II, Sigma) and bovine serum albumin (6 mg ml−1 ) for an additional 15-min period.

    Gradient Centrifugation:

    Article Title: Optimization and qualification of a memory B-cell ELISpot for the detection of vaccine-induced memory responses in HIV vaccine trials
    Article Snippet: .. GMMC from biopsies obtained by flexible sigmoidoscopy were isolated by two rounds of digestion with collagenase II (Sigma-Aldrich, St. Louis, MO) followed by gradient centrifugation using Histopaque (Sigma, St. Louis, MO). .. GMMC were counted on a Guava Counter using αCD45-FITC, αCD19-PE and 7AAD (BD Biosciences, San Jose, CA) for enumeration of live B cells, and were used after overnight rest at 37°C.

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  • 93
    Millipore matrix metalloproteinase 2
    Regulation of cell migration-associated proteins by NCKU-21 in A549 and CL1-5 cells. Protein expressions of matrix <t>metalloproteinase-2</t> (MMP-2) and MMP-9 were analyzed in A549 (A) and CL1-5 (B) cells treated with NCKU-21 for 24 hr. * P
    Matrix Metalloproteinase 2, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/matrix metalloproteinase 2/product/Millipore
    Average 93 stars, based on 5 article reviews
    Price from $9.99 to $1999.99
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    85
    Millipore mouse anti gelatinase b igg
    Matrilysin “deficiency” abrogates plasminogen-dependent elastolysis by human MDMs and mouse peritoneal macrophages. (A) Mouse peritoneal macrophages or human monocytes differentiated for 9 d atop the surface of either bacteriologic plastic dishes (Plastic) or a cell-derived ECM (Matrix; phase micrographs are shown on the right of A) were cultured with elastin suspended in transwell inserts as described in Fig. 1 in the absence or presence of 50 μg/ml plasminogen (plg). Where indicated, macrophages were incubated with or without 5 μM BB-94. In the presence of plasminogen and BB-94, the release of radiolabel from elastin is due primarily to plasmin activity and can be reduced to background levels with aprotinin (unpublished data). Results are shown as μg elastin degraded/10 6 cells for 5 d (mean ± SEM; n = 3). (B) Secretion of elastolytic MMPs by human MDMs and murine macrophages as a function of in vitro culture conditions. Human MDMs differentiated atop surfaces of bacteriologic plastic (Plastic) or the cell-derived matrix (Matrix) were cultured under serum-free conditions for 48 h. Conditioned media was collected and analyzed by immunoblot for gelatinase B, human metalloelastase (HME), and matrilysin. Mouse macrophages were cultured in bacteriologic plastic dishes for 48 h under serum-free conditions and conditioned media was analyzed for MMPs by immunoblot as described in Fig. 1 . (C) Human MDMs were cocultured with [ 3 H]elastin and incubated alone (lane 1), with 50 μg/ml plasminogen (plg; lane 2), or plasminogen in the presence of aprotinin (lane 3), BB-94 (lane 4), anti–gelatinase B antibody (lane 5), or normal mouse <t>IgG</t> (both 50 μg/ml; lane 6). MMP-9 processing was assessed by gelatin zymography (top) and the effects on degradative activity were quantified (bottom). Results are expressed as μg elastin degraded/10 6 cells for 5 d (mean ± SEM; n = 3). (D) Human MDMs differentiated atop a cell-derived matrix (Matrix) or mouse peritoneal macrophages cultured under standard conditions (Plastic) were incubated with [ 3 H]elastin and 50 μg/ml plasminogen in the absence or presence of 5 μM BB-94. Where indicated, 20 nM recombinant promatrilysin was added to the culture system in the absence or presence of BB-94. 20 nM recombinant promatrilysin and 25 μg/ml plasmin were also incubated with elastin under cell-free conditions (Cell-Free). Inset shows the relative levels of matrilysin detected in media conditioned by human MDMs (Mφ CM) and the amount of recombinant matrilysin added (rMMP-7). Results are expressed as μg elastin degraded/10 6 cells for 5 d (mean ± SEM; n = 3). (E) Equimolar quantities (1.0 pmol) of active site–titrated gelatinase B, human metalloelastase, or matrilysin alone, or all three enzymes together were incubated with [ 3 H]elastin in serum-free media at 37°C. Results are expressed as μg elastin degraded for 5 d (mean ± SEM; n = 3).
    Mouse Anti Gelatinase B Igg, supplied by Millipore, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore zymography digestion buffer
    The activities of MMPs and TIMPs, and cell invasion through Mtrigel are examined in hypoxic condition. Left; Gelatin and reverse <t>zymography</t> reveal that the activities of MMP-2, MMP-9 and TIMP-1 are not affected by incubation of HP-75 cells under hypoxic
    Zymography Digestion Buffer, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/zymography digestion buffer/product/Millipore
    Average 99 stars, based on 2 article reviews
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    zymography digestion buffer - by Bioz Stars, 2020-05
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    Image Search Results


