biotrak activity assay Search Results


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  • 99
    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: 99/100, based on 59 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare biotrak mmp 2 activity
    Metalloprotease activity is inhibited by Dox-treated melanoma cells grown on different substrates. (A) Zymography assay of human melanoma cell lines SK-Mel-19, SK-Mel-103, and SK-Mel-147 treated with 1.2 μM of Dox (IC 50 ) or NT. (B) Gelatinolytic activity of <t>MMP-2</t> and -9 in human melanoma cell line SK-Mel-103 (C) Inhibition of MMP-2 activity of by <t>Biotrak</t> ® assay in human melanoma cell line SK-Mel-103, whose culture medium was incubated with a fluorescent substrate. Treatment conditions were melanoma cells seeded on plastic, in monolayer (M); on type I collagen (M+Col); on dermal equivalent (M+Eq); and the dermal equivalent control with no melanoma cells (Eq). *** p
    Biotrak Mmp 2 Activity, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 86/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare biotrak activity assay system
    Expression of MMP-2 and -9 activities (ng/mL) obtained with the <t>Biotrak™</t> activity assay system. ( A ) Comparison of enzyme activity in the etch-and-rinse group. Bar 1 , control mineralized dentin powder (G1 - MD); Bar 2 , dentin powder etched with
    Biotrak Activity Assay System, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 94/100, based on 22 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare mmp9 biotrak activity assay
    S1943 NMHC-IIA phosphorylation regulates <t>MMP9</t> secretion. (A) Gelatin zymography of conditioned medium from MDA-MB-231 cells expressing wild-type, S1943A or S1943E NMHC-IIA. Standards are human proMMP9 and active MMP2. (B and C) <t>Biotrak</t> MMP9 activity assay of (B) total MMP9 and (C) active MMP9 in conditioned medium from MDA-MB-231 cells expressing wild-type, S1943A or S1943E NMHC-IIA. Data represent the mean ± SEM from 3 independent experiments. Statistical analyses were performed using ANOVA.
    Mmp9 Biotrak Activity Assay, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 94/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    GE Healthcare biotrak mmp2 activity assay system
    S1943 NMHC-IIA phosphorylation regulates <t>MMP9</t> secretion. (A) Gelatin zymography of conditioned medium from MDA-MB-231 cells expressing wild-type, S1943A or S1943E NMHC-IIA. Standards are human proMMP9 and active MMP2. (B and C) <t>Biotrak</t> MMP9 activity assay of (B) total MMP9 and (C) active MMP9 in conditioned medium from MDA-MB-231 cells expressing wild-type, S1943A or S1943E NMHC-IIA. Data represent the mean ± SEM from 3 independent experiments. Statistical analyses were performed using ANOVA.
    Biotrak Mmp2 Activity Assay System, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 86/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    GE Healthcare biotrak activity assays
    Finasteride’s effects on MMP2 and MMP9 activity and TIMP-1 and TIMP-2 expression in the conditioned medium of RWPE-1 cells. a) Conditioned medium of untreated (Control) and finasteride-treated RWPE-1 cells were collected, concentrated and analyzed for MMP2 and MMP9 activities using their respective <t>Biotrak®</t> Activity Assays. Low-dose finasteride (10 µM) for 72 hours of exposure downregulated MMP2 and MMP9 activity by 25% and 30%, respectively, when compared to control values. High-dose finasteride (50 µM) downregulated MMP2 and MMP9 activities at all tested time points, up to 90% and 55% after 72 hours of exposure, respectively. b) Conditioned medium of untreated (Control) and finasteride-treated RWPE-1 cells were collected, concentrated and analyzed for TIMP-1 and TIMP-2 protein expression using their respective Biotrak® Assays. Finasteride exposure, at both doses, induced the upregulation of TIMP-2 expression at the 72 hour time point, up to 150% more expression than control levels. Data are expressed as a fold-change graphic of the IOD values that were obtained for finasteride-treated cells over those of the control cells. (*) Statistically significant values with p
    Biotrak Activity Assays, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 86/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare mmp 9 biotrak activity system
    Up-regulated <t>MMP-9</t> is not uniquely responsible for CD73 shedding. LPS and TNF-α, individually or in combination, on regulating MMP-9 expression extracellular activity were detected by qPCR ( a ) and a MMP-9 <t>Biotrak</t> activity assay ( b ). Effect of exogenous MMP-9 on CD73 shedding in Mmp9 −/− RPE cells received LPS/TNF-α treatment or not ( c ). a qPCR results of Mmp-9 expression in RPE cells ( n = 6). b Amount of active MMP-9 in the medium of RPE cells. c Effect of exogenous recombinant MMP-9 on regulating CD73 shedding; a representative flow cytometry result (left column) and statistical analysis of FACS determined percentage of CD73 positive cells (right column)
    Mmp 9 Biotrak Activity System, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 93/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare mmp 14 biotrak activity assay system
    Up-regulated <t>MMP-9</t> is not uniquely responsible for CD73 shedding. LPS and TNF-α, individually or in combination, on regulating MMP-9 expression extracellular activity were detected by qPCR ( a ) and a MMP-9 <t>Biotrak</t> activity assay ( b ). Effect of exogenous MMP-9 on CD73 shedding in Mmp9 −/− RPE cells received LPS/TNF-α treatment or not ( c ). a qPCR results of Mmp-9 expression in RPE cells ( n = 6). b Amount of active MMP-9 in the medium of RPE cells. c Effect of exogenous recombinant MMP-9 on regulating CD73 shedding; a representative flow cytometry result (left column) and statistical analysis of FACS determined percentage of CD73 positive cells (right column)
    Mmp 14 Biotrak Activity Assay System, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 85/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    GE Healthcare mmp1 biotrak activity assay system
    Up-regulated <t>MMP-9</t> is not uniquely responsible for CD73 shedding. LPS and TNF-α, individually or in combination, on regulating MMP-9 expression extracellular activity were detected by qPCR ( a ) and a MMP-9 <t>Biotrak</t> activity assay ( b ). Effect of exogenous MMP-9 on CD73 shedding in Mmp9 −/− RPE cells received LPS/TNF-α treatment or not ( c ). a qPCR results of Mmp-9 expression in RPE cells ( n = 6). b Amount of active MMP-9 in the medium of RPE cells. c Effect of exogenous recombinant MMP-9 on regulating CD73 shedding; a representative flow cytometry result (left column) and statistical analysis of FACS determined percentage of CD73 positive cells (right column)
    Mmp1 Biotrak Activity Assay System, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 86/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare mmps activity biotrak assay kits
    Up-regulated <t>MMP-9</t> is not uniquely responsible for CD73 shedding. LPS and TNF-α, individually or in combination, on regulating MMP-9 expression extracellular activity were detected by qPCR ( a ) and a MMP-9 <t>Biotrak</t> activity assay ( b ). Effect of exogenous MMP-9 on CD73 shedding in Mmp9 −/− RPE cells received LPS/TNF-α treatment or not ( c ). a qPCR results of Mmp-9 expression in RPE cells ( n = 6). b Amount of active MMP-9 in the medium of RPE cells. c Effect of exogenous recombinant MMP-9 on regulating CD73 shedding; a representative flow cytometry result (left column) and statistical analysis of FACS determined percentage of CD73 positive cells (right column)
    Mmps Activity Biotrak Assay Kits, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 86/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    GE Healthcare colorimetric biotrak mmp 9 activity assay
    Up-regulated <t>MMP-9</t> is not uniquely responsible for CD73 shedding. LPS and TNF-α, individually or in combination, on regulating MMP-9 expression extracellular activity were detected by qPCR ( a ) and a MMP-9 <t>Biotrak</t> activity assay ( b ). Effect of exogenous MMP-9 on CD73 shedding in Mmp9 −/− RPE cells received LPS/TNF-α treatment or not ( c ). a qPCR results of Mmp-9 expression in RPE cells ( n = 6). b Amount of active MMP-9 in the medium of RPE cells. c Effect of exogenous recombinant MMP-9 on regulating CD73 shedding; a representative flow cytometry result (left column) and statistical analysis of FACS determined percentage of CD73 positive cells (right column)
    Colorimetric Biotrak Mmp 9 Activity Assay, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 85/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    87
    GE Healthcare mmp9 biotrak activity assay kit
    Effects of rosiglitazone on the expression of MMP2 and <t>MMP9</t> in Cs-induced emphysema in rats. Notes: Effects of rosiglitazone on the expression of MMP2 and MMP9 in CS-induced emphysema in rats as measured by Western blotting ( A ). The target protein bands were desitometrically analyzed normalized to β-actin ( B ). The activities of MMP2 ( C ) and MMP9 ( D ) in each group were determined by using MMP2 and MMP9 <t>Biotrak™</t> activity assay. The expression of MMP2 and MMP9 was confirmed by using immunohistochemistry for each group (magnification ×400) ( E ). The values presented are the mean ± SD. * P
    Mmp9 Biotrak Activity Assay Kit, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 87/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare biotrak activity assay kits
    Evodiamine inhibits the expression of migration-associated regulators. ( A ) VSMCs were pretreated with evodiamine for 6 h and then stimulated with PDGF-BB for another 24 h. Western blot was used to measure the protein expression levels of regulators involved in the VSMC migration, including matrix metalloproteinase (MMP)-2, MMP-9, intercellular adhesion molecule-1 (ICAM-1), vascular cell adhesion molecule-1 (VCAM-1), and osteopontin (OPN). For both MMP-2 and MMP-9, their latent forms (72 and 92 kDa, respectively) were detected; ( B ) The signal ratio of examined protein to the internal control glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was quantified by densitometric scanning; ( C ) The concentrations of MMP-2 and -9 in the culture medium were detected by Enzyme Linked Immunosorbent Assay (ELISA); ( D ) The activities of MMP-2 and MMP-9 were determined by using their respective <t>Biotrak</t> Activity Assay Systems. Evo, evodiamine. Data are presented as mean values ± SD of three independent experiments. * p
    Biotrak Activity Assay Kits, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 88/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    84
    R&D Systems mmp 9 biotrak activity assay system kits
    Evodiamine inhibits the expression of migration-associated regulators. ( A ) VSMCs were pretreated with evodiamine for 6 h and then stimulated with PDGF-BB for another 24 h. Western blot was used to measure the protein expression levels of regulators involved in the VSMC migration, including matrix metalloproteinase (MMP)-2, MMP-9, intercellular adhesion molecule-1 (ICAM-1), vascular cell adhesion molecule-1 (VCAM-1), and osteopontin (OPN). For both MMP-2 and MMP-9, their latent forms (72 and 92 kDa, respectively) were detected; ( B ) The signal ratio of examined protein to the internal control glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was quantified by densitometric scanning; ( C ) The concentrations of MMP-2 and -9 in the culture medium were detected by Enzyme Linked Immunosorbent Assay (ELISA); ( D ) The activities of MMP-2 and MMP-9 were determined by using their respective <t>Biotrak</t> Activity Assay Systems. Evo, evodiamine. Data are presented as mean values ± SD of three independent experiments. * p
    Mmp 9 Biotrak Activity Assay System Kits, supplied by R&D Systems, used in various techniques. Bioz Stars score: 84/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare mmp 9 activity assay biotrak system elisa
