Efficient expression and purification of biologically active human cystatin proteins
Cystatins are reversible cysteine protease inhibitor proteins. They are known to play important roles in controlling cathepsins, neurodegenerative disease, and in immune system regulation. Production of recombinant cystatin proteins is important for biochemical and function characterization. In this...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Chauhan, Sakshi [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2016transfer abstract |
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| Schlagwörter: |
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| Umfang: |
8 |
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| Übergeordnetes Werk: |
Enthalten in: Structural and thermal control of seismic activity and megathrust rupture dynamics in subduction zones: Lessons from the Mw 9.0, 2011 Tohoku earthquake - Satriano, Claudio ELSEVIER, 2014, Amsterdam [u.a.] |
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| Übergeordnetes Werk: |
volume:118 ; year:2016 ; pages:10-17 ; extent:8 |
| Links: |
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| DOI / URN: |
10.1016/j.pep.2015.10.005 |
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| 520 | |a Cystatins are reversible cysteine protease inhibitor proteins. They are known to play important roles in controlling cathepsins, neurodegenerative disease, and in immune system regulation. Production of recombinant cystatin proteins is important for biochemical and function characterization. In this study, we cloned and expressed human stefin A, stefin B and cystatin C in Escherichia coli. Human stefin A, stefin B and cystatin C were purified from soluble fraction. For cystatin C, we used various chaperone plasmids to make cystatin C soluble, as it is reported to localize in inclusion bodies. Trigger factor, GroES-GroEL, DnaK-DnaJ-GrpE chaperones lead to the presence of cystatin C in the soluble fraction. Immobilized metal affinity chromatography, glutathione sepharose and anion exchange chromatography techniques were employed for efficient purification of these proteins. Their biological activities were tested by inhibition assays against cathepsin L and H3 protease. | ||
| 520 | |a Cystatins are reversible cysteine protease inhibitor proteins. They are known to play important roles in controlling cathepsins, neurodegenerative disease, and in immune system regulation. Production of recombinant cystatin proteins is important for biochemical and function characterization. In this study, we cloned and expressed human stefin A, stefin B and cystatin C in Escherichia coli. Human stefin A, stefin B and cystatin C were purified from soluble fraction. For cystatin C, we used various chaperone plasmids to make cystatin C soluble, as it is reported to localize in inclusion bodies. Trigger factor, GroES-GroEL, DnaK-DnaJ-GrpE chaperones lead to the presence of cystatin C in the soluble fraction. Immobilized metal affinity chromatography, glutathione sepharose and anion exchange chromatography techniques were employed for efficient purification of these proteins. Their biological activities were tested by inhibition assays against cathepsin L and H3 protease. | ||
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| 773 | 0 | 8 | |i Enthalten in |n Elsevier |a Satriano, Claudio ELSEVIER |t Structural and thermal control of seismic activity and megathrust rupture dynamics in subduction zones: Lessons from the Mw 9.0, 2011 Tohoku earthquake |d 2014 |g Amsterdam [u.a.] |w (DE-627)ELV023049715 |
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10.1016/j.pep.2015.10.005 doi GBVA2016018000022.pica (DE-627)ELV035489308 (ELSEVIER)S1046-5928(15)30084-X DE-627 ger DE-627 rakwb eng 570 610 570 DE-600 610 DE-600 550 VZ 610 333.7 VZ BIODIV DE-30 fid 42.90 bkl 42.11 bkl Chauhan, Sakshi verfasserin aut Efficient expression and purification of biologically active human cystatin proteins 2016transfer abstract 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Cystatins are reversible cysteine protease inhibitor proteins. They are known to play important roles in controlling cathepsins, neurodegenerative disease, and in immune system regulation. Production of recombinant cystatin proteins is important for biochemical and function characterization. In this study, we cloned and expressed human stefin A, stefin B and cystatin C in Escherichia coli. Human stefin A, stefin B and cystatin C were purified from soluble fraction. For cystatin C, we used various chaperone plasmids to make cystatin C soluble, as it is reported to localize in inclusion bodies. Trigger factor, GroES-GroEL, DnaK-DnaJ-GrpE chaperones lead to the presence of cystatin C