    Regulation of cell migration-associated proteins by NCKU-21 in A549 and CL1-5 cells. Protein expressions of matrix metalloproteinase-2 (MMP-2) and MMP-9 were analyzed in A549 (A) and CL1-5 (B) cells treated with NCKU-21 for 24 hr. * P

    Journal: PLoS ONE

    Article Title: Toxicological effects of NCKU-21, a phenanthrene derivative, on cell growth and migration of A549 and CL1-5 human lung adenocarcinoma cells

    doi: 10.1371/journal.pone.0185021

    Figure Lengend Snippet: Regulation of cell migration-associated proteins by NCKU-21 in A549 and CL1-5 cells. Protein expressions of matrix metalloproteinase-2 (MMP-2) and MMP-9 were analyzed in A549 (A) and CL1-5 (B) cells treated with NCKU-21 for 24 hr. * P

    Article Snippet: Primary antibodies for detecting phosphatidylinositol-3-kinase (PI3K; #06–497), AKT (#07–416), phospho-AKT (#07–310), p53 (#CBL404), matrix metalloproteinase-2 (MMP-2; #AB19015), and MMP-9 (#AB19016) were from Millipore (Bedford, MA, USA).

    Techniques: Migration

    Analysis of the association of n-3 polyunsaturated fatty acid with the concentration of interferon gamma, interleukin-8, matrix metalloproteinase-2 and matrix metalloproteinase-9 in colorectal cancer. Q means quartiles. PUFA: Polyunsaturated fatty acids;

    Journal: World Journal of Gastroenterology

    Article Title: Relationship of serum polyunsaturated fatty acids with cytokines in colorectal cancer

    doi: 10.3748/wjg.v22.i8.2524

    Figure Lengend Snippet: Analysis of the association of n-3 polyunsaturated fatty acid with the concentration of interferon gamma, interleukin-8, matrix metalloproteinase-2 and matrix metalloproteinase-9 in colorectal cancer. Q means quartiles. PUFA: Polyunsaturated fatty acids;

    Article Snippet: A multiplex bead-based sandwich immunoassay kits was used to detect the serum concentration of interferon gamma (IFN-γ), IL-10, IL-6, IL-8, TNF-α, matrix metalloproteinase-2 (MMP-2), MMP-7 and MMP-9 according to the instruction of manufacturer (HCYTOMAG-60K, Millipore, Billerica, MA, United States).

