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Gen-Probe ltd recombinant adamts-13

( A ) Cleavage of VWF-A2 (100 nM) by <t>ADAMTS-13</t> (10 nM) after 1 hr incubation in the presence or absence of fH (0.6 µM) was detected by immunoblotting (IB) with polyclonal anti-VWF antibody. A representative blot is shown (n=5). ( B ) The results of three separate experiments with ADAMTS-13-mediated VWF-A2 cleavage were summarized as bar graphs. The VWF-A2 cleavage (%) was calculated by measuring the ratio of band density of cleaved to uncleaved + cleaved VWF-A2. ( C ) Recombinant GST VWF-A2 (100 nM) was incubated with ADAMTS-13 (10 nM), in the presence or absence of fH (0.6 µM) for different time intervals. The cleavage products were detected by immunoblotting with anti-GST antibody. A representative blot is shown (n=3). ( D ) The half maximal cleavage time of GST VWF-A2 by ADAMTS-13 was calculated using the data obtained from different incubation intervals (20 minutes to 2 hours), in the presence or absence of fH. The results of these experiments were summarized as a linear graph (n=3, t-test, ** p<0.01, * p<0.05).

Recombinant Adamts 13, supplied by Gen-Probe ltd, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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recombinant adamts-13 - by Bioz Stars, 2026-10

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1) Product Images from "The Interaction between Factor H and Von Willebrand Factor"

Article Title: The Interaction between Factor H and Von Willebrand Factor

Journal: PLoS ONE

doi: 10.1371/journal.pone.0073715

( A ) Cleavage of VWF-A2 (100 nM) by ADAMTS-13 (10 nM) after 1 hr incubation in the presence or absence of fH (0.6 µM) was detected by immunoblotting (IB) with polyclonal anti-VWF antibody. A representative blot is shown (n=5). ( B ) The results of three separate experiments with ADAMTS-13-mediated VWF-A2 cleavage were summarized as bar graphs. The VWF-A2 cleavage (%) was calculated by measuring the ratio of band density of cleaved to uncleaved + cleaved VWF-A2. ( C ) Recombinant GST VWF-A2 (100 nM) was incubated with ADAMTS-13 (10 nM), in the presence or absence of fH (0.6 µM) for different time intervals. The cleavage products were detected by immunoblotting with anti-GST antibody. A representative blot is shown (n=3). ( D ) The half maximal cleavage time of GST VWF-A2 by ADAMTS-13 was calculated using the data obtained from different incubation intervals (20 minutes to 2 hours), in the presence or absence of fH. The results of these experiments were summarized as a linear graph (n=3, t-test, ** p<0.01, * p<0.05).

Figure Legend Snippet: ( A ) Cleavage of VWF-A2 (100 nM) by ADAMTS-13 (10 nM) after 1 hr incubation in the presence or absence of fH (0.6 µM) was detected by immunoblotting (IB) with polyclonal anti-VWF antibody. A representative blot is shown (n=5). ( B ) The results of three separate experiments with ADAMTS-13-mediated VWF-A2 cleavage were summarized as bar graphs. The VWF-A2 cleavage (%) was calculated by measuring the ratio of band density of cleaved to uncleaved + cleaved VWF-A2. ( C ) Recombinant GST VWF-A2 (100 nM) was incubated with ADAMTS-13 (10 nM), in the presence or absence of fH (0.6 µM) for different time intervals. The cleavage products were detected by immunoblotting with anti-GST antibody. A representative blot is shown (n=3). ( D ) The half maximal cleavage time of GST VWF-A2 by ADAMTS-13 was calculated using the data obtained from different incubation intervals (20 minutes to 2 hours), in the presence or absence of fH. The results of these experiments were summarized as a linear graph (n=3, t-test, ** p<0.01, * p<0.05).