in the soluble fraction. Immobilized metal affinity chromatography, glutathione sepharose and anion exchange chromatography techniques were employed for efficient purification of these proteins. Their biological activities were tested by inhibition assays against cathepsin L and H3 protease. Cystatins are reversible cysteine protease inhibitor proteins. They are known to play important roles in controlling cathepsins, neurodegenerative disease, and in immune system regulation. Production of recombinant cystatin proteins is important for biochemical and function characterization. In this study, we cloned and expressed human stefin A, stefin B and cystatin C in Escherichia coli. Human stefin A, stefin B and cystatin C were purified from soluble fraction. For cystatin C, we used various chaperone plasmids to make cystatin C soluble, as it is reported to localize in inclusion bodies. Trigger factor, GroES-GroEL, DnaK-DnaJ-GrpE chaperones lead to the presence of cystatin C in the soluble fraction. Immobilized metal affinity chromatography, glutathione sepharose and anion exchange chromatography techniques were employed for efficient purification of these proteins. Their biological activities were tested by inhibition assays against cathepsin L and H3 protease. Stefin A Elsevier Stefin B Elsevier Cystatin C Elsevier Trigger factor Elsevier GroES-GroEL Elsevier DnaK-DnaJ-GrpE Elsevier Tomar, Raghuvir S. oth Enthalten in Elsevier Satriano, Claudio ELSEVIER Structural and thermal control of seismic activity and megathrust rupture dynamics in subduction zones: Lessons from the Mw 9.0, 2011 Tohoku earthquake 2014 Amsterdam [u.a.] (DE-627)ELV023049715 volume:118 year:2016 pages:10-17 extent:8 https://doi.org/10.1016/j.pep.2015.10.005 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV SSG-OLC-PHA GBV_ILN_31 GBV_ILN_72 GBV_ILN_217 GBV_ILN_255 GBV_ILN_257 GBV_ILN_286 GBV_ILN_341 42.90 Ökologie: Allgemeines VZ 42.11 Biomathematik Biokybernetik VZ AR 118 2016 10-17 8 045F 570 |
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10.1016/j.pep.2015.10.005 doi GBVA2016018000022.pica (DE-627)ELV035489308 (ELSEVIER)S1046-5928(15)30084-X DE-627 ger DE-627 rakwb eng 570 610 570 DE-600 610 DE-600 550 VZ 610 333.7 VZ BIODIV DE-30 fid 42.90 bkl 42.11 bkl Chauhan, Sakshi verfasserin aut Efficient expression and purification of biologically active human cystatin proteins 2016transfer abstract 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Cystatins are reversible cysteine protease inhibitor proteins. They are known to play important roles in controlling cathepsins, neurodegenerative disease, and in immune system regulation. Production of recombinant cystatin proteins is important for biochemical and function characterization. In this study, we cloned and expressed human stefin A, stefin B and cystatin C in Escherichia coli. Human stefin A, stefin B and cystatin C were purified from soluble fraction. For cystatin C, we used various chaperone plasmids to make cystatin C soluble, as it is reported to localize in inclusion bodies. Trigger factor, GroES-GroEL, DnaK-DnaJ-GrpE chaperones lead to the presence of cystatin C in the soluble fraction. Immobilized metal affinity chromatography, glutathione sepharose and anion exchange chromatography techniques were employed for efficient purification of these proteins. Their biological activities were tested by inhibition assays against cathepsin L and H3 protease. Cystatins are reversible cysteine protease inhibitor proteins. They are known to play important roles in controlling cathepsins, neurodegenerative disease, and in immune system regulation. Production of recombinant cystatin proteins is important for biochemical and function characterization. In this study, we cloned and expressed human stefin A, stefin B and cystatin C in Escherichia coli. Human stefin A, stefin B and cystatin C were purified from soluble fraction. For cystatin C, we used various chaperone plasmids to make cystatin C soluble, as it is reported to localize in inclusion bodies. Trigger factor, GroES-GroEL, DnaK-DnaJ-GrpE chaperones lead to the presence of cystatin C in the soluble fraction. Immobilized metal affinity chromatography, glutathione sepharose and anion exchange chromatography techniques were employed for efficient purification of these proteins. Their biological activities were tested by inhibition assays against cathepsin L and H3 protease. Stefin A Elsevier Stefin B Elsevier Cystatin C Elsevier Trigger factor Elsevier GroES-GroEL Elsevier DnaK-DnaJ-GrpE Elsevier Tomar, Raghuvir S. oth Enthalten in Elsevier Satriano, Claudio ELSEVIER Structural and thermal control of seismic activity and megathrust rupture dynamics in subduction zones: Lessons from the Mw 9.0, 2011 Tohoku earthquake 2014 Amsterdam [u.a.] (DE-627)ELV023049715 volume:118 year:2016 pages:10-17 extent:8 https://doi.org/10.1016/j.pep.2015.10.005 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV SSG-OLC-PHA GBV_ILN_31 GBV_ILN_72 GBV_ILN_217 GBV_ILN_255 GBV_ILN_257 GBV_ILN_286 GBV_ILN_341 42.90 Ökologie: Allgemeines VZ 42.11 Biomathematik Biokybernetik VZ AR 118 2016 10-17 8 045F 570 |