    MMP Activation and KitL Release Are Impaired in Plg −/− Mice after Myelosuppression, Resulting in BM Recovery Failure (A–D) Plg +/+ and Plg −/− mice were injected with a single dose of 5-FU i.v. (A) BM cells (three mice per time point) were cultured in serum-free medium overnight. Cell supernatants were assayed for proMMP-9 (103 kDa), active <t>MMP-9</t> (86 kDa), proMMP-2 (72 kDa), and active MMP-2 (62 kDa) by gelatin zymography. Error bars represent standard deviation. (B) Immunohistochemistry of BM sections 9 days after 5-FU injection for proMMP-9 with positive staining in the BM stromal compartment of Plg +/+ , but less in the BM stromal compartment of Plg −/− mice. Magnification ×200. (C and D) Plasma obtained from peripheral blood (PB) was assayed for active MMP-9 (C) or KitL (D) by <t>ELISA</t> (p
    Mmp 9 Activity Assay Biotrak System Elisa, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 84/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare mmp 2 biotrak activity assay kit
    Evodiamine inhibits the expression of migration-associated regulators. ( A ) VSMCs were pretreated with evodiamine for 6 h and then stimulated with PDGF-BB for another 24 h. Western blot was used to measure the protein expression levels of regulators involved in the VSMC migration, including matrix metalloproteinase (MMP)-2, <t>MMP-9,</t> intercellular adhesion molecule-1 (ICAM-1), vascular cell adhesion molecule-1 (VCAM-1), and osteopontin (OPN). For both MMP-2 and MMP-9, their latent forms (72 and 92 kDa, respectively) were detected; ( B ) The signal ratio of examined protein to the internal control glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was quantified by densitometric scanning; ( C ) The concentrations of MMP-2 and -9 in the culture medium were detected by Enzyme Linked Immunosorbent Assay (ELISA); ( D ) The activities of MMP-2 and MMP-9 were determined by using their respective <t>Biotrak</t> Activity Assay Systems. Evo, evodiamine. Data are presented as mean values ± SD of three independent experiments. * p
    Mmp 2 Biotrak Activity Assay Kit, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 88/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    GE Healthcare matrix metalloproteinase biotrak activity assay system
    Evodiamine inhibits the expression of migration-associated regulators. ( A ) VSMCs were pretreated with evodiamine for 6 h and then stimulated with PDGF-BB for another 24 h. Western blot was used to measure the protein expression levels of regulators involved in the VSMC migration, including matrix metalloproteinase (MMP)-2, <t>MMP-9,</t> intercellular adhesion molecule-1 (ICAM-1), vascular cell adhesion molecule-1 (VCAM-1), and osteopontin (OPN). For both MMP-2 and MMP-9, their latent forms (72 and 92 kDa, respectively) were detected; ( B ) The signal ratio of examined protein to the internal control glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was quantified by densitometric scanning; ( C ) The concentrations of MMP-2 and -9 in the culture medium were detected by Enzyme Linked Immunosorbent Assay (ELISA); ( D ) The activities of MMP-2 and MMP-9 were determined by using their respective <t>Biotrak</t> Activity Assay Systems. Evo, evodiamine. Data are presented as mean values ± SD of three independent experiments. * p
    Matrix Metalloproteinase Biotrak Activity Assay System, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 85/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    GE Healthcare biotrak
    Evodiamine inhibits the expression of migration-associated regulators. ( A ) VSMCs were pretreated with evodiamine for 6 h and then stimulated with PDGF-BB for another 24 h. Western blot was used to measure the protein expression levels of regulators involved in the VSMC migration, including matrix metalloproteinase (MMP)-2, <t>MMP-9,</t> intercellular adhesion molecule-1 (ICAM-1), vascular cell adhesion molecule-1 (VCAM-1), and osteopontin (OPN). For both MMP-2 and MMP-9, their latent forms (72 and 92 kDa, respectively) were detected; ( B ) The signal ratio of examined protein to the internal control glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was quantified by densitometric scanning; ( C ) The concentrations of MMP-2 and -9 in the culture medium were detected by Enzyme Linked Immunosorbent Assay (ELISA); ( D ) The activities of MMP-2 and MMP-9 were determined by using their respective <t>Biotrak</t> Activity Assay Systems. Evo, evodiamine. Data are presented as mean values ± SD of three independent experiments. * p
    Biotrak, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 93/100, based on 72 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare high sensitivity mmp 2 activity biotrak assay system kit
    Evodiamine inhibits the expression of migration-associated regulators. ( A ) VSMCs were pretreated with evodiamine for 6 h and then stimulated with PDGF-BB for another 24 h. Western blot was used to measure the protein expression levels of regulators involved in the VSMC migration, including matrix metalloproteinase (MMP)-2, <t>MMP-9,</t> intercellular adhesion molecule-1 (ICAM-1), vascular cell adhesion molecule-1 (VCAM-1), and osteopontin (OPN). For both MMP-2 and MMP-9, their latent forms (72 and 92 kDa, respectively) were detected; ( B ) The signal ratio of examined protein to the internal control glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was quantified by densitometric scanning; ( C ) The concentrations of MMP-2 and -9 in the culture medium were detected by Enzyme Linked Immunosorbent Assay (ELISA); ( D ) The activities of MMP-2 and MMP-9 were determined by using their respective <t>Biotrak</t> Activity Assay Systems. Evo, evodiamine. Data are presented as mean values ± SD of three independent experiments. * p
    High Sensitivity Mmp 2 Activity Biotrak Assay System Kit, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 85/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare amersham biotrak
    Evodiamine inhibits the expression of migration-associated regulators. ( A ) VSMCs were pretreated with evodiamine for 6 h and then stimulated with PDGF-BB for another 24 h. Western blot was used to measure the protein expression levels of regulators involved in the VSMC migration, including matrix metalloproteinase (MMP)-2, <t>MMP-9,</t> intercellular adhesion molecule-1 (ICAM-1), vascular cell adhesion molecule-1 (VCAM-1), and osteopontin (OPN). For both MMP-2 and MMP-9, their latent forms (72 and 92 kDa, respectively) were detected; ( B ) The signal ratio of examined protein to the internal control glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was quantified by densitometric scanning; ( C ) The concentrations of MMP-2 and -9 in the culture medium were detected by Enzyme Linked Immunosorbent Assay (ELISA); ( D ) The activities of MMP-2 and MMP-9 were determined by using their respective <t>Biotrak</t> Activity Assay Systems. Evo, evodiamine. Data are presented as mean values ± SD of three independent experiments. * p
    Amersham Biotrak, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 90/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare biotrak cgmp
    Evodiamine inhibits the expression of migration-associated regulators. ( A ) VSMCs were pretreated with evodiamine for 6 h and then stimulated with PDGF-BB for another 24 h. Western blot was used to measure the protein expression levels of regulators involved in the VSMC migration, including matrix metalloproteinase (MMP)-2, <t>MMP-9,</t> intercellular adhesion molecule-1 (ICAM-1), vascular cell adhesion molecule-1 (VCAM-1), and osteopontin (OPN). For both MMP-2 and MMP-9, their latent forms (72 and 92 kDa, respectively) were detected; ( B ) The signal ratio of examined protein to the internal control glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was quantified by densitometric scanning; ( C ) The concentrations of MMP-2 and -9 in the culture medium were detected by Enzyme Linked Immunosorbent Assay (ELISA); ( D ) The activities of MMP-2 and MMP-9 were determined by using their respective <t>Biotrak</t> Activity Assay Systems. Evo, evodiamine. Data are presented as mean values ± SD of three independent experiments. * p
    Biotrak Cgmp, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 85/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    GE Healthcare biotrak assay kit
    Evodiamine inhibits the expression of migration-associated regulators. ( A ) VSMCs were pretreated with evodiamine for 6 h and then stimulated with PDGF-BB for another 24 h. Western blot was used to measure the protein expression levels of regulators involved in the VSMC migration, including matrix metalloproteinase (MMP)-2, <t>MMP-9,</t> intercellular adhesion molecule-1 (ICAM-1), vascular cell adhesion molecule-1 (VCAM-1), and osteopontin (OPN). For both MMP-2 and MMP-9, their latent forms (72 and 92 kDa, respectively) were detected; ( B ) The signal ratio of examined protein to the internal control glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was quantified by densitometric scanning; ( C ) The concentrations of MMP-2 and -9 in the culture medium were detected by Enzyme Linked Immunosorbent Assay (ELISA); ( D ) The activities of MMP-2 and MMP-9 were determined by using their respective <t>Biotrak</t> Activity Assay Systems. Evo, evodiamine. Data are presented as mean values ± SD of three independent experiments. * p
    Biotrak Assay Kit, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 91/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare activity assay kits
    Evodiamine inhibits the expression of migration-associated regulators. ( A ) VSMCs were pretreated with evodiamine for 6 h and then stimulated with PDGF-BB for another 24 h. Western blot was used to measure the protein expression levels of regulators involved in the VSMC migration, including matrix metalloproteinase (MMP)-2, <t>MMP-9,</t> intercellular adhesion molecule-1 (ICAM-1), vascular cell adhesion molecule-1 (VCAM-1), and osteopontin (OPN). For both MMP-2 and MMP-9, their latent forms (72 and 92 kDa, respectively) were detected; ( B ) The signal ratio of examined protein to the internal control glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was quantified by densitometric scanning; ( C ) The concentrations of MMP-2 and -9 in the culture medium were detected by Enzyme Linked Immunosorbent Assay (ELISA); ( D ) The activities of MMP-2 and MMP-9 were determined by using their respective <t>Biotrak</t> Activity Assay Systems. Evo, evodiamine. Data are presented as mean values ± SD of three independent experiments. * p
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    GE Healthcare camp biotrak enzymeimmunoassay system
    AC6mut Design, Expression, Activity and Cellular Distribution. A . The diagram depicts the site of substitution of alanine (ala) for aspartic acid (asp) at position 426 in the C1 domain (intracellular loop) in the construction of AC6mut. The substitution inhibits Mg 2+ binding and alters the efficiency of Gsα-mediated activation of the catalytic core, which impairs the enzymatic activity of AC6, resulting in reduced <t>cAMP</t> production. M1 and M2, transmembrane domains of AC6; C1 and C2, cytoplasmic domains of AC6, which form the catalytic core; βAR, β-adrenergic receptor; βΥ and α, components of the guanosine 5′-triphosphate (GTP)-binding protein, Gs. B . AC6mut mRNA expression was assessed by qRT-PCR using primers common to endogenous AC6 and transgene AC6mut. Primers for detecting GAPDH mRNA were used for internal control of the qRT-PCR reaction. AC6mut mRNA was increased 62-fold vs endogenous AC6. Animal number in bars +SE; Student's t-test, unpaired, 2 tails. C . AC6mut protein was detected in immunoblotting using anti-AC5/6 antibody and confirmed using anti-AU1 tag antibody. AC6mut protein was increased 17-fold vs endogenous AC6. D . Cyclic AMP production in isolated cardiac myocytes from AC6mut and control mice, before (Basal) and after stimulation with isoproterenol (Iso; 10 µM, 10 min) or NKH477 (NKH; 10 µM, 10 min), using cAMP <t>Enzymeimmunoassay.</t> Cardiac myocytes from AC6mut mice (M vs C, control) showed impaired cAMP production in response to Iso and NKH477, a forskolin analog. Bars denote mean +SE; p values from 1-way ANOVA followed by Bonferroni post test (n = 6, each group). E . Double immunofluorescence staining of AC6mut protein in cardiac myocytes isolated from AC6mut vs control mice using anti-AU1 antibody (red); anti-caveolin 3 (Cav-3) antibody (green, for caveolae); anti-protein disulphide-isomerase (PDI) antibody (green, for sarcoplasmic reticulum); and anti-lamin A antibody (green, for nuclear envelope). Nucleus is blue. AC6mut transgene was detected in caveolae, SR, and nuclear envelope.