Techniques Used: Incubation, Western Blot, Recombinant

( A ) Cleavage of ADAMTS-13 substrate (FRETS-VWF73) at different concentrations of fH was quantified using a commercial kit (ATS-13, Gen-Probe). Polyclonal anti-fH antibody (100 nM) was used to block the effect of fH on ADAMTS-13-mediated cleavage of the substrate (n=3). ( B ) Factor H was removed from normal serum by immunoadsorption using sepharose beads coated with polyclonal anti-fH antibody. Immunoblotting of 1 µl of fH-depleted serum with an anti-fH antibody showed the absence of fH band in comparison to normal serum. ( C ) The number of ULVWF strings anchored to the surface of histamine-stimulated-HUVECs (with adherent platelets) in the presence of recombinant ADAMTS-13 (control); ADAMTS-13 and factor H; or ADAMTS-13, factor H and a polyclonal anti-factor H antibody was counted starting at 10 sec or 2 min after perfusion in 20 review fields (×200 magnifications; n=4, *p<0.05).

Figure Legend Snippet: ( A ) Cleavage of ADAMTS-13 substrate (FRETS-VWF73) at different concentrations of fH was quantified using a commercial kit (ATS-13, Gen-Probe). Polyclonal anti-fH antibody (100 nM) was used to block the effect of fH on ADAMTS-13-mediated cleavage of the substrate (n=3). ( B ) Factor H was removed from normal serum by immunoadsorption using sepharose beads coated with polyclonal anti-fH antibody. Immunoblotting of 1 µl of fH-depleted serum with an anti-fH antibody showed the absence of fH band in comparison to normal serum. ( C ) The number of ULVWF strings anchored to the surface of histamine-stimulated-HUVECs (with adherent platelets) in the presence of recombinant ADAMTS-13 (control); ADAMTS-13 and factor H; or ADAMTS-13, factor H and a polyclonal anti-factor H antibody was counted starting at 10 sec or 2 min after perfusion in 20 review fields (×200 magnifications; n=4, *p<0.05).

Techniques Used: Blocking Assay, Western Blot, Recombinant

( A ) Cleavage of recombinant VWF-A2 (100 nM) after 30 minutes of incubation with ADAMTS-13 (10 nM) in the presence or absence of full-length or truncated fH (100 nM) was studied by Western-blotting using anti-GST antibody. A representative blot is shown (n=7). ( B ) The band intensity of the VWF-A2 cleavage products was compared between samples with full-length and truncated fH (n=7, t-test).

Figure Legend Snippet: ( A ) Cleavage of recombinant VWF-A2 (100 nM) after 30 minutes of incubation with ADAMTS-13 (10 nM) in the presence or absence of full-length or truncated fH (100 nM) was studied by Western-blotting using anti-GST antibody. A representative blot is shown (n=7). ( B ) The band intensity of the VWF-A2 cleavage products was compared between samples with full-length and truncated fH (n=7, t-test).

Techniques Used: Recombinant, Incubation, Western Blot

Recombinant:

Article Title: Rituximab pharmacokinetics during the management of acute idiopathic thrombotic thrombocytopenic purpura.
Article Snippet: Background: Increasingly, patients with acute, idiopathic, antibody mediated thrombotic thrombocytopenic purpura (TTP) are being treated with rituximab to achieve a durable remission, however, there is the potential that it is removed by plasma exchange (PEX).Objectives: To look at the pharmacokinetics and pharmacodynamics of rituximab in patients with acute idiopathic TTP undergoing PEX.. Patients and methods: Patients who received rituximab for acute idiopathic TTP (group 1, n = 30) and a control group (group 2, n = 3) of TTP patients in remission receiving rituximab electively as maintenance were included.. Rituximab levels were measured before/after each infusion, before/after PEX and in follow-up.

other:

Article Title: Complement C3 is a novel modulator of the anti-factor VIII immune response
Article Snippet: Recombinant ADAMTS-13 and FVIII were kind gifts from Baxter Innovations GmbH (Vienna, Austria), and CSL-Behring (Marburg, Germany), respectively.

Article Title: The Interaction between Factor H and Von Willebrand Factor
Article Snippet: To quantify the effect of fH on ADAMTS-13-mediated VWF cleavage, we measured the activity of recombinant ADAMTS-13 in the presence or absence of plasma-purified fH using FRETS-VWF73 as substrate in a commercial kit (ATS-13, Gen-Probe).

Article Title: Lupus nephritis combined with renal injury due to thrombotic thrombocytopaenic purpura-haemolytic uraemic syndrome.
Article Snippet: Detection of the ADAMTS-13 autoantibody by Western blot analysis Recombinant ADAMTS-13 (15.75 μg) (kindly donated by Dr Scheiflinger, Baxter BioScience, Biomedical Research Center) was prepared in non-reducing condition.