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10.1016/j.pep.2015.10.005 doi GBVA2016018000022.pica (DE-627)ELV035489308 (ELSEVIER)S1046-5928(15)30084-X DE-627 ger DE-627 rakwb eng 570 610 570 DE-600 610 DE-600 550 VZ 610 333.7 VZ BIODIV DE-30 fid 42.90 bkl 42.11 bkl Chauhan, Sakshi verfasserin aut Efficient expression and purification of biologically active human cystatin proteins 2016transfer abstract 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Cystatins are reversible cysteine protease inhibitor proteins. They are known to play important roles in controlling cathepsins, neurodegenerative disease, and in immune system regulation. Production of recombinant cystatin proteins is important for biochemical and function characterization. In this study, we cloned and expressed human stefin A, stefin B and cystatin C in Escherichia coli. Human stefin A, stefin B and cystatin C were purified from soluble fraction. For cystatin C, we used various chaperone plasmids to make cystatin C soluble, as it is reported to localize in inclusion bodies. Trigger factor, GroES-GroEL, DnaK-DnaJ-GrpE chaperones lead to the presence of cystatin C in the soluble fraction. Immobilized metal affinity chromatography, glutathione sepharose and anion exchange chromatography techniques were employed for efficient purification of these proteins. Their biological activities were tested by inhibition assays against cathepsin L and H3 protease. Cystatins are reversible cysteine protease inhibitor proteins. They are known to play important roles in controlling cathepsins, neurodegenerative disease, and in immune system regulation. Production of recombinant cystatin proteins is important for biochemical and function characterization. In this study, we cloned and expressed human stefin A, stefin B and cystatin C in Escherichia coli. Human stefin A, stefin B and cystatin C were purified from soluble fraction. For cystatin C, we used various chaperone plasmids to make cystatin C soluble, as it is reported to localize in inclusion bodies. Trigger factor, GroES-GroEL, DnaK-DnaJ-GrpE chaperones lead to the presence of cystatin C in the soluble fraction. Immobilized metal affinity chromatography, glutathione sepharose and anion exchange chromatography techniques were employed for efficient purification of these proteins. Their biological activities were tested by inhibition assays against cathepsin L and H3 protease. Stefin A Elsevier Stefin B Elsevier Cystatin C Elsevier Trigger factor Elsevier GroES-GroEL Elsevier DnaK-DnaJ-GrpE Elsevier Tomar, Raghuvir S. oth Enthalten in Elsevier Satriano, Claudio ELSEVIER Structural and thermal control of seismic activity and megathrust rupture dynamics in subduction zones: Lessons from the Mw 9.0, 2011 Tohoku earthquake 2014 Amsterdam [u.a.] (DE-627)ELV023049715 volume:118 year:2016 pages:10-17 extent:8 https://doi.org/10.1016/j.pep.2015.10.005 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV SSG-OLC-PHA GBV_ILN_31 GBV_ILN_72 GBV_ILN_217 GBV_ILN_255 GBV_ILN_257 GBV_ILN_286 GBV_ILN_341 42.90 Ökologie: Allgemeines VZ 42.11 Biomathematik Biokybernetik VZ AR 118 2016 10-17 8 045F 570 |
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10.1016/j.pep.2015.10.005 doi GBVA2016018000022.pica (DE-627)ELV035489308 (ELSEVIER)S1046-5928(15)30084-X DE-627 ger DE-627 rakwb eng 570 610 570 DE-600 610 DE-600 550 VZ 610 333.7 VZ BIODIV DE-30 fid 42.90 bkl 42.11 bkl Chauhan, Sakshi verfasserin aut Efficient expression and purification of biologically active human cystatin proteins 2016transfer abstract 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Cystatins are reversible cysteine protease inhibitor proteins. They are known to play important roles in controlling cathepsins, neurodegenerative disease, and in immune system regulation. Production of recombinant cystatin proteins is important for biochemical and function characterization. In this study, we cloned and expressed human stefin A, stefin B and cystatin C in Escherichia coli. Human stefin A, stefin B and cystatin C were purified from soluble fraction. For cystatin C, we used various chaperone plasmids to make cystatin C soluble, as it is reported to localize in inclusion bodies. Trigger factor, GroES-GroEL, DnaK-DnaJ-GrpE chaperones lead to the presence of cystatin C in the soluble fraction. Immobilized