htc75 cell line (Federation of European Neuroscience Societies)
90
Structured Review
Federation of European Neuroscience Societies
htc75 cell line
Htc75 Cell Line, supplied by Federation of European Neuroscience Societies, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/htc75+cell+line/htc75+cell+line/pm12459476-27-1-46
Average 90 stars, based on 1 article reviews
Htc75 Cell Line, supplied by Federation of European Neuroscience Societies, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/htc75+cell+line/htc75+cell+line/pm12459476-27-1-46
Average 90 stars, based on 1 article reviews
htc75 cell line - by Bioz Stars,
2026-10
90/100 stars
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Related Articles
Control:Article Title: Cellular activation of proMMP-13 by MT1-MMP depends on the C-terminal domain of MMP-13. Article Snippet: Procollagenase-3 (proMMP-13) can be activated by soluble or cell associated membrane type matrix metalloproteinase 1 (MT1-MMP).. In this study we show that the cell based activation of proMMP-13 by MT1-MMP was dependent on the C-terminal domain, as v249 451 proMMP-13, which lacks the haemopexin domain, and a chimaera from N-terminal MMP-13 and C-terminal MMP-19 (proMMP-13/19) were not processed by MT1-MMP expressing cells.. Only the initial cleavage at Gly35^Ile36 was dependent on MT1-MMP activity, as conversion to the active enzyme (Tyr85 N-terminus) required a functional MMP-13 active site. Transfection:Article Title: Cellular activation of proMMP-13 by MT1-MMP depends on the C-terminal domain of MMP-13. Article Snippet: Procollagenase-3 (proMMP-13) can be activated by soluble or cell associated membrane type matrix metalloproteinase 1 (MT1-MMP).. In this study we show that the cell based activation of proMMP-13 by MT1-MMP was dependent on the C-terminal domain, as v249 451 proMMP-13, which lacks the haemopexin domain, and a chimaera from N-terminal MMP-13 and C-terminal MMP-19 (proMMP-13/19) were not processed by MT1-MMP expressing cells.. Only the initial cleavage at Gly35^Ile36 was dependent on MT1-MMP activity, as conversion to the active enzyme (Tyr85 N-terminus) required a functional MMP-13 active site. Plasmid Preparation:Article Title: Cellular activation of proMMP-13 by MT1-MMP depends on the C-terminal domain of MMP-13. Article Snippet: Procollagenase-3 (proMMP-13) can be activated by soluble or cell associated membrane type matrix metalloproteinase 1 (MT1-MMP).. In this study we show that the cell based activation of proMMP-13 by MT1-MMP was dependent on the C-terminal domain, as v249 451 proMMP-13, which lacks the haemopexin domain, and a chimaera from N-terminal MMP-13 and C-terminal MMP-19 (proMMP-13/19) were not processed by MT1-MMP expressing cells.. Only the initial cleavage at Gly35^Ile36 was dependent on MT1-MMP activity, as conversion to the active enzyme (Tyr85 N-terminus) required a functional MMP-13 active site. Marker:Article Title: Cellular activation of proMMP-13 by MT1-MMP depends on the C-terminal domain of MMP-13. Article Snippet: Procollagenase-3 (proMMP-13) can be activated by soluble or cell associated membrane type matrix metalloproteinase 1 (MT1-MMP).. In this study we show that the cell based activation of proMMP-13 by MT1-MMP was dependent on the C-terminal domain, as v249 451 proMMP-13, which lacks the haemopexin domain, and a chimaera from N-terminal MMP-13 and C-terminal MMP-19 (proMMP-13/19) were not processed by MT1-MMP expressing cells.. Only the initial cleavage at Gly35^Ile36 was dependent on MT1-MMP activity, as conversion to the active enzyme (Tyr85 N-terminus) required a functional MMP-13 active site. |