Article Title: Plasma ADAMTS-13 activity in proliferative lupus nephritis: a large cohort study from China.
Article Snippet: Y Tan, ZQ Luan, JB Hao, D Song, F Yu and MH Zhao Renal Division, Department of Medicine, Peking University First Hospital; Peking University Institute of Nephrology; Key Laboratory of Renal Disease, Ministry of Health of China; Key Laboratory of Chronic Kidney Disease Prevention and Treatment, Ministry of Education of China, Beijing, PR.. China; Department of Nephrology, First Affiliated Hospital of Heilongjiang University of Chinese Medicine, Harbin, PR.. China; Department of Nephrology, The First Clinical Medicine of Zhengzhou University, Zhengzhou, PR.

Article Title: Open ADAMTS-13 conformation index predicts earlier relapse in immune-mediated thrombotic thrombocytopenic purpura.
Article Snippet: Laboratory for Thrombosis Research, Interdisciplinary Research Facility Life Sciences, Katholieke Universiteit Leuven Campus Kulak Kortrijk, Kortrijk, Belgium Department of Blood Transfusion Medicine, Nara Medical University, Kashihara, Japan Fondazione IRCCS Ca’ Granda Ospedale Maggiore Policlinico, Angelo Bianchi Bonomi Hemophilia and Thrombosis Center, Università degli Studi di Milano, Department of Pathophysiology and Transplantation, and Fondazione Luigi Villa, Milan, Italy Department of Internal Medicine and Hematology, Semmelweis University and Research Group for Immunology and Haematology, Semmelweis University Eötvös Loránd Research Network (Office for Supported Research Groups), Budapest, Hungary Institute of Clinical Chemistry and Laboratory Medicine, University Medical Center of the Johannes Gutenberg University, Mainz, Germany Center for Thrombosis and Hemostasis, University Medical Center of the Johannes Gutenberg University, Mainz, Germany Department of Evidence-Based Medicine, Nara Medical University, Kashihara, Japan Department of Hematology, Oncology and Pneumology, University Medical Center of the Johannes Gutenberg University, Mainz, Germany Service d’Hématologie Biologique, Hôpital Lariboisière, Assistance Publique–Hôpitaux de Paris and EA3518, Institut de Recherche Saint Louis, Université de Paris, Paris, France Centre de Référence des Microangiopathies Thrombotiques, Service d’hématologie, Hôpital Saint Antoine, Assistance Publique–Hôpitaux de Paris and Sorbonne Université, Paris, France Department for Clinical Chemistry and Haematology, University Medical Center Utrecht, Utrecht University, Utrecht, The Netherlands Department of Hematology and Central Hematology Laboratory, Inselspital, Bern University Hospital, University of Bern, Bern, Switzerland Haemostasis Research Unit, University College London, London, United Kingdom

Article Title: Role of von Willebrand factor and ADAMTS ‐13 in early brain injury after experimental subarachnoid hemorrhage
Article Snippet: Recombinant ADAMTS‐13 was kindly provided by Baxalta under the same grant, and Baxalta US Inc., now part of Shire, had no further role in project planning, experiments, or data analysis.

Article Title: Prevalence of the ADAMTS-13 missense mutation R1060W in late onset adult thrombotic thrombocytopenic purpura
Article Snippet: Microtiter plates were coated with recombinant ADAMTS-13 (rADAMTS-13; Baxter Bioscience, Vienna, Austria).