metal affinity chromatography, glutathione sepharose and anion exchange chromatography techniques were employed for efficient purification of these proteins. Their biological activities were tested by inhibition assays against cathepsin L and H3 protease. Cystatins are reversible cysteine protease inhibitor proteins. They are known to play important roles in controlling cathepsins, neurodegenerative disease, and in immune system regulation. Production of recombinant cystatin proteins is important for biochemical and function characterization. In this study, we cloned and expressed human stefin A, stefin B and cystatin C in Escherichia coli. Human stefin A, stefin B and cystatin C were purified from soluble fraction. For cystatin C, we used various chaperone plasmids to make cystatin C soluble, as it is reported to localize in inclusion bodies. Trigger factor, GroES-GroEL, DnaK-DnaJ-GrpE chaperones lead to the presence of cystatin C in the soluble fraction. Immobilized metal affinity chromatography, glutathione sepharose and anion exchange chromatography techniques were employed for efficient purification of these proteins. Their biological activities were tested by inhibition assays against cathepsin L and H3 protease. Stefin A Elsevier Stefin B Elsevier Cystatin C Elsevier Trigger factor Elsevier GroES-GroEL Elsevier DnaK-DnaJ-GrpE Elsevier Tomar, Raghuvir S. oth Enthalten in Elsevier Satriano, Claudio ELSEVIER Structural and thermal control of seismic activity and megathrust rupture dynamics in subduction zones: Lessons from the Mw 9.0, 2011 Tohoku earthquake 2014 Amsterdam [u.a.] (DE-627)ELV023049715 volume:118 year:2016 pages:10-17 extent:8 https://doi.org/10.1016/j.pep.2015.10.005 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV SSG-OLC-PHA GBV_ILN_31 GBV_ILN_72 GBV_ILN_217 GBV_ILN_255 GBV_ILN_257 GBV_ILN_286 GBV_ILN_341 42.90 Ökologie: Allgemeines VZ 42.11 Biomathematik Biokybernetik VZ AR 118 2016 10-17 8 045F 570 |
| allfieldsSound |
10.1016/j.pep.2015.10.005 doi GBVA2016018000022.pica (DE-627)ELV035489308 (ELSEVIER)S1046-5928(15)30084-X DE-627 ger DE-627 rakwb eng 570 610 570 DE-600 610 DE-600 550 VZ 610 333.7 VZ BIODIV DE-30 fid 42.90 bkl 42.11 bkl Chauhan, Sakshi verfasserin aut Efficient expression and purification of biologically active human cystatin proteins 2016transfer abstract 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Cystatins are reversible cysteine protease inhibitor proteins. They are known to play important roles in controlling cathepsins, neurodegenerative disease, and in immune system regulation. Production of recombinant cystatin proteins is important for biochemical and function characterization. In this study, we cloned and expressed human stefin A, stefin B and cystatin C in Escherichia coli. Human stefin A, stefin B and cystatin C were purified from soluble fraction. For cystatin C, we used various chaperone plasmids to make cystatin C soluble, as it is reported to localize in inclusion bodies. Trigger factor, GroES-GroEL, DnaK-DnaJ-GrpE chaperones lead to the presence of cystatin C in the soluble fraction. Immobilized metal affinity chromatography, glutathione sepharose and anion exchange chromatography techniques were employed for efficient purification of these proteins. Their biological activities were tested by inhibition assays against cathepsin L and H3 protease. Cystatins are reversible cysteine protease inhibitor proteins. They are known to play important roles in controlling cathepsins, neurodegenerative disease, and in immune system regulation. Production of recombinant cystatin proteins is important for biochemical and function characterization. In this study, we cloned and expressed human stefin A, stefin B and cystatin C in Escherichia coli. Human stefin A, stefin B and cystatin C were purified from soluble fraction. For cystatin C, we used various chaperone plasmids to make cystatin C soluble, as it is reported to localize in inclusion bodies. Trigger factor, GroES-GroEL, DnaK-DnaJ-GrpE chaperones lead to the presence of cystatin C in the soluble fraction. Immobilized metal affinity chromatography, glutathione sepharose and anion exchange chromatography techniques were employed for efficient purification of these proteins. Their biological activities were tested by inhibition assays against cathepsin L and H3 protease. Stefin A Elsevier Stefin B Elsevier Cystatin C Elsevier Trigger factor Elsevier GroES-GroEL Elsevier DnaK-DnaJ-GrpE Elsevier Tomar, Raghuvir S. oth Enthalten in Elsevier Satriano, Claudio ELSEVIER Structural and thermal control of seismic activity and megathrust rupture dynamics in subduction zones: Lessons from the Mw 9.0, 2011 Tohoku earthquake 2014 Amsterdam [u.a.] (DE-627)ELV023049715 volume:118 year:2016 pages:10-17 extent:8 https://doi.org/10.1016/j.pep.2015.10.005 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV SSG-OLC-PHA GBV_ILN_31 GBV_ILN_72 GBV_ILN_217 GBV_ILN_255 GBV_ILN_257 GBV_ILN_286 GBV_ILN_341 42.90 Ökologie: Allgemeines VZ 42.11 Biomathematik Biokybernetik VZ AR 118 2016 10-17 8 045F 570 |
