adam 17 (R&D Systems)
R&D Systems is a verified supplier 
R&D Systems manufactures this product 
94
Structured Review
R&D Systems
adam 17
Adam 17, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 47 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/adam+17/Recombinant+Human+TACE%2FADAM17+Protein%2C+CF/us12612459-769-7-14
Average 94 stars, based on 47 article reviews
Adam 17, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 47 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/adam+17/Recombinant+Human+TACE%2FADAM17+Protein%2C+CF/us12612459-769-7-14
Average 94 stars, based on 47 article reviews
adam 17 - by Bioz Stars,
2026-09
94/100 stars
Images
Related Articles
Recombinant:Article Title: Internal Disulfide Bonding and Glycosylation of Interleukin-7 Protect Against Proteolytic Inactivation by Neutrophil Metalloproteinases and Serine Proteases. Article Snippet: .. Recombinant human proMMP-2, proMMP-7, proMMP-8 and ‘a disintegrin and metalloproteases’ ( Article Title: Design of Peptide Hydroxamate-Based Photoreactive Activity-Based Probes of Zinc-Dependent Metalloproteases Article Snippet: Metalloproteases (ADAMs, MMPs) are multidomain proteins that play key roles in extracellular matrix remodelling and degradation, in cell–cell and cell–matrix interactions and in the proteolytic liberation of membrane-anchored proforms of cytokines and growth factors, the so-called ectodomain shedding.. In this work we describe the development of photoactivatable activity-based probes with which active Article Title: Methods of identifying agents that block MCD28 cleavage by MMPS Article Snippet: Matrix Metalloproteinases and ADAM's—Commercial recombinant human metalloproteinases MMP-1 (Cat. No. AS-55575), MMP-9 (Cat. No. AS-55576), MMP-10 (Cat. No. AS-72067), MMP-12 (Cat. No. AS-55525) and MMP-13 (Cat. No. AS-72257) are from AnaSpec. .. Recombinant human ADAM-10 (Cat. No. 936-AD) and Incubation:Article Title: DYNAMIC CHANGES IN MATRIX METALLOPROTIENASE ACTIVITY WITHIN THE HUMAN MYOCARDIAL INTERSTITIUM DURING MYOCARDIAL ARREST AND REPERFUSION Article Snippet: In previously performed in-vivo animal experiments, we determined that optimal response was achieved with a 60 uM MMP substrate concentration 25 and this was utilized in the present study. fig ft0 fig mode=article f1 caption a4 A) Validation of the MMP fluorogenic substrate (0.03 mM, Anaspec, # 27074) was performed by using increasing concentrations of an MMP 2/9 recombinant catalytic domain (BIOMOL, SE-237,SE-244). .. Following an incubation period of 2 hrs at 37°C, fluorescence ... fig ft0 fig mode=article f1 caption a4 In order to further examine the specificity of the MMP substrate (0.03 mM) was incubated in the presence of ( A ) a disintegrin and metalloprotease, Fluorescence:Article Title: DYNAMIC CHANGES IN MATRIX METALLOPROTIENASE ACTIVITY WITHIN THE HUMAN MYOCARDIAL INTERSTITIUM DURING MYOCARDIAL ARREST AND REPERFUSION Article Snippet: In previously performed in-vivo animal experiments, we determined that optimal response was achieved with a 60 uM MMP substrate concentration 25 and this was utilized in the present study. fig ft0 fig mode=article f1 caption a4 A) Validation of the MMP fluorogenic substrate (0.03 mM, Anaspec, # 27074) was performed by using increasing concentrations of an MMP 2/9 recombinant catalytic domain (BIOMOL, SE-237,SE-244). .. Following an incubation period of 2 hrs at 37°C, fluorescence ... fig ft0 fig mode=article f1 caption a4 In order to further examine the specificity of the MMP substrate (0.03 mM) was incubated in the presence of ( A ) a disintegrin and metalloprotease, Inhibition:Article Title: Design of Peptide Hydroxamate-Based Photoreactive Activity-Based Probes of Zinc-Dependent Metalloproteases Article Snippet: Metalloproteases (ADAMs, MMPs) are multidomain proteins that play key roles in extracellular matrix remodelling and degradation, in cell–cell and cell–matrix interactions and in the proteolytic liberation of membrane-anchored proforms of cytokines and growth factors, the so-called ectodomain shedding.. In this work we describe the development of photoactivatable activity-based probes with which active Labeling:Article Title: Design of Peptide Hydroxamate-Based Photoreactive Activity-Based Probes of Zinc-Dependent Metalloproteases Article Snippet: Metalloproteases (ADAMs, MMPs) are multidomain proteins that play key roles in extracellular matrix remodelling and degradation, in cell–cell and cell–matrix interactions and in the proteolytic liberation of membrane-anchored proforms of cytokines and growth factors, the so-called ectodomain shedding.. In this work we describe the development of photoactivatable activity-based probes with which active Derivative Assay:Article Title: Design of Peptide Hydroxamate-Based Photoreactive Activity-Based Probes of Zinc-Dependent Metalloproteases Article Snippet: Metalloproteases (ADAMs, MMPs) are multidomain proteins that play key roles in extracellular matrix remodelling and degradation, in cell–cell and cell–matrix interactions and in the proteolytic liberation of membrane-anchored proforms of cytokines and growth factors, the so-called ectodomain shedding.. In this work we describe the development of photoactivatable activity-based probes with which active |