Image Search Results

Journal: PLoS ONE

Article Title: The Interaction between Factor H and Von Willebrand Factor

doi: 10.1371/journal.pone.0073715

Figure Lengend Snippet: ( A ) Cleavage of VWF-A2 (100 nM) by ADAMTS-13 (10 nM) after 1 hr incubation in the presence or absence of fH (0.6 µM) was detected by immunoblotting (IB) with polyclonal anti-VWF antibody. A representative blot is shown (n=5). ( B ) The results of three separate experiments with ADAMTS-13-mediated VWF-A2 cleavage were summarized as bar graphs. The VWF-A2 cleavage (%) was calculated by measuring the ratio of band density of cleaved to uncleaved + cleaved VWF-A2. ( C ) Recombinant GST VWF-A2 (100 nM) was incubated with ADAMTS-13 (10 nM), in the presence or absence of fH (0.6 µM) for different time intervals. The cleavage products were detected by immunoblotting with anti-GST antibody. A representative blot is shown (n=3). ( D ) The half maximal cleavage time of GST VWF-A2 by ADAMTS-13 was calculated using the data obtained from different incubation intervals (20 minutes to 2 hours), in the presence or absence of fH. The results of these experiments were summarized as a linear graph (n=3, t-test, ** p<0.01, * p<0.05).

Article Snippet: To quantify the effect of fH on ADAMTS-13-mediated VWF cleavage, we measured the activity of recombinant ADAMTS-13 in the presence or absence of plasma-purified fH using FRETS-VWF73 as substrate in a commercial kit (ATS-13, Gen-Probe).

Techniques: Incubation, Western Blot, Recombinant

Journal: PLoS ONE

Article Title: The Interaction between Factor H and Von Willebrand Factor

doi: 10.1371/journal.pone.0073715

Figure Lengend Snippet: ( A ) Cleavage of ADAMTS-13 substrate (FRETS-VWF73) at different concentrations of fH was quantified using a commercial kit (ATS-13, Gen-Probe). Polyclonal anti-fH antibody (100 nM) was used to block the effect of fH on ADAMTS-13-mediated cleavage of the substrate (n=3). ( B ) Factor H was removed from normal serum by immunoadsorption using sepharose beads coated with polyclonal anti-fH antibody. Immunoblotting of 1 µl of fH-depleted serum with an anti-fH antibody showed the absence of fH band in comparison to normal serum. ( C ) The number of ULVWF strings anchored to the surface of histamine-stimulated-HUVECs (with adherent platelets) in the presence of recombinant ADAMTS-13 (control); ADAMTS-13 and factor H; or ADAMTS-13, factor H and a polyclonal anti-factor H antibody was counted starting at 10 sec or 2 min after perfusion in 20 review fields (×200 magnifications; n=4, *p<0.05).

Techniques: Blocking Assay, Western Blot, Recombinant

Journal: PLoS ONE

Article Title: The Interaction between Factor H and Von Willebrand Factor

doi: 10.1371/journal.pone.0073715

Figure Lengend Snippet: ( A ) Cleavage of recombinant VWF-A2 (100 nM) after 30 minutes of incubation with ADAMTS-13 (10 nM) in the presence or absence of full-length or truncated fH (100 nM) was studied by Western-blotting using anti-GST antibody. A representative blot is shown (n=7). ( B ) The band intensity of the VWF-A2 cleavage products was compared between samples with full-length and truncated fH (n=7, t-test).

Techniques: Recombinant, Incubation, Western Blot

Constructs and purified full-length ADAMTS13 and variant proteins. (A). Schematic representation of the domain structures of a full-length ADAMTS13 and two truncated variants. (B). SDS-polyacrylamide gel with Coomassie blue staining demonstrates the purified recombinant full-length ADAMTS13, MDTCS, and T5C, ∼5 μg per lane (arrowhead).

Journal: Research and Practice in Thrombosis and Haemostasis

Article Title: A novel mechanism underlying allosteric regulation of ADAMTS-13 revealed by hydrogen−deuterium exchange plus mass spectrometry

doi: 10.1016/j.rpth.2022.100012

Figure Lengend Snippet: Constructs and purified full-length ADAMTS13 and variant proteins. (A). Schematic representation of the domain structures of a full-length ADAMTS13 and two truncated variants. (B). SDS-polyacrylamide gel with Coomassie blue staining demonstrates the purified recombinant full-length ADAMTS13, MDTCS, and T5C, ∼5 μg per lane (arrowhead).

Article Snippet: A full-length recombinant ADAMTS-13 (FL-A13) was expressed in human embryonic kidney (HEK)-293 cells (Invitrogen, Carlsbad, CA) [ ].