    Techniques: Concentration Assay

    Matrilysin “deficiency” abrogates plasminogen-dependent elastolysis by human MDMs and mouse peritoneal macrophages. (A) Mouse peritoneal macrophages or human monocytes differentiated for 9 d atop the surface of either bacteriologic plastic dishes (Plastic) or a cell-derived ECM (Matrix; phase micrographs are shown on the right of A) were cultured with elastin suspended in transwell inserts as described in Fig. 1 in the absence or presence of 50 μg/ml plasminogen (plg). Where indicated, macrophages were incubated with or without 5 μM BB-94. In the presence of plasminogen and BB-94, the release of radiolabel from elastin is due primarily to plasmin activity and can be reduced to background levels with aprotinin (unpublished data). Results are shown as μg elastin degraded/10 6 cells for 5 d (mean ± SEM; n = 3). (B) Secretion of elastolytic MMPs by human MDMs and murine macrophages as a function of in vitro culture conditions. Human MDMs differentiated atop surfaces of bacteriologic plastic (Plastic) or the cell-derived matrix (Matrix) were cultured under serum-free conditions for 48 h. Conditioned media was collected and analyzed by immunoblot for gelatinase B, human metalloelastase (HME), and matrilysin. Mouse macrophages were cultured in bacteriologic plastic dishes for 48 h under serum-free conditions and conditioned media was analyzed for MMPs by immunoblot as described in Fig. 1 . (C) Human MDMs were cocultured with [ 3 H]elastin and incubated alone (lane 1), with 50 μg/ml plasminogen (plg; lane 2), or plasminogen in the presence of aprotinin (lane 3), BB-94 (lane 4), anti–gelatinase B antibody (lane 5), or normal mouse IgG (both 50 μg/ml; lane 6). MMP-9 processing was assessed by gelatin zymography (top) and the effects on degradative activity were quantified (bottom). Results are expressed as μg elastin degraded/10 6 cells for 5 d (mean ± SEM; n = 3). (D) Human MDMs differentiated atop a cell-derived matrix (Matrix) or mouse peritoneal macrophages cultured under standard conditions (Plastic) were incubated with [ 3 H]elastin and 50 μg/ml plasminogen in the absence or presence of 5 μM BB-94. Where indicated, 20 nM recombinant promatrilysin was added to the culture system in the absence or presence of BB-94. 20 nM recombinant promatrilysin and 25 μg/ml plasmin were also incubated with elastin under cell-free conditions (Cell-Free). Inset shows the relative levels of matrilysin detected in media conditioned by human MDMs (Mφ CM) and the amount of recombinant matrilysin added (rMMP-7). Results are expressed as μg elastin degraded/10 6 cells for 5 d (mean ± SEM; n = 3). (E) Equimolar quantities (1.0 pmol) of active site–titrated gelatinase B, human metalloelastase, or matrilysin alone, or all three enzymes together were incubated with [ 3 H]elastin in serum-free media at 37°C. Results are expressed as μg elastin degraded for 5 d (mean ± SEM; n = 3).

    Journal: The Journal of Experimental Medicine

    Article Title: Matrilysin-dependent Elastolysis by Human Macrophages

    doi: 10.1084/jem.20030626

    Figure Lengend Snippet: Matrilysin “deficiency” abrogates plasminogen-dependent elastolysis by human MDMs and mouse peritoneal macrophages. (A) Mouse peritoneal macrophages or human monocytes differentiated for 9 d atop the surface of either bacteriologic plastic dishes (Plastic) or a cell-derived ECM (Matrix; phase micrographs are shown on the right of A) were cultured with elastin suspended in transwell inserts as described in Fig. 1 in the absence or presence of 50 μg/ml plasminogen (plg). Where indicated, macrophages were incubated with or without 5 μM BB-94. In the presence of plasminogen and BB-94, the release of radiolabel from elastin is due primarily to plasmin activity and can be reduced to background levels with aprotinin (unpublished data). Results are shown as μg elastin degraded/10 6 cells for 5 d (mean ± SEM; n = 3). (B) Secretion of elastolytic MMPs by human MDMs and murine macrophages as a function of in vitro culture conditions. Human MDMs differentiated atop surfaces of bacteriologic plastic (Plastic) or the cell-derived matrix (Matrix) were cultured under serum-free conditions for 48 h. Conditioned media was collected and analyzed by immunoblot for gelatinase B, human metalloelastase (HME), and matrilysin. Mouse macrophages were cultured in bacteriologic plastic dishes for 48 h under serum-free conditions and conditioned media was analyzed for MMPs by immunoblot as described in Fig. 1 . (C) Human MDMs were cocultured with [ 3 H]elastin and incubated alone (lane 1), with 50 μg/ml plasminogen (plg; lane 2), or plasminogen in the presence of aprotinin (lane 3), BB-94 (lane 4), anti–gelatinase B antibody (lane 5), or normal mouse IgG (both 50 μg/ml; lane 6). MMP-9 processing was assessed by gelatin zymography (top) and the effects on degradative activity were quantified (bottom). Results are expressed as μg elastin degraded/10 6 cells for 5 d (mean ± SEM; n = 3). (D) Human MDMs differentiated atop a cell-derived matrix (Matrix) or mouse peritoneal macrophages cultured under standard conditions (Plastic) were incubated with [ 3 H]elastin and 50 μg/ml plasminogen in the absence or presence of 5 μM BB-94. Where indicated, 20 nM recombinant promatrilysin was added to the culture system in the absence or presence of BB-94. 20 nM recombinant promatrilysin and 25 μg/ml plasmin were also incubated with elastin under cell-free conditions (Cell-Free). Inset shows the relative levels of matrilysin detected in media conditioned by human MDMs (Mφ CM) and the amount of recombinant matrilysin added (rMMP-7). Results are expressed as μg elastin degraded/10 6 cells for 5 d (mean ± SEM; n = 3). (E) Equimolar quantities (1.0 pmol) of active site–titrated gelatinase B, human metalloelastase, or matrilysin alone, or all three enzymes together were incubated with [ 3 H]elastin in serum-free media at 37°C. Results are expressed as μg elastin degraded for 5 d (mean ± SEM; n = 3).