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    GE Healthcare biotrak eia system
    AC6mut Design, Expression, Activity and Cellular Distribution. A . The diagram depicts the site of substitution of alanine (ala) for aspartic acid (asp) at position 426 in the C1 domain (intracellular loop) in the construction of AC6mut. The substitution inhibits Mg 2+ binding and alters the efficiency of Gsα-mediated activation of the catalytic core, which impairs the enzymatic activity of AC6, resulting in reduced <t>cAMP</t> production. M1 and M2, transmembrane domains of AC6; C1 and C2, cytoplasmic domains of AC6, which form the catalytic core; βAR, β-adrenergic receptor; βΥ and α, components of the guanosine 5′-triphosphate (GTP)-binding protein, Gs. B . AC6mut mRNA expression was assessed by qRT-PCR using primers common to endogenous AC6 and transgene AC6mut. Primers for detecting GAPDH mRNA were used for internal control of the qRT-PCR reaction. AC6mut mRNA was increased 62-fold vs endogenous AC6. Animal number in bars +SE; Student's t-test, unpaired, 2 tails. C . AC6mut protein was detected in immunoblotting using anti-AC5/6 antibody and confirmed using anti-AU1 tag antibody. AC6mut protein was increased 17-fold vs endogenous AC6. D . Cyclic AMP production in isolated cardiac myocytes from AC6mut and control mice, before (Basal) and after stimulation with isoproterenol (Iso; 10 µM, 10 min) or NKH477 (NKH; 10 µM, 10 min), using cAMP <t>Enzymeimmunoassay.</t> Cardiac myocytes from AC6mut mice (M vs C, control) showed impaired cAMP production in response to Iso and NKH477, a forskolin analog. Bars denote mean +SE; p values from 1-way ANOVA followed by Bonferroni post test (n = 6, each group). E . Double immunofluorescence staining of AC6mut protein in cardiac myocytes isolated from AC6mut vs control mice using anti-AU1 antibody (red); anti-caveolin 3 (Cav-3) antibody (green, for caveolae); anti-protein disulphide-isomerase (PDI) antibody (green, for sarcoplasmic reticulum); and anti-lamin A antibody (green, for nuclear envelope). Nucleus is blue. AC6mut transgene was detected in caveolae, SR, and nuclear envelope.
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    GE Healthcare biotrak assay system
    AC6mut Design, Expression, Activity and Cellular Distribution. A . The diagram depicts the site of substitution of alanine (ala) for aspartic acid (asp) at position 426 in the C1 domain (intracellular loop) in the construction of AC6mut. The substitution inhibits Mg 2+ binding and alters the efficiency of Gsα-mediated activation of the catalytic core, which impairs the enzymatic activity of AC6, resulting in reduced <t>cAMP</t> production. M1 and M2, transmembrane domains of AC6; C1 and C2, cytoplasmic domains of AC6, which form the catalytic core; βAR, β-adrenergic receptor; βΥ and α, components of the guanosine 5′-triphosphate (GTP)-binding protein, Gs. B . AC6mut mRNA expression was assessed by qRT-PCR using primers common to endogenous AC6 and transgene AC6mut. Primers for detecting GAPDH mRNA were used for internal control of the qRT-PCR reaction. AC6mut mRNA was increased 62-fold vs endogenous AC6. Animal number in bars +SE; Student's t-test, unpaired, 2 tails. C . AC6mut protein was detected in immunoblotting using anti-AC5/6 antibody and confirmed using anti-AU1 tag antibody. AC6mut protein was increased 17-fold vs endogenous AC6. D . Cyclic AMP production in isolated cardiac myocytes from AC6mut and control mice, before (Basal) and after stimulation with isoproterenol (Iso; 10 µM, 10 min) or NKH477 (NKH; 10 µM, 10 min), using cAMP <t>Enzymeimmunoassay.</t> Cardiac myocytes from AC6mut mice (M vs C, control) showed impaired cAMP production in response to Iso and NKH477, a forskolin analog. Bars denote mean +SE; p values from 1-way ANOVA followed by Bonferroni post test (n = 6, each group). E . Double immunofluorescence staining of AC6mut protein in cardiac myocytes isolated from AC6mut vs control mice using anti-AU1 antibody (red); anti-caveolin 3 (Cav-3) antibody (green, for caveolae); anti-protein disulphide-isomerase (PDI) antibody (green, for sarcoplasmic reticulum); and anti-lamin A antibody (green, for nuclear envelope). Nucleus is blue. AC6mut transgene was detected in caveolae, SR, and nuclear envelope.
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    GE Healthcare biotrak pkc system
    AC6mut Design, Expression, Activity and Cellular Distribution. A . The diagram depicts the site of substitution of alanine (ala) for aspartic acid (asp) at position 426 in the C1 domain (intracellular loop) in the construction of AC6mut. The substitution inhibits Mg 2+ binding and alters the efficiency of Gsα-mediated activation of the catalytic core, which impairs the enzymatic activity of AC6, resulting in reduced <t>cAMP</t> production. M1 and M2, transmembrane domains of AC6; C1 and C2, cytoplasmic domains of AC6, which form the catalytic core; βAR, β-adrenergic receptor; βΥ and α, components of the guanosine 5′-triphosphate (GTP)-binding protein, Gs. B . AC6mut mRNA expression was assessed by qRT-PCR using primers common to endogenous AC6 and transgene AC6mut. Primers for detecting GAPDH mRNA were used for internal control of the qRT-PCR reaction. AC6mut mRNA was increased 62-fold vs endogenous AC6. Animal number in bars +SE; Student's t-test, unpaired, 2 tails. C . AC6mut protein was detected in immunoblotting using anti-AC5/6 antibody and confirmed using anti-AU1 tag antibody. AC6mut protein was increased 17-fold vs endogenous AC6. D . Cyclic AMP production in isolated cardiac myocytes from AC6mut and control mice, before (Basal) and after stimulation with isoproterenol (Iso; 10 µM, 10 min) or NKH477 (NKH; 10 µM, 10 min), using cAMP <t>Enzymeimmunoassay.</t> Cardiac myocytes from AC6mut mice (M vs C, control) showed impaired cAMP production in response to Iso and NKH477, a forskolin analog. Bars denote mean +SE; p values from 1-way ANOVA followed by Bonferroni post test (n = 6, each group). E . Double immunofluorescence staining of AC6mut protein in cardiac myocytes isolated from AC6mut vs control mice using anti-AU1 antibody (red); anti-caveolin 3 (Cav-3) antibody (green, for caveolae); anti-protein disulphide-isomerase (PDI) antibody (green, for sarcoplasmic reticulum); and anti-lamin A antibody (green, for nuclear envelope). Nucleus is blue. AC6mut transgene was detected in caveolae, SR, and nuclear envelope.
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    GE Healthcare biotrak enzymeimmunoassay system
    AC6mut Design, Expression, Activity and Cellular Distribution. A . The diagram depicts the site of substitution of alanine (ala) for aspartic acid (asp) at position 426 in the C1 domain (intracellular loop) in the construction of AC6mut. The substitution inhibits Mg 2+ binding and alters the efficiency of Gsα-mediated activation of the catalytic core, which impairs the enzymatic activity of AC6, resulting in reduced <t>cAMP</t> production. M1 and M2, transmembrane domains of AC6; C1 and C2, cytoplasmic domains of AC6, which form the catalytic core; βAR, β-adrenergic receptor; βΥ and α, components of the guanosine 5′-triphosphate (GTP)-binding protein, Gs. B . AC6mut mRNA expression was assessed by qRT-PCR using primers common to endogenous AC6 and transgene AC6mut. Primers for detecting GAPDH mRNA were used for internal control of the qRT-PCR reaction. AC6mut mRNA was increased 62-fold vs endogenous AC6. Animal number in bars +SE; Student's t-test, unpaired, 2 tails. C . AC6mut protein was detected in immunoblotting using anti-AC5/6 antibody and confirmed using anti-AU1 tag antibody. AC6mut protein was increased 17-fold vs endogenous AC6. D . Cyclic AMP production in isolated cardiac myocytes from AC6mut and control mice, before (Basal) and after stimulation with isoproterenol (Iso; 10 µM, 10 min) or NKH477 (NKH; 10 µM, 10 min), using cAMP <t>Enzymeimmunoassay.</t> Cardiac myocytes from AC6mut mice (M vs C, control) showed impaired cAMP production in response to Iso and NKH477, a forskolin analog. Bars denote mean +SE; p values from 1-way ANOVA followed by Bonferroni post test (n = 6, each group). E . Double immunofluorescence staining of AC6mut protein in cardiac myocytes isolated from AC6mut vs control mice using anti-AU1 antibody (red); anti-caveolin 3 (Cav-3) antibody (green, for caveolae); anti-protein disulphide-isomerase (PDI) antibody (green, for sarcoplasmic reticulum); and anti-lamin A antibody (green, for nuclear envelope). Nucleus is blue. AC6mut transgene was detected in caveolae, SR, and nuclear envelope.
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    GE Healthcare biotrak mmp 2
    AC6mut Design, Expression, Activity and Cellular Distribution. A . The diagram depicts the site of substitution of alanine (ala) for aspartic acid (asp) at position 426 in the C1 domain (intracellular loop) in the construction of AC6mut. The substitution inhibits Mg 2+ binding and alters the efficiency of Gsα-mediated activation of the catalytic core, which impairs the enzymatic activity of AC6, resulting in reduced <t>cAMP</t> production. M1 and M2, transmembrane domains of AC6; C1 and C2, cytoplasmic domains of AC6, which form the catalytic core; βAR, β-adrenergic receptor; βΥ and α, components of the guanosine 5′-triphosphate (GTP)-binding protein, Gs. B . AC6mut mRNA expression was assessed by qRT-PCR using primers common to endogenous AC6 and transgene AC6mut. Primers for detecting GAPDH mRNA were used for internal control of the qRT-PCR reaction. AC6mut mRNA was increased 62-fold vs endogenous AC6. Animal number in bars +SE; Student's t-test, unpaired, 2 tails. C . AC6mut protein was detected in immunoblotting using anti-AC5/6 antibody and confirmed using anti-AU1 tag antibody. AC6mut protein was increased 17-fold vs endogenous AC6. D . Cyclic AMP production in isolated cardiac myocytes from AC6mut and control mice, before (Basal) and after stimulation with isoproterenol (Iso; 10 µM, 10 min) or NKH477 (NKH; 10 µM, 10 min), using cAMP <t>Enzymeimmunoassay.</t> Cardiac myocytes from AC6mut mice (M vs C, control) showed impaired cAMP production in response to Iso and NKH477, a forskolin analog. Bars denote mean +SE; p values from 1-way ANOVA followed by Bonferroni post test (n = 6, each group). E . Double immunofluorescence staining of AC6mut protein in cardiac myocytes isolated from AC6mut vs control mice using anti-AU1 antibody (red); anti-caveolin 3 (Cav-3) antibody (green, for caveolae); anti-protein disulphide-isomerase (PDI) antibody (green, for sarcoplasmic reticulum); and anti-lamin A antibody (green, for nuclear envelope). Nucleus is blue. AC6mut transgene was detected in caveolae, SR, and nuclear envelope.
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    GE Healthcare mmp9 activity
    S1943 NMHC-IIA phosphorylation regulates <t>MMP9</t> secretion. (A) Gelatin zymography of conditioned medium from MDA-MB-231 cells expressing wild-type, S1943A or S1943E NMHC-IIA. Standards are human proMMP9 and active MMP2. (B and C) Biotrak MMP9 activity assay of (B) total MMP9 and (C) active MMP9 in conditioned medium from MDA-MB-231 cells expressing wild-type, S1943A or S1943E NMHC-IIA. Data represent the mean ± SEM from 3 independent experiments. Statistical analyses were performed using ANOVA.
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    GE Healthcare camp biotrak competitive enzyme immunoassay
    S1943 NMHC-IIA phosphorylation regulates <t>MMP9</t> secretion. (A) Gelatin zymography of conditioned medium from MDA-MB-231 cells expressing wild-type, S1943A or S1943E NMHC-IIA. Standards are human proMMP9 and active MMP2. (B and C) Biotrak MMP9 activity assay of (B) total MMP9 and (C) active MMP9 in conditioned medium from MDA-MB-231 cells expressing wild-type, S1943A or S1943E NMHC-IIA. Data represent the mean ± SEM from 3 independent experiments. Statistical analyses were performed using ANOVA.
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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