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English |
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Enthalten in Structural and thermal control of seismic activity and megathrust rupture dynamics in subduction zones: Lessons from the Mw 9.0, 2011 Tohoku earthquake Amsterdam [u.a.] volume:118 year:2016 pages:10-17 extent:8 |
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Enthalten in Structural and thermal control of seismic activity and megathrust rupture dynamics in subduction zones: Lessons from the Mw 9.0, 2011 Tohoku earthquake Amsterdam [u.a.] volume:118 year:2016 pages:10-17 extent:8 |
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Structural and thermal control of seismic activity and megathrust rupture dynamics in subduction zones: Lessons from the Mw 9.0, 2011 Tohoku earthquake |
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efficient expression and purification of biologically active human cystatin proteins |
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Efficient expression and purification of biologically active human cystatin proteins |
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Cystatins are reversible cysteine protease inhibitor proteins. They are known to play important roles in controlling cathepsins, neurodegenerative disease, and in immune system regulation. Production of recombinant cystatin proteins is important for biochemical and function characterization. In this study, we cloned and expressed human stefin A, stefin B and cystatin C in Escherichia coli. Human stefin A, stefin B and cystatin C were purified from soluble fraction. For cystatin C, we used various chaperone plasmids to make cystatin C soluble, as it is reported to localize in inclusion bodies. Trigger factor, GroES-GroEL, DnaK-DnaJ-GrpE chaperones lead to the presence of cystatin C in the soluble fraction. Immobilized metal affinity chromatography, glutathione sepharose and anion exchange chromatography techniques were employed for efficient purification of these proteins. Their biological activities were tested by inhibition assays against cathepsin L and H3 protease. |
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Cystatins are reversible cysteine protease inhibitor proteins. They are known to play important roles in controlling cathepsins, neurodegenerative disease, and in immune system regulation. Production of recombinant cystatin proteins is important for biochemical and function characterization. In this study, we cloned and expressed human stefin A, stefin B and cystatin C in Escherichia coli. Human stefin A, stefin B and cystatin C were purified from soluble fraction. For cystatin C, we used various chaperone plasmids to make cystatin C soluble, as it is reported to localize in inclusion bodies. Trigger factor, GroES-GroEL, DnaK-DnaJ-GrpE chaperones lead to the presence of cystatin C in the soluble fraction. Immobilized metal affinity chromatography, glutathione sepharose and anion exchange chromatography techniques were employed for efficient purification of these proteins. Their biological activities were tested by inhibition assays against cathepsin L and H3 protease. |
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Cystatins are reversible cysteine protease inhibitor proteins. They are known to play important roles in controlling cathepsins, neurodegenerative disease, and in immune system regulation. Production of recombinant cystatin proteins is important for biochemical and function characterization. In this study, we cloned and expressed human stefin A, stefin B and cystatin C in Escherichia coli. Human stefin A, stefin B and cystatin C were purified from soluble fraction. For cystatin C, we used various chaperone plasmids to make cystatin C soluble, as it is reported to localize in inclusion bodies. Trigger factor, GroES-GroEL, DnaK-DnaJ-GrpE chaperones lead to the presence of cystatin C in the soluble fraction. Immobilized metal affinity chromatography, glutathione sepharose and anion exchange chromatography techniques were employed for efficient purification of these proteins. Their biological activities were tested by inhibition assays against cathepsin L and H3 protease. |
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Efficient expression and purification of biologically active human cystatin proteins |
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