    Article Snippet: Where indicated, macrophage/[3 H]elastin cocultures were incubated alone, with 50 μg/ml glu-type human plasminogen, 100 μg/ml mouse-neutralizing antibody against human uPA (American Diagnostica, Inc.), mouse anti–gelatinase B IgG (ab-2; reference ), 50 μg/ml normal mouse IgG (both from Oncogene Research Products and Calbiochem-Novabiochem), recombinant human pro–MMP-7 (Chemicon International, Inc.), recombinant human pro–gelatinase B and A (R & D Systems), 5 μM of the synthetic MMP inhibitor, BB94 (0.1% DMSO final; provided by British Biotechnology; reference 22), 5 μg/ml endotoxin-free recombinant human tissue inhibitor of metalloproteinases-2 (TIMP-2; Fuji Chemical Industries, LTD.; reference 22), 100 μM the pan-specific cysteine proteinase inhibitors, E-64 (0.05% ethanol final; Sigma-Aldrich; reference 16), 100 μg/ml aprotinin (Roche; reference 22), 5 μM the aspartate protease inhibitor, pepstatin (0.05% ethanol final; Roche; reference 23), or solvents (0.1% DMSO and 0.05% ethanol) alone.

    Techniques: Derivative Assay, Cell Culture, Incubation, Activity Assay, In Vitro, Zymography, Recombinant

    The activities of MMPs and TIMPs, and cell invasion through Mtrigel are examined in hypoxic condition. Left; Gelatin and reverse zymography reveal that the activities of MMP-2, MMP-9 and TIMP-1 are not affected by incubation of HP-75 cells under hypoxic

    Journal:

    Article Title: Elevated Cell Invasion Is Induced by Hypoxia in a Human Pituitary Adenoma Cell Line

    doi:

    Figure Lengend Snippet: The activities of MMPs and TIMPs, and cell invasion through Mtrigel are examined in hypoxic condition. Left; Gelatin and reverse zymography reveal that the activities of MMP-2, MMP-9 and TIMP-1 are not affected by incubation of HP-75 cells under hypoxic

    Article Snippet: The cell supernatants were resolved as described above, and the gels were washed in 50 mM Tris, 5 mM CaCl2 and 2.5% (v/v) Triton X-100 for 2.5 hours at 23°C and then incubated in reverse zymography digestion buffer (50 mM Tris, 5 mM CaCl2 , 100 mU/ml gelatinase A (Calbiochem, Cambridge, Mass., USA) for four hours at 37°C.

    Techniques: Zymography, Incubation