Techniques: Construct, Purification, Variant Assay, Staining, Recombinant

Peptide coverage and representative illustration of single and bimodal deuterium incorporations. (A). Overall peptide coverage in all H of a full-length ADAMTS13 (FL-A13) (pink) and a truncated ADATMS13 variant (eg, MDTCS or T5C) (black) following protease digestion, column chromatography, and mass spectrometric analysis. (B). Representative illustration of bimodal deuterium incorporations in peptides (eg, 217-230 and 282-304) of a full-length ADAMTS13 at pD7.0. From top to bottom is the exchange occurring from 10 to 6000 seconds.

Journal: Research and Practice in Thrombosis and Haemostasis

Article Title: A novel mechanism underlying allosteric regulation of ADAMTS-13 revealed by hydrogen−deuterium exchange plus mass spectrometry

doi: 10.1016/j.rpth.2022.100012

Figure Lengend Snippet: Peptide coverage and representative illustration of single and bimodal deuterium incorporations. (A). Overall peptide coverage in all H of a full-length ADAMTS13 (FL-A13) (pink) and a truncated ADATMS13 variant (eg, MDTCS or T5C) (black) following protease digestion, column chromatography, and mass spectrometric analysis. (B). Representative illustration of bimodal deuterium incorporations in peptides (eg, 217-230 and 282-304) of a full-length ADAMTS13 at pD7.0. From top to bottom is the exchange occurring from 10 to 6000 seconds.

Article Snippet: A full-length recombinant ADAMTS-13 (FL-A13) was expressed in human embryonic kidney (HEK)-293 cells (Invitrogen, Carlsbad, CA) [ ].

Techniques: Variant Assay, Column Chromatography

Time-dependent incorporation of deuterium in various peptides from a full-length ADAMTS13 and a MDTCS fragment. Each panel demonstrates the rate of deuterium incorporation as a function of time (10-6000 seconds) in various peptides (as labeled in a-l) derived from a full-length ADAMTS13 (ie, FL-A13) (closed circle and black line) and a truncated ADAMTS13 variant (ie, MDTCS) (open triangle and cyan line). Images a to d show the peptides derived from the metalloprotease domain; e, from the Cys-rich domain; and f to l, from the spacer domain.

Journal: Research and Practice in Thrombosis and Haemostasis

Article Title: A novel mechanism underlying allosteric regulation of ADAMTS-13 revealed by hydrogen−deuterium exchange plus mass spectrometry

doi: 10.1016/j.rpth.2022.100012

Figure Lengend Snippet: Time-dependent incorporation of deuterium in various peptides from a full-length ADAMTS13 and a MDTCS fragment. Each panel demonstrates the rate of deuterium incorporation as a function of time (10-6000 seconds) in various peptides (as labeled in a-l) derived from a full-length ADAMTS13 (ie, FL-A13) (closed circle and black line) and a truncated ADAMTS13 variant (ie, MDTCS) (open triangle and cyan line). Images a to d show the peptides derived from the metalloprotease domain; e, from the Cys-rich domain; and f to l, from the spacer domain.

Article Snippet: A full-length recombinant ADAMTS-13 (FL-A13) was expressed in human embryonic kidney (HEK)-293 cells (Invitrogen, Carlsbad, CA) [ ].

Techniques: Labeling, Derivative Assay, Variant Assay

Ribbon representation of the peptides with altered deuterium incorporation rates in the M-D-T-C-S domains of a full-length ADAMTS13 comparing with the same regions in a truncated MDTCS variant. The M-D-T-C-S domains (as indicated in the bottom on the left column and on the top in the right column) demonstrate the peptides involving in the differential deuterium incorporation rates as a function of time (10 to 6000 seconds) from top to bottom in a full-length ADAMTS13 (left) and a truncated MDTCS fragment (right). The color from blue to red indicates that the percentage of update of deuterium increases from 5% to 10% to >60%. Here Met, Dis, CysR, and Spa indicate metalloprotease, disintegrin, cysteine-rich, and spacer domains, respectively.

