recombinant timp 1 Search Results


timp3  (R&D Systems)
94
R&D Systems timp3
Figure 2. Inhibition of ADAMTS1 by TIMPs. A, inhibition of versicanase activity by TIMP family members. TIMP1, TIMP2, <t>TIMP3,</t> and TIMP4 (each at 500 nM) were incubated with ADAMTS1 (100 nM) for 1 h at 37 C before addition of V1-5GAG and digestion for 2 h. Following SDS-PAGE under reducing conditions (5% β-mercaptoethanol) and immunoblotting, FL V1-5GAG and versikine (VSK) were detected by the anti-Vc antibody. A representative immunoblot is shown (n = 2 independent experiments). B, inhibition of peptidolytic activity. TIMPs (each 25 nM) were incubated with a nominal con- centration of 25 nM ADAMTS1 for 1 h at 37 C before addition of the QF peptide substrate fluorescein-5(6)-carbonyl-Ala-Glu-Leu-Asn-Gly-Arg-Pro-Ile-Ser-Ile- Ala-Lys (5(6)-TAMRA) (3.5 μM) and digestion for 2 h. Following subtraction of the background (reactions not containing ADAMTS1), values were converted into percentage of ADAMTS1 activity in the absence of TIMPs and reported as average ± SD (n = 3, each point representing a technical replicate), p < 0.05 by Mann-Whitney test. C, titration of ADAMTS1 with TIMP3. TIMP3 (0–16 nM) was incubated with ADAMTS1 (20 nM nominal concentration) at 37 C for 1 h, and residual activity against the QF peptide FAM-AELNGRPISIAK-Tamra (3.5 μM) was determined. A representative titration curve is shown, each point representing a mean of two technical replicates. Final concentration of ADAMTS1 following titration was 10 nM. FL, full-length; No E, no enzyme; No I, no inhibitor; QF, Quenched-Fluorescent; TIMP, tissue inhibitor of metalloproteinase.
Timp3, 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
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timp 1  (Boster Bio)
94
Boster Bio timp 1
Figure 2. Inhibition of ADAMTS1 by TIMPs. A, inhibition of versicanase activity by TIMP family members. TIMP1, TIMP2, <t>TIMP3,</t> and TIMP4 (each at 500 nM) were incubated with ADAMTS1 (100 nM) for 1 h at 37 C before addition of V1-5GAG and digestion for 2 h. Following SDS-PAGE under reducing conditions (5% β-mercaptoethanol) and immunoblotting, FL V1-5GAG and versikine (VSK) were detected by the anti-Vc antibody. A representative immunoblot is shown (n = 2 independent experiments). B, inhibition of peptidolytic activity. TIMPs (each 25 nM) were incubated with a nominal con- centration of 25 nM ADAMTS1 for 1 h at 37 C before addition of the QF peptide substrate fluorescein-5(6)-carbonyl-Ala-Glu-Leu-Asn-Gly-Arg-Pro-Ile-Ser-Ile- Ala-Lys (5(6)-TAMRA) (3.5 μM) and digestion for 2 h. Following subtraction of the background (reactions not containing ADAMTS1), values were converted into percentage of ADAMTS1 activity in the absence of TIMPs and reported as average ± SD (n = 3, each point representing a technical replicate), p < 0.05 by Mann-Whitney test. C, titration of ADAMTS1 with TIMP3. TIMP3 (0–16 nM) was incubated with ADAMTS1 (20 nM nominal concentration) at 37 C for 1 h, and residual activity against the QF peptide FAM-AELNGRPISIAK-Tamra (3.5 μM) was determined. A representative titration curve is shown, each point representing a mean of two technical replicates. Final concentration of ADAMTS1 following titration was 10 nM. FL, full-length; No E, no enzyme; No I, no inhibitor; QF, Quenched-Fluorescent; TIMP, tissue inhibitor of metalloproteinase.
Timp 1, supplied by Boster Bio, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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129 187 254 47 heruntergeladen  (R&D Systems)
93
R&D Systems 129 187 254 47 heruntergeladen
Figure 2. Inhibition of ADAMTS1 by TIMPs. A, inhibition of versicanase activity by TIMP family members. TIMP1, TIMP2, <t>TIMP3,</t> and TIMP4 (each at 500 nM) were incubated with ADAMTS1 (100 nM) for 1 h at 37 C before addition of V1-5GAG and digestion for 2 h. Following SDS-PAGE under reducing conditions (5% β-mercaptoethanol) and