    Evodiamine inhibits the expression of migration-associated regulators. ( A ) VSMCs were pretreated with evodiamine for 6 h and then stimulated with PDGF-BB for another 24 h. Western blot was used to measure the protein expression levels of regulators involved in the VSMC migration, including matrix metalloproteinase (MMP)-2, MMP-9, intercellular adhesion molecule-1 (ICAM-1), vascular cell adhesion molecule-1 (VCAM-1), and osteopontin (OPN). For both MMP-2 and MMP-9, their latent forms (72 and 92 kDa, respectively) were detected; ( B ) The signal ratio of examined protein to the internal control glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was quantified by densitometric scanning; ( C ) The concentrations of MMP-2 and -9 in the culture medium were detected by Enzyme Linked Immunosorbent Assay (ELISA); ( D ) The activities of MMP-2 and MMP-9 were determined by using their respective Biotrak Activity Assay Systems. Evo, evodiamine. Data are presented as mean values ± SD of three independent experiments. * p

    Journal: International Journal of Molecular Sciences

    Article Title: Evodiamine Attenuates PDGF-BB-Induced Migration of Rat Vascular Smooth Muscle Cells through Activating PPARγ

    doi: 10.3390/ijms161226093

    Figure Lengend Snippet: Evodiamine inhibits the expression of migration-associated regulators. ( A ) VSMCs were pretreated with evodiamine for 6 h and then stimulated with PDGF-BB for another 24 h. Western blot was used to measure the protein expression levels of regulators involved in the VSMC migration, including matrix metalloproteinase (MMP)-2, MMP-9, intercellular adhesion molecule-1 (ICAM-1), vascular cell adhesion molecule-1 (VCAM-1), and osteopontin (OPN). For both MMP-2 and MMP-9, their latent forms (72 and 92 kDa, respectively) were detected; ( B ) The signal ratio of examined protein to the internal control glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was quantified by densitometric scanning; ( C ) The concentrations of MMP-2 and -9 in the culture medium were detected by Enzyme Linked Immunosorbent Assay (ELISA); ( D ) The activities of MMP-2 and MMP-9 were determined by using their respective Biotrak Activity Assay Systems. Evo, evodiamine. Data are presented as mean values ± SD of three independent experiments. * p

    Article Snippet: Matrix Metalloproteinase (MMP)-2 and MMP-9 Activity Assays The culture supernatants of VSMCs were collected by centrifuging at 1000× g for 20 min, and concentrated 10× using Centriprep 10,000 MWCO tubes (Millipore) by centrifuging at 4900 rpm for 30 min.

