recombinant human adamts5 protein Search Results


93
R&D Systems recombinant human active adamts 5
Recombinant Human Active Adamts 5, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/recombinant+human+adamts5+protein/Recombinant+Human+ADAMTS5+Protein%2C+CF/pmc04409205-61-0-17
Average 93 stars, based on 1 article reviews
recombinant human active adamts 5 - by Bioz Stars, 2026-11
93/100 stars
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94
R&D Systems recombinant human adamts5
Figure 7. <t>ADAMTS5</t> (a disintegrin and metalloproteinase with thrombospondin motifs 5) knockdown enhances the effect of matrilin 2 on valvular interstitial cell (VIC) phenotypic change. A, VICs from calcified aortic valves were treated with recombinant human ADAMTS5 (rhADAMTS5; 5.0 µg/mL) for 48 h. Immunoblots and densitometric data show that ADAMTS5 decreased the baseline levels of α-SMA (α-smooth muscle actin), Runx2 (runt-related transcription factor 2), and ALP (alkaline phosphatase). B, VICs from normal aortic valves were treated with rhADAMTS5 (5.0 µg/mL) 1 h before matrilin 2 (2.0 μg/mL) stimulation for 48 h. ADAMTS5 attenuated the upregulation of α-SMA, Runx2, and ALP by matrilin 2. C, ADAMTS5 small interfering RNA (siRNA) reduced ADAMTS5 levels in VICs from normal aortic valves. D and E, VICs from normal aortic valves were transfected with ADAMTS5 siRNA 72 h before matrilin 2 stimulation for 48 h. Immu- noblots and densitometric data show that ADAMTS5 knockdown augmented the upregulation of α-SMA, Runx2, and ALP by matrilin 2. Mean±SE; n=4 separate experiments using distinct cell isolates; *P<0.05 vs untreated control and control siRNA-treated; #P<0.05 vs matrilin 2 alone or matrilin 2+control siRNA.
Recombinant Human Adamts5, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/recombinant+human+adamts5+protein/Recombinant+Human+ADAMTS5+Protein%2C+CF/10__1161_slash_atvbaha__117__309021-460-0-17
Average 94 stars, based on 1 article reviews
recombinant human adamts5 - by Bioz Stars, 2026-11
94/100 stars
  Buy from Supplier

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Purified recombinant protein of Human ADAM metallopeptidase with thrombospondin type 1 motif 5 ADAMTS5 His346 Pro622 with N terminal His tag expressed in E coli 50ug
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The Recombinant Human ADAMTS5 Protein from R D Systems is derived from NS0 The Recombinant Human ADAMTS5 Protein has been validated for the following applications Enzyme Activity
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ADAMTS5 (human) Recombinant Protein for Ctrl
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Figure 7. ADAMTS5 (a disintegrin and metalloproteinase with thrombospondin motifs 5) knockdown enhances the effect of matrilin 2 on valvular interstitial cell (VIC) phenotypic change. A, VICs from calcified aortic valves were treated with recombinant human ADAMTS5 (rhADAMTS5; 5.0 µg/mL) for 48 h. Immunoblots and densitometric data show that ADAMTS5 decreased the baseline levels of α-SMA (α-smooth muscle actin), Runx2 (runt-related transcription factor 2), and ALP (alkaline phosphatase). B, VICs from normal aortic valves were treated with rhADAMTS5 (5.0 µg/mL) 1 h before matrilin 2 (2.0 μg/mL) stimulation for 48 h. ADAMTS5 attenuated the upregulation of α-SMA, Runx2, and ALP by matrilin 2. C, ADAMTS5 small interfering RNA (siRNA) reduced ADAMTS5 levels in VICs from normal aortic valves. D and E, VICs from normal aortic valves were transfected with ADAMTS5 siRNA 72 h before matrilin 2 stimulation for 48 h. Immu- noblots and densitometric data show that ADAMTS5 knockdown augmented the upregulation of α-SMA, Runx2, and ALP by matrilin 2. Mean±SE; n=4 separate experiments using distinct cell isolates; *P<0.05 vs untreated control and control siRNA-treated; #P<0.05 vs matrilin 2 alone or matrilin 2+control siRNA.

Journal: Arteriosclerosis, Thrombosis, and Vascular Biology

Article Title: ADAMTS5 Deficiency in Calcified Aortic Valves Is Associated With Elevated Pro-Osteogenic Activity in Valvular Interstitial Cells

doi: 10.1161/atvbaha.117.309021

Figure Lengend Snippet: Figure 7. ADAMTS5 (a disintegrin and metalloproteinase with thrombospondin motifs 5) knockdown enhances the effect of matrilin 2 on valvular interstitial cell (VIC) phenotypic change. A, VICs from calcified aortic valves were treated with recombinant human ADAMTS5 (rhADAMTS5; 5.0 µg/mL) for 48 h. Immunoblots and densitometric data show that ADAMTS5 decreased the baseline levels of α-SMA (α-smooth muscle actin), Runx2 (runt-related transcription factor 2), and ALP (alkaline phosphatase). B, VICs from normal aortic valves were treated with rhADAMTS5 (5.0 µg/mL) 1 h before matrilin 2 (2.0 μg/mL) stimulation for 48 h. ADAMTS5 attenuated the upregulation of α-SMA, Runx2, and ALP by matrilin 2. C, ADAMTS5 small interfering RNA (siRNA) reduced ADAMTS5 levels in VICs from normal aortic valves. D and E, VICs from normal aortic valves were transfected with ADAMTS5 siRNA 72 h before matrilin 2 stimulation for 48 h. Immu- noblots and densitometric data show that ADAMTS5 knockdown augmented the upregulation of α-SMA, Runx2, and ALP by matrilin 2. Mean±SE; n=4 separate experiments using distinct cell isolates; *P<0.05 vs untreated control and control siRNA-treated; #P<0.05 vs matrilin 2 alone or matrilin 2+control siRNA.

Article Snippet: Recombinant human ADAMTS5 and matrilin2 proteins (expressed by mouse myeloma cell line; endotoxin free) were purchased from R&D Systems (Minneapolis, MN).

Techniques: Knockdown, Recombinant, Western Blot, Small Interfering RNA, Transfection, Control