Journal: Research and Practice in Thrombosis and Haemostasis

Article Title: A novel mechanism underlying allosteric regulation of ADAMTS-13 revealed by hydrogen−deuterium exchange plus mass spectrometry

doi: 10.1016/j.rpth.2022.100012

Figure Lengend Snippet: Ribbon representation of the peptides with altered deuterium incorporation rates in the M-D-T-C-S domains of a full-length ADAMTS13 comparing with the same regions in a truncated MDTCS variant. The M-D-T-C-S domains (as indicated in the bottom on the left column and on the top in the right column) demonstrate the peptides involving in the differential deuterium incorporation rates as a function of time (10 to 6000 seconds) from top to bottom in a full-length ADAMTS13 (left) and a truncated MDTCS fragment (right). The color from blue to red indicates that the percentage of update of deuterium increases from 5% to 10% to >60%. Here Met, Dis, CysR, and Spa indicate metalloprotease, disintegrin, cysteine-rich, and spacer domains, respectively.

Article Snippet: A full-length recombinant ADAMTS-13 (FL-A13) was expressed in human embryonic kidney (HEK)-293 cells (Invitrogen, Carlsbad, CA) [ ].

Techniques: Variant Assay

Detailed analysis of deuterium incorporation at a single-residue resolution in the spacer domain. (A) A ribbon representation of low and high rates of deuterium incorporation in the peptides derived from the metalloprotease (Met), Cysteine-rich (Cys-R), and spacer domains (Spa) in the truncated MDTCS compared with that in the peptides in the full-length ADAMTS13 at a neutral pD. (B) A heat map demonstrates differential rates of deuterium incorporation in the portion of spacer domain of the full-length ADAMTS13 (top) and MDTCS fragment at pD7.0. The percentage of uptake ranges from blue (<10% D uptake) to red (>90% D uptake). No back-exchange correction and statistical filtering were performed for the generation of heat map.

Journal: Research and Practice in Thrombosis and Haemostasis

Article Title: A novel mechanism underlying allosteric regulation of ADAMTS-13 revealed by hydrogen−deuterium exchange plus mass spectrometry

doi: 10.1016/j.rpth.2022.100012

Figure Lengend Snippet: Detailed analysis of deuterium incorporation at a single-residue resolution in the spacer domain. (A) A ribbon representation of low and high rates of deuterium incorporation in the peptides derived from the metalloprotease (Met), Cysteine-rich (Cys-R), and spacer domains (Spa) in the truncated MDTCS compared with that in the peptides in the full-length ADAMTS13 at a neutral pD. (B) A heat map demonstrates differential rates of deuterium incorporation in the portion of spacer domain of the full-length ADAMTS13 (top) and MDTCS fragment at pD7.0. The percentage of uptake ranges from blue (<10% D uptake) to red (>90% D uptake). No back-exchange correction and statistical filtering were performed for the generation of heat map.

Article Snippet: A full-length recombinant ADAMTS-13 (FL-A13) was expressed in human embryonic kidney (HEK)-293 cells (Invitrogen, Carlsbad, CA) [ ].

Techniques: Derivative Assay

Deuterium incorporation rates over time in peptides from a full-length ADAMTS-13 and its truncated variant (MDTCS or T5C) at pD6.0 in comparison to that at pD8.0.

Journal: Research and Practice in Thrombosis and Haemostasis

Article Title: A novel mechanism underlying allosteric regulation of ADAMTS-13 revealed by hydrogen−deuterium exchange plus mass spectrometry

doi: 10.1016/j.rpth.2022.100012

Figure Lengend Snippet: Deuterium incorporation rates over time in peptides from a full-length ADAMTS-13 and its truncated variant (MDTCS or T5C) at pD6.0 in comparison to that at pD8.0.

Article Snippet: A full-length recombinant ADAMTS-13 (FL-A13) was expressed in human embryonic kidney (HEK)-293 cells (Invitrogen, Carlsbad, CA) [ ].

Techniques: Variant Assay

Deuterium incorporation in the peptides from the full-length ADAMTS13 and the truncated variants at pD6.0 over time in comparison to that of the same peptides at pD8.0. The deuterium incorporation rates in the peptides derived from the N-terminal portion the full-length ADAMTS13 (A) and the MDTCS fragment (B) at pD6.0 compared with that at pD8.0 at 2 different time points. In addition, the deuterium incorporation rates of the peptides derived from C-terminus of a full-length ADAMTS13 (C) and T5C (D) at pD6.0 compared with that of the same peptides at pD8.0 at 2 different time points. The deuterium incorporation rate is approximately 100× slower at pD6.0 than at pD8.0. Thus, the comparison of the deuterium incorporation was made between 6000 seconds at pD6.0 and 60 seconds at pD8.0, for instance. Here, Met, Dis, CysR, Spa, CUB1, and CUB2 indicate metalloprotease, disintegrin, cysteine-rich, spacer, CUB-1 and CUB-2 domains, respectively. The purple or blue colors indicate an increase of deuterium incorporation rate at pD6.0 compared with pD8.0. Yellow indicates the peptides with same deuterium incorporation rate at pD6.0 and pD8.0. Gray shows the areas of no peptides recovered.