    Techniques: Expressing, Migration, Western Blot, Enzyme-linked Immunosorbent Assay, MMP-2 Human Biotrak Assay

    Metalloprotease activity is inhibited by Dox-treated melanoma cells grown on different substrates. (A) Zymography assay of human melanoma cell lines SK-Mel-19, SK-Mel-103, and SK-Mel-147 treated with 1.2 μM of Dox (IC 50 ) or NT. (B) Gelatinolytic activity of MMP-2 and -9 in human melanoma cell line SK-Mel-103 (C) Inhibition of MMP-2 activity of by Biotrak ® assay in human melanoma cell line SK-Mel-103, whose culture medium was incubated with a fluorescent substrate. Treatment conditions were melanoma cells seeded on plastic, in monolayer (M); on type I collagen (M+Col); on dermal equivalent (M+Eq); and the dermal equivalent control with no melanoma cells (Eq). *** p

    Journal: Tissue Engineering. Part A

    Article Title: Fibroblasts Protect Melanoma Cells from the Cytotoxic Effects of Doxorubicin

    doi: 10.1089/ten.tea.2013.0473

    Figure Lengend Snippet: Metalloprotease activity is inhibited by Dox-treated melanoma cells grown on different substrates. (A) Zymography assay of human melanoma cell lines SK-Mel-19, SK-Mel-103, and SK-Mel-147 treated with 1.2 μM of Dox (IC 50 ) or NT. (B) Gelatinolytic activity of MMP-2 and -9 in human melanoma cell line SK-Mel-103 (C) Inhibition of MMP-2 activity of by Biotrak ® assay in human melanoma cell line SK-Mel-103, whose culture medium was incubated with a fluorescent substrate. Treatment conditions were melanoma cells seeded on plastic, in monolayer (M); on type I collagen (M+Col); on dermal equivalent (M+Eq); and the dermal equivalent control with no melanoma cells (Eq). *** p

    Article Snippet: Protein concentration was determined by the Folin method and the supernatant used to perform the MMP-2 activity assay using a standard colorimetric kit, Biotrak MMP-2 Activity (Amersham, GE Healthcare Biosciences, Pittsburgh, PA), which provides a colorimetric quantitative determination of pro- and active- enzyme after incubation with a fluorescent substrate.

    Techniques: Activity Assay, Zymography, Inhibition, MMP-2 Human Biotrak Assay, Incubation

    Expression of MMP-2 and -9 activities (ng/mL) obtained with the Biotrak™ activity assay system. ( A ) Comparison of enzyme activity in the etch-and-rinse group. Bar 1 , control mineralized dentin powder (G1 - MD); Bar 2 , dentin powder etched with

    Journal: Journal of Dental Research

    Article Title: Effects of Etch-and-Rinse and Self-etch Adhesives on Dentin MMP-2 and MMP-9

    doi: 10.1177/0022034512467034

    Figure Lengend Snippet: Expression of MMP-2 and -9 activities (ng/mL) obtained with the Biotrak™ activity assay system. ( A ) Comparison of enzyme activity in the etch-and-rinse group. Bar 1 , control mineralized dentin powder (G1 - MD); Bar 2 , dentin powder etched with

    Article Snippet: The enzymatic activities of MMP-2 and -9 were determined with the Biotrak™ activity assay system (GE Healthcare, Buckinghamshire, UK).

    Techniques: Expressing, MMP-2 Human Biotrak Assay, Activity Assay

    S1943 NMHC-IIA phosphorylation regulates MMP9 secretion. (A) Gelatin zymography of conditioned medium from MDA-MB-231 cells expressing wild-type, S1943A or S1943E NMHC-IIA. Standards are human proMMP9 and active MMP2. (B and C) Biotrak MMP9 activity assay of (B) total MMP9 and (C) active MMP9 in conditioned medium from MDA-MB-231 cells expressing wild-type, S1943A or S1943E NMHC-IIA. Data represent the mean ± SEM from 3 independent experiments. Statistical analyses were performed using ANOVA.

    Journal: Experimental cell research

    Article Title: Myosin-IIA heavy chain phosphorylation on SI943 regulates tumor metastasis

    doi: 10.1016/j.yexcr.2018.06.028

    Figure Lengend Snippet: S1943 NMHC-IIA phosphorylation regulates MMP9 secretion. (A) Gelatin zymography of conditioned medium from MDA-MB-231 cells expressing wild-type, S1943A or S1943E NMHC-IIA. Standards are human proMMP9 and active MMP2. (B and C) Biotrak MMP9 activity assay of (B) total MMP9 and (C) active MMP9 in conditioned medium from MDA-MB-231 cells expressing wild-type, S1943A or S1943E NMHC-IIA. Data represent the mean ± SEM from 3 independent experiments. Statistical analyses were performed using ANOVA.

    Article Snippet: MMP9 activity in conditioned media collected from MDA-MB-231 cells (as described above) was determined using the MMP9 Biotrak Activity Assay (GE Healthcare Life Sciences) following the manufacturers protocol.

    Techniques: Zymography, Multiple Displacement Amplification, Expressing, Activity Assay

    Finasteride’s effects on MMP2 and MMP9 activity and TIMP-1 and TIMP-2 expression in the conditioned medium of RWPE-1 cells. a) Conditioned medium of untreated (Control) and finasteride-treated RWPE-1 cells were collected, concentrated and analyzed for MMP2 and MMP9 activities using their respective Biotrak® Activity Assays. Low-dose finasteride (10 µM) for 72 hours of exposure downregulated MMP2 and MMP9 activity by 25% and 30%, respectively, when compared to control values. High-dose finasteride (50 µM) downregulated MMP2 and MMP9 activities at all tested time points, up to 90% and 55% after 72 hours of exposure, respectively. b) Conditioned medium of untreated (Control) and finasteride-treated RWPE-1 cells were collected, concentrated and analyzed for TIMP-1 and TIMP-2 protein expression using their respective Biotrak® Assays. Finasteride exposure, at both doses, induced the upregulation of TIMP-2 expression at the 72 hour time point, up to 150% more expression than control levels. Data are expressed as a fold-change graphic of the IOD values that were obtained for finasteride-treated cells over those of the control cells. (*) Statistically significant values with p

    Journal: PLoS ONE

    Article Title: Finasteride Inhibits Human Prostate Cancer Cell Invasion through MMP2 and MMP9 Downregulation

    doi: 10.1371/journal.pone.0084757

    Figure Lengend Snippet: Finasteride’s effects on MMP2 and MMP9 activity and TIMP-1 and TIMP-2 expression in the conditioned medium of RWPE-1 cells. a) Conditioned medium of untreated (Control) and finasteride-treated RWPE-1 cells were collected, concentrated and analyzed for MMP2 and MMP9 activities using their respective Biotrak® Activity Assays. Low-dose finasteride (10 µM) for 72 hours of exposure downregulated MMP2 and MMP9 activity by 25% and 30%, respectively, when compared to control values. High-dose finasteride (50 µM) downregulated MMP2 and MMP9 activities at all tested time points, up to 90% and 55% after 72 hours of exposure, respectively. b) Conditioned medium of untreated (Control) and finasteride-treated RWPE-1 cells were collected, concentrated and analyzed for TIMP-1 and TIMP-2 protein expression using their respective Biotrak® Assays. Finasteride exposure, at both doses, induced the upregulation of TIMP-2 expression at the 72 hour time point, up to 150% more expression than control levels. Data are expressed as a fold-change graphic of the IOD values that were obtained for finasteride-treated cells over those of the control cells. (*) Statistically significant values with p

    Article Snippet: MMP2 and MMP9 Activity Assays The total (pro-form+active form) MMP2 and MMP9 activities in the CM and cell extracts were measured using the Biotrak® Activity Assays (GE Healthcare LifeSciences™) according to the manufacturer’s guidelines.