Journal: Research and Practice in Thrombosis and Haemostasis

Article Title: A novel mechanism underlying allosteric regulation of ADAMTS-13 revealed by hydrogen−deuterium exchange plus mass spectrometry

doi: 10.1016/j.rpth.2022.100012

Figure Lengend Snippet: Deuterium incorporation in the peptides from the full-length ADAMTS13 and the truncated variants at pD6.0 over time in comparison to that of the same peptides at pD8.0. The deuterium incorporation rates in the peptides derived from the N-terminal portion the full-length ADAMTS13 (A) and the MDTCS fragment (B) at pD6.0 compared with that at pD8.0 at 2 different time points. In addition, the deuterium incorporation rates of the peptides derived from C-terminus of a full-length ADAMTS13 (C) and T5C (D) at pD6.0 compared with that of the same peptides at pD8.0 at 2 different time points. The deuterium incorporation rate is approximately 100× slower at pD6.0 than at pD8.0. Thus, the comparison of the deuterium incorporation was made between 6000 seconds at pD6.0 and 60 seconds at pD8.0, for instance. Here, Met, Dis, CysR, Spa, CUB1, and CUB2 indicate metalloprotease, disintegrin, cysteine-rich, spacer, CUB-1 and CUB-2 domains, respectively. The purple or blue colors indicate an increase of deuterium incorporation rate at pD6.0 compared with pD8.0. Yellow indicates the peptides with same deuterium incorporation rate at pD6.0 and pD8.0. Gray shows the areas of no peptides recovered.

Article Snippet: A full-length recombinant ADAMTS-13 (FL-A13) was expressed in human embryonic kidney (HEK)-293 cells (Invitrogen, Carlsbad, CA) [ ].

Techniques: Derivative Assay

Binding interactions between N-terminus and C-terminus of ADAMTS13. (A) and (B) show the representative traces of the association and dissociation rates as a function of time following an injection of a purified recombinant MDTCS and DTCS fragment, respectively, over a CM5 surface that was immobilized with a purified CUB fragment. (C) and (D) are the means of maximal response units (RU) as a function of the concentration (0-1.0 μM) of the recombinant MDTCS ( K D =0.33 μm and Chi 2 , 5.84) and DTCS ( K D =0.46 μm, Chi 2 4.34), respectively. K D , equilibrium dissociation constant, was determined using the Prism 8.0 software.

Journal: Research and Practice in Thrombosis and Haemostasis

Article Title: A novel mechanism underlying allosteric regulation of ADAMTS-13 revealed by hydrogen−deuterium exchange plus mass spectrometry

doi: 10.1016/j.rpth.2022.100012

Figure Lengend Snippet: Binding interactions between N-terminus and C-terminus of ADAMTS13. (A) and (B) show the representative traces of the association and dissociation rates as a function of time following an injection of a purified recombinant MDTCS and DTCS fragment, respectively, over a CM5 surface that was immobilized with a purified CUB fragment. (C) and (D) are the means of maximal response units (RU) as a function of the concentration (0-1.0 μM) of the recombinant MDTCS ( K D =0.33 μm and Chi 2 , 5.84) and DTCS ( K D =0.46 μm, Chi 2 4.34), respectively. K D , equilibrium dissociation constant, was determined using the Prism 8.0 software.

Article Snippet: A full-length recombinant ADAMTS-13 (FL-A13) was expressed in human embryonic kidney (HEK)-293 cells (Invitrogen, Carlsbad, CA) [ ].

Techniques: Binding Assay, Injection, Purification, Recombinant, Concentration Assay, Software

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recombinant adamts-13 (Gen-Probe ltd)

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