    Techniques: Activity Assay, Expressing

    Finasteride’s effects on MMP2 and MMP9 activity and TIMP-1 and TIMP-2 expression in the conditioned medium of PC3 cells. a) Conditioned medium of untreated and finasteride-treated PC3 cells was collected, concentrated and analyzed for MMP2 and MMP9 activities using their respective Biotrak® Activity Assays. Low-dose finasteride exposure (10 µM) did not induce the downregulation of MMP2 or MMP9 activities, except at the 24 hour time point. High-dose finasteride induced the downregulation of MMP2 at the 48 hour and 72 hour time points and of MMP9 at all assessed time points, up to 70% reduction. b) Conditioned medium of untreated (Control) and finasteride-treated PC3 cells was collected, concentrated and analyzed for TIMP-1 and TIMP-2 protein expression using their respective Biotrak® Assays. Finasteride exposure did not induce any significant modulation of TIMP-1 and TIMP-2 expression, except for the 10 µM finasteride dose at 24 hours of exposure. Data are expressed as a fold-change of the IOD values obtained for finasteride treated cells over control cells. (*) Statistically significant values with p

    Journal: PLoS ONE

    Article Title: Finasteride Inhibits Human Prostate Cancer Cell Invasion through MMP2 and MMP9 Downregulation

    doi: 10.1371/journal.pone.0084757

    Figure Lengend Snippet: Finasteride’s effects on MMP2 and MMP9 activity and TIMP-1 and TIMP-2 expression in the conditioned medium of PC3 cells. a) Conditioned medium of untreated and finasteride-treated PC3 cells was collected, concentrated and analyzed for MMP2 and MMP9 activities using their respective Biotrak® Activity Assays. Low-dose finasteride exposure (10 µM) did not induce the downregulation of MMP2 or MMP9 activities, except at the 24 hour time point. High-dose finasteride induced the downregulation of MMP2 at the 48 hour and 72 hour time points and of MMP9 at all assessed time points, up to 70% reduction. b) Conditioned medium of untreated (Control) and finasteride-treated PC3 cells was collected, concentrated and analyzed for TIMP-1 and TIMP-2 protein expression using their respective Biotrak® Assays. Finasteride exposure did not induce any significant modulation of TIMP-1 and TIMP-2 expression, except for the 10 µM finasteride dose at 24 hours of exposure. Data are expressed as a fold-change of the IOD values obtained for finasteride treated cells over control cells. (*) Statistically significant values with p

    Article Snippet: MMP2 and MMP9 Activity Assays The total (pro-form+active form) MMP2 and MMP9 activities in the CM and cell extracts were measured using the Biotrak® Activity Assays (GE Healthcare LifeSciences™) according to the manufacturer’s guidelines.

    Techniques: Activity Assay, Expressing

    Up-regulated MMP-9 is not uniquely responsible for CD73 shedding. LPS and TNF-α, individually or in combination, on regulating MMP-9 expression extracellular activity were detected by qPCR ( a ) and a MMP-9 Biotrak activity assay ( b ). Effect of exogenous MMP-9 on CD73 shedding in Mmp9 −/− RPE cells received LPS/TNF-α treatment or not ( c ). a qPCR results of Mmp-9 expression in RPE cells ( n = 6). b Amount of active MMP-9 in the medium of RPE cells. c Effect of exogenous recombinant MMP-9 on regulating CD73 shedding; a representative flow cytometry result (left column) and statistical analysis of FACS determined percentage of CD73 positive cells (right column)

    Journal: Purinergic Signalling

    Article Title: Multiple steps determine CD73 shedding from RPE: lipid raft localization, ARA1 interaction, and MMP-9 up-regulation

    doi: 10.1007/s11302-018-9628-1

    Figure Lengend Snippet: Up-regulated MMP-9 is not uniquely responsible for CD73 shedding. LPS and TNF-α, individually or in combination, on regulating MMP-9 expression extracellular activity were detected by qPCR ( a ) and a MMP-9 Biotrak activity assay ( b ). Effect of exogenous MMP-9 on CD73 shedding in Mmp9 −/− RPE cells received LPS/TNF-α treatment or not ( c ). a qPCR results of Mmp-9 expression in RPE cells ( n = 6). b Amount of active MMP-9 in the medium of RPE cells. c Effect of exogenous recombinant MMP-9 on regulating CD73 shedding; a representative flow cytometry result (left column) and statistical analysis of FACS determined percentage of CD73 positive cells (right column)

    Article Snippet: The activity of secreted MMP-9 in the medium was evaluated by a MMP-9 Biotrak activity system (GE Healthcare, RPN2634) following manufacture’s protocol.

    Techniques: Expressing, Activity Assay, Real-time Polymerase Chain Reaction, MMP-2 Human Biotrak Assay, Recombinant, Flow Cytometry, Cytometry, FACS

    Lipid raft localization is necessary for CD73 shedding. Cell membrane extract was primarily isolated from differently treated RPE cells, further separated into lipid raft and non-lipid raft fractions by either detergent free ( a ) or detergent resistant methods ( b ). All the fractions were western blotting for CAV-1 as the marker of lipid rafts fractions and Na + /K + ATPase as the marker of non-lipid fractions. The effect of mevastatinon CD73 shedding ( c ), CD73 lipid rafts localization ( e ) and ARA1 co-IP ( f ) were evaluated by western blotting. The amount of active MMP-9 in the medium was detected (D). a The existence of CD73 and ARA1 in lipid raft and non-lipid raft fractions, determined by western blotting. b The co-existence of CD73 and ARA1 in lipid raft fractions prepared by detergent resistant methods. c Localization of ARA1 in Cd73 −/− RPE, with or without Wt-CD73 modification. d The effect of mevastatin on CD73 shedding was determined by western blotting (upper panel). Active MMP-9 in the medium was determined by MMP-9 Biotrak activity assay (lower panel, n = 6). e The effect of mevastatin on CD73 localization, determined by western blotting. f The effect of mevastatin on the Co-IP of CD73 and ARA1

    Journal: Purinergic Signalling

    Article Title: Multiple steps determine CD73 shedding from RPE: lipid raft localization, ARA1 interaction, and MMP-9 up-regulation

    doi: 10.1007/s11302-018-9628-1

    Figure Lengend Snippet: Lipid raft localization is necessary for CD73 shedding. Cell membrane extract was primarily isolated from differently treated RPE cells, further separated into lipid raft and non-lipid raft fractions by either detergent free ( a ) or detergent resistant methods ( b ). All the fractions were western blotting for CAV-1 as the marker of lipid rafts fractions and Na + /K + ATPase as the marker of non-lipid fractions. The effect of mevastatinon CD73 shedding ( c ), CD73 lipid rafts localization ( e ) and ARA1 co-IP ( f ) were evaluated by western blotting. The amount of active MMP-9 in the medium was detected (D). a The existence of CD73 and ARA1 in lipid raft and non-lipid raft fractions, determined by western blotting. b The co-existence of CD73 and ARA1 in lipid raft fractions prepared by detergent resistant methods. c Localization of ARA1 in Cd73 −/− RPE, with or without Wt-CD73 modification. d The effect of mevastatin on CD73 shedding was determined by western blotting (upper panel). Active MMP-9 in the medium was determined by MMP-9 Biotrak activity assay (lower panel, n = 6). e The effect of mevastatin on CD73 localization, determined by western blotting. f The effect of mevastatin on the Co-IP of CD73 and ARA1

    Article Snippet: The activity of secreted MMP-9 in the medium was evaluated by a MMP-9 Biotrak activity system (GE Healthcare, RPN2634) following manufacture’s protocol.

    Techniques: Isolation, Western Blot, Marker, Co-Immunoprecipitation Assay, Modification, MMP-2 Human Biotrak Assay

    Effects of rosiglitazone on the expression of MMP2 and MMP9 in Cs-induced emphysema in rats. Notes: Effects of rosiglitazone on the expression of MMP2 and MMP9 in CS-induced emphysema in rats as measured by Western blotting ( A ). The target protein bands were desitometrically analyzed normalized to β-actin ( B ). The activities of MMP2 ( C ) and MMP9 ( D ) in each group were determined by using MMP2 and MMP9 Biotrak™ activity assay. The expression of MMP2 and MMP9 was confirmed by using immunohistochemistry for each group (magnification ×400) ( E ). The values presented are the mean ± SD. * P

    Journal: International Journal of Chronic Obstructive Pulmonary Disease

    Article Title: Rosiglitazone attenuates the metalloprotease/anti-metalloprotease imbalance in emphysema induced by cigarette smoke: involvement of extracellular signal-regulated kinase and NFκB signaling

    doi: 10.2147/COPD.S77514

    Figure Lengend Snippet: Effects of rosiglitazone on the expression of MMP2 and MMP9 in Cs-induced emphysema in rats. Notes: Effects of rosiglitazone on the expression of MMP2 and MMP9 in CS-induced emphysema in rats as measured by Western blotting ( A ). The target protein bands were desitometrically analyzed normalized to β-actin ( B ). The activities of MMP2 ( C ) and MMP9 ( D ) in each group were determined by using MMP2 and MMP9 Biotrak™ activity assay. The expression of MMP2 and MMP9 was confirmed by using immunohistochemistry for each group (magnification ×400) ( E ). The values presented are the mean ± SD. * P

    Article Snippet: Determination of MMP2 and MMP9 activity in lung tissues The resected lung tissues of each group were homogenized and the activity of MMP2 and MMP9 was quantitatively determined using MMP2 and MMP9 Biotrak™ activity assay kit (GE Healthcare Bio-Sciences Corp., Piscataway, NJ, USA).

    Techniques: Expressing, Western Blot, MMP-2 Human Biotrak Assay, Immunohistochemistry

    Evodiamine inhibits the expression of migration-associated regulators. ( A ) VSMCs were pretreated with evodiamine for 6 h and then stimulated with PDGF-BB for another 24 h. Western blot was used to measure the protein expression levels of regulators involved in the VSMC migration, including matrix metalloproteinase (MMP)-2, MMP-9, intercellular adhesion molecule-1 (ICAM-1), vascular cell adhesion molecule-1 (VCAM-1), and osteopontin (OPN). For both MMP-2 and MMP-9, their latent forms (72 and 92 kDa, respectively) were detected; ( B ) The signal ratio of examined protein to the internal control glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was quantified by densitometric scanning; ( C ) The concentrations of MMP-2 and -9 in the culture medium were detected by Enzyme Linked Immunosorbent Assay (ELISA); ( D ) The activities of MMP-2 and MMP-9 were determined by using their respective Biotrak Activity Assay Systems. Evo, evodiamine. Data are presented as mean values ± SD of three independent experiments. * p

    Journal: International Journal of Molecular Sciences

    Article Title: Evodiamine Attenuates PDGF-BB-Induced Migration of Rat Vascular Smooth Muscle Cells through Activating PPARγ

    doi: 10.3390/ijms161226093

    Figure Lengend Snippet: Evodiamine inhibits the expression of migration-associated regulators. ( A ) VSMCs were pretreated with evodiamine for 6 h and then stimulated with PDGF-BB for another 24 h. Western blot was used to measure the protein expression levels of regulators involved in the VSMC migration, including matrix metalloproteinase (MMP)-2, MMP-9, intercellular adhesion molecule-1 (ICAM-1), vascular cell adhesion molecule-1 (VCAM-1), and osteopontin (OPN). For both MMP-2 and MMP-9, their latent forms (72 and 92 kDa, respectively) were detected; ( B ) The signal ratio of examined protein to the internal control glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was quantified by densitometric scanning; ( C ) The concentrations of MMP-2 and -9 in the culture medium were detected by Enzyme Linked Immunosorbent Assay (ELISA); ( D ) The activities of MMP-2 and MMP-9 were determined by using their respective Biotrak Activity Assay Systems. Evo, evodiamine. Data are presented as mean values ± SD of three independent experiments. * p

    Article Snippet: We also used Biotrak Activity Assay Kits (GE Healthcare) to quantify actual enzymatic activities of MMP-2 and MMP-9 in their active form and our results indicated that evodiamine indeed suppressed PDGF-BB-induced upregulation in their activities ( D).

    Techniques: Expressing, Migration, Western Blot, Enzyme-linked Immunosorbent Assay, MMP-2 Human Biotrak Assay

    MMP Activation and KitL Release Are Impaired in Plg −/− Mice after Myelosuppression, Resulting in BM Recovery Failure (A–D) Plg +/+ and Plg −/− mice were injected with a single dose of 5-FU i.v. (A) BM cells (three mice per time point) were cultured in serum-free medium overnight. Cell supernatants were assayed for proMMP-9 (103 kDa), active MMP-9 (86 kDa), proMMP-2 (72 kDa), and active MMP-2 (62 kDa) by gelatin zymography. Error bars represent standard deviation. (B) Immunohistochemistry of BM sections 9 days after 5-FU injection for proMMP-9 with positive staining in the BM stromal compartment of Plg +/+ , but less in the BM stromal compartment of Plg −/− mice. Magnification ×200. (C and D) Plasma obtained from peripheral blood (PB) was assayed for active MMP-9 (C) or KitL (D) by ELISA (p

    Journal: Cell stem cell

    Article Title: The Plasminogen Fibrinolytic Pathway Is Required for Hematopoietic Regeneration

    doi: 10.1016/j.stem.2007.10.012

    Figure Lengend Snippet: MMP Activation and KitL Release Are Impaired in Plg −/− Mice after Myelosuppression, Resulting in BM Recovery Failure (A–D) Plg +/+ and Plg −/− mice were injected with a single dose of 5-FU i.v. (A) BM cells (three mice per time point) were cultured in serum-free medium overnight. Cell supernatants were assayed for proMMP-9 (103 kDa), active MMP-9 (86 kDa), proMMP-2 (72 kDa), and active MMP-2 (62 kDa) by gelatin zymography. Error bars represent standard deviation. (B) Immunohistochemistry of BM sections 9 days after 5-FU injection for proMMP-9 with positive staining in the BM stromal compartment of Plg +/+ , but less in the BM stromal compartment of Plg −/− mice. Magnification ×200. (C and D) Plasma obtained from peripheral blood (PB) was assayed for active MMP-9 (C) or KitL (D) by ELISA (p

    Article Snippet: Active MMP-9 was analyzed using the MMP-9 Activity Assay Biotrak System ELISA (Amersham Biosciences, UK).

    Techniques: Activation Assay, Mouse Assay, Injection, Cell Culture, Zymography, Standard Deviation, Immunohistochemistry, Staining, Enzyme-linked Immunosorbent Assay

    tPA-Mediated MMP Activation Releases KitL from Stromal Cells (A) RT-PCR for tPA and Plg in liver (sample 1; positive control for Plg), 4-week-old BM stroma of Plg +/+ mice (sample 2) and of Plg −/− mice (sample 3), MS-5 cells (sample 4), freshly isolated BM-derived lin− cells from Plg +/+ mice (sample 5), or Plg −/− mice (sample 6), as well as freshly isolated BM-derived lin+ cells from Plg +/+ mice (sample 7) or Plg −/− mice (sample 8). Agarose gel of one representative experiment. (B) Immunohistochemistry for tPA in BM sections of Plg +/+ mice under steady-state conditions (magnification ×200). (Insert) Vessel stained positive for tPA. (C–F) MS-5 cells (C) or lin+ BMMCs from Plg +/+ mice (D) were cultured overnight with/without tPA under serum-free conditions. Supernatants were analyzed by zymography for MMP-2 and MMP-9. Error bars represent standard deviation. Immunohistochemistry for Plg (E) and MMP-9 (F) in BM sections of Plg +/+ mice 3 days after starting tPA treatment (magnification ×200). (G and H) Confluent MS-5 stromal cells (G) or Plg +/+ primary BM stroma cells (H) were cultured overnight in serum-free medium (n = 3) in the presence of recombinant tPA, recombinant PAI-1, and MPI (CGS 27023A) with or without tPA. Supernatants were collected and analyzed for KitL by ELISA (n = 3, p

    Journal: Cell stem cell

    Article Title: The Plasminogen Fibrinolytic Pathway Is Required for Hematopoietic Regeneration

    doi: 10.1016/j.stem.2007.10.012

    Figure Lengend Snippet: tPA-Mediated MMP Activation Releases KitL from Stromal Cells (A) RT-PCR for tPA and Plg in liver (sample 1; positive control for Plg), 4-week-old BM stroma of Plg +/+ mice (sample 2) and of Plg −/− mice (sample 3), MS-5 cells (sample 4), freshly isolated BM-derived lin− cells from Plg +/+ mice (sample 5), or Plg −/− mice (sample 6), as well as freshly isolated BM-derived lin+ cells from Plg +/+ mice (sample 7) or Plg −/− mice (sample 8). Agarose gel of one representative experiment. (B) Immunohistochemistry for tPA in BM sections of Plg +/+ mice under steady-state conditions (magnification ×200). (Insert) Vessel stained positive for tPA. (C–F) MS-5 cells (C) or lin+ BMMCs from Plg +/+ mice (D) were cultured overnight with/without tPA under serum-free conditions. Supernatants were analyzed by zymography for MMP-2 and MMP-9. Error bars represent standard deviation. Immunohistochemistry for Plg (E) and MMP-9 (F) in BM sections of Plg +/+ mice 3 days after starting tPA treatment (magnification ×200). (G and H) Confluent MS-5 stromal cells (G) or Plg +/+ primary BM stroma cells (H) were cultured overnight in serum-free medium (n = 3) in the presence of recombinant tPA, recombinant PAI-1, and MPI (CGS 27023A) with or without tPA. Supernatants were collected and analyzed for KitL by ELISA (n = 3, p

    Article Snippet: Active MMP-9 was analyzed using the MMP-9 Activity Assay Biotrak System ELISA (Amersham Biosciences, UK).

    Techniques: Activation Assay, Reverse Transcription Polymerase Chain Reaction, Positive Control, Mouse Assay, Mass Spectrometry, Isolation, Derivative Assay, Agarose Gel Electrophoresis, Immunohistochemistry, Staining, Cell Culture, Zymography, Standard Deviation, Recombinant, Enzyme-linked Immunosorbent Assay

    Evodiamine inhibits the expression of migration-associated regulators. ( A ) VSMCs were pretreated with evodiamine for 6 h and then stimulated with PDGF-BB for another 24 h. Western blot was used to measure the protein expression levels of regulators involved in the VSMC migration, including matrix metalloproteinase (MMP)-2, MMP-9, intercellular adhesion molecule-1 (ICAM-1), vascular cell adhesion molecule-1 (VCAM-1), and osteopontin (OPN). For both MMP-2 and MMP-9, their latent forms (72 and 92 kDa, respectively) were detected; ( B ) The signal ratio of examined protein to the internal control glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was quantified by densitometric scanning; ( C ) The concentrations of MMP-2 and -9 in the culture medium were detected by Enzyme Linked Immunosorbent Assay (ELISA); ( D ) The activities of MMP-2 and MMP-9 were determined by using their respective Biotrak Activity Assay Systems. Evo, evodiamine. Data are presented as mean values ± SD of three independent experiments. * p

    Journal: International Journal of Molecular Sciences

    Article Title: Evodiamine Attenuates PDGF-BB-Induced Migration of Rat Vascular Smooth Muscle Cells through Activating PPARγ

    doi: 10.3390/ijms161226093

    Figure Lengend Snippet: Evodiamine inhibits the expression of migration-associated regulators. ( A ) VSMCs were pretreated with evodiamine for 6 h and then stimulated with PDGF-BB for another 24 h. Western blot was used to measure the protein expression levels of regulators involved in the VSMC migration, including matrix metalloproteinase (MMP)-2, MMP-9, intercellular adhesion molecule-1 (ICAM-1), vascular cell adhesion molecule-1 (VCAM-1), and osteopontin (OPN). For both MMP-2 and MMP-9, their latent forms (72 and 92 kDa, respectively) were detected; ( B ) The signal ratio of examined protein to the internal control glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was quantified by densitometric scanning; ( C ) The concentrations of MMP-2 and -9 in the culture medium were detected by Enzyme Linked Immunosorbent Assay (ELISA); ( D ) The activities of MMP-2 and MMP-9 were determined by using their respective Biotrak Activity Assay Systems. Evo, evodiamine. Data are presented as mean values ± SD of three independent experiments. * p

    Article Snippet: The levels of active MMP-2 and MMP-9 were measured by using MMP-2 and MMP-9 Biotrak Activity Assay Kits (Cat. No. RPN2631, and RPN2634, GE Healthcare, Piscataway, NJ, USA) according to the manufacturer’s protocol.

    Techniques: Expressing, Migration, Western Blot, Enzyme-linked Immunosorbent Assay, MMP-2 Human Biotrak Assay

    AC6mut Design, Expression, Activity and Cellular Distribution. A . The diagram depicts the site of substitution of alanine (ala) for aspartic acid (asp) at position 426 in the C1 domain (intracellular loop) in the construction of AC6mut. The substitution inhibits Mg 2+ binding and alters the efficiency of Gsα-mediated activation of the catalytic core, which impairs the enzymatic activity of AC6, resulting in reduced cAMP production. M1 and M2, transmembrane domains of AC6; C1 and C2, cytoplasmic domains of AC6, which form the catalytic core; βAR, β-adrenergic receptor; βΥ and α, components of the guanosine 5′-triphosphate (GTP)-binding protein, Gs. B . AC6mut mRNA expression was assessed by qRT-PCR using primers common to endogenous AC6 and transgene AC6mut. Primers for detecting GAPDH mRNA were used for internal control of the qRT-PCR reaction. AC6mut mRNA was increased 62-fold vs endogenous AC6. Animal number in bars +SE; Student's t-test, unpaired, 2 tails. C . AC6mut protein was detected in immunoblotting using anti-AC5/6 antibody and confirmed using anti-AU1 tag antibody. AC6mut protein was increased 17-fold vs endogenous AC6. D . Cyclic AMP production in isolated cardiac myocytes from AC6mut and control mice, before (Basal) and after stimulation with isoproterenol (Iso; 10 µM, 10 min) or NKH477 (NKH; 10 µM, 10 min), using cAMP Enzymeimmunoassay. Cardiac myocytes from AC6mut mice (M vs C, control) showed impaired cAMP production in response to Iso and NKH477, a forskolin analog. Bars denote mean +SE; p values from 1-way ANOVA followed by Bonferroni post test (n = 6, each group). E . Double immunofluorescence staining of AC6mut protein in cardiac myocytes isolated from AC6mut vs control mice using anti-AU1 antibody (red); anti-caveolin 3 (Cav-3) antibody (green, for caveolae); anti-protein disulphide-isomerase (PDI) antibody (green, for sarcoplasmic reticulum); and anti-lamin A antibody (green, for nuclear envelope). Nucleus is blue. AC6mut transgene was detected in caveolae, SR, and nuclear envelope.

    Journal: PLoS ONE

    Article Title: Preserved Cardiac Function despite Marked Impairment of cAMP Generation

    doi: 10.1371/journal.pone.0072151

    Figure Lengend Snippet: AC6mut Design, Expression, Activity and Cellular Distribution. A . The diagram depicts the site of substitution of alanine (ala) for aspartic acid (asp) at position 426 in the C1 domain (intracellular loop) in the construction of AC6mut. The substitution inhibits Mg 2+ binding and alters the efficiency of Gsα-mediated activation of the catalytic core, which impairs the enzymatic activity of AC6, resulting in reduced cAMP production. M1 and M2, transmembrane domains of AC6; C1 and C2, cytoplasmic domains of AC6, which form the catalytic core; βAR, β-adrenergic receptor; βΥ and α, components of the guanosine 5′-triphosphate (GTP)-binding protein, Gs. B . AC6mut mRNA expression was assessed by qRT-PCR using primers common to endogenous AC6 and transgene AC6mut. Primers for detecting GAPDH mRNA were used for internal control of the qRT-PCR reaction. AC6mut mRNA was increased 62-fold vs endogenous AC6. Animal number in bars +SE; Student's t-test, unpaired, 2 tails. C . AC6mut protein was detected in immunoblotting using anti-AC5/6 antibody and confirmed using anti-AU1 tag antibody. AC6mut protein was increased 17-fold vs endogenous AC6. D . Cyclic AMP production in isolated cardiac myocytes from AC6mut and control mice, before (Basal) and after stimulation with isoproterenol (Iso; 10 µM, 10 min) or NKH477 (NKH; 10 µM, 10 min), using cAMP Enzymeimmunoassay. Cardiac myocytes from AC6mut mice (M vs C, control) showed impaired cAMP production in response to Iso and NKH477, a forskolin analog. Bars denote mean +SE; p values from 1-way ANOVA followed by Bonferroni post test (n = 6, each group). E . Double immunofluorescence staining of AC6mut protein in cardiac myocytes isolated from AC6mut vs control mice using anti-AU1 antibody (red); anti-caveolin 3 (Cav-3) antibody (green, for caveolae); anti-protein disulphide-isomerase (PDI) antibody (green, for sarcoplasmic reticulum); and anti-lamin A antibody (green, for nuclear envelope). Nucleus is blue. AC6mut transgene was detected in caveolae, SR, and nuclear envelope.

    Article Snippet: Cyclic AMP was measured using the cAMP Biotrak Enzymeimmunoassay System (GE Healthcare) as previously reported .

    Techniques: Expressing, Activity Assay, Binding Assay, Activation Assay, Quantitative RT-PCR, Isolation, Mouse Assay, Double Immunofluorescence Staining

    S1943 NMHC-IIA phosphorylation regulates MMP9 secretion. (A) Gelatin zymography of conditioned medium from MDA-MB-231 cells expressing wild-type, S1943A or S1943E NMHC-IIA. Standards are human proMMP9 and active MMP2. (B and C) Biotrak MMP9 activity assay of (B) total MMP9 and (C) active MMP9 in conditioned medium from MDA-MB-231 cells expressing wild-type, S1943A or S1943E NMHC-IIA. Data represent the mean ± SEM from 3 independent experiments. Statistical analyses were performed using ANOVA.

    Journal: Experimental cell research

    Article Title: Myosin-IIA heavy chain phosphorylation on SI943 regulates tumor metastasis

    doi: 10.1016/j.yexcr.2018.06.028

    Figure Lengend Snippet: S1943 NMHC-IIA phosphorylation regulates MMP9 secretion. (A) Gelatin zymography of conditioned medium from MDA-MB-231 cells expressing wild-type, S1943A or S1943E NMHC-IIA. Standards are human proMMP9 and active MMP2. (B and C) Biotrak MMP9 activity assay of (B) total MMP9 and (C) active MMP9 in conditioned medium from MDA-MB-231 cells expressing wild-type, S1943A or S1943E NMHC-IIA. Data represent the mean ± SEM from 3 independent experiments. Statistical analyses were performed using ANOVA.

    Article Snippet: MMP9 activity in conditioned media collected from MDA-MB-231 cells (as described above) was determined using the MMP9 Biotrak Activity Assay (GE Healthcare Life Sciences) following the manufacturers protocol.

    Techniques: Zymography, Multiple Displacement Amplification, Expressing, Activity Assay

    HPV-16 E7 up-regulates MMP-9 activity in organotypic cultures. Primary HFKs were transduced with pLXSN-based retroviral vectors expressing HPV16 E6wt and/or E7wt. Cells were then differentiated in organotypic cultures for 9 to 11 days. A, Determination of gelatinase activity in organotypic cultures homogenates (epidermis separated from dermis). Equal amounts of proteins were loaded. Note the increase in MMP-9 gelatinase activity in HPV-16 E7wt and E6E7- expressing epidermis. B-B′, densitometry of pro-MMP-9 bands in epidermis and dermis, respectively. C, MMP-9 levels in epidermis homogenates were determined by Western blot. P

    Journal: PLoS ONE

    Article Title: HPV16 Oncoproteins Induce MMPs/RECK-TIMP-2 Imbalance in Primary Keratinocytes: Possible Implications in Cervical Carcinogenesis

    doi: 10.1371/journal.pone.0033585

    Figure Lengend Snippet: HPV-16 E7 up-regulates MMP-9 activity in organotypic cultures. Primary HFKs were transduced with pLXSN-based retroviral vectors expressing HPV16 E6wt and/or E7wt. Cells were then differentiated in organotypic cultures for 9 to 11 days. A, Determination of gelatinase activity in organotypic cultures homogenates (epidermis separated from dermis). Equal amounts of proteins were loaded. Note the increase in MMP-9 gelatinase activity in HPV-16 E7wt and E6E7- expressing epidermis. B-B′, densitometry of pro-MMP-9 bands in epidermis and dermis, respectively. C, MMP-9 levels in epidermis homogenates were determined by Western blot. P

    Article Snippet: Measurement of MMP-2 and MMP-9 activity MMP-2 and MMP-9 activity was quantified in the culture supernatants from monolayer cultures of HFK transduced with retroviral vectors expressing HPV16 oncoproteins using specific Biotrak assay systems (MMP-2 Biotrak Activity Assay RPN 2631; MMP-9 Biotrak Activity Assay RPN2634, GE Healthcare, Buckinghamshire, UK) according to the manufacturer's instructions.

    Techniques: Activity Assay, Transduction, Expressing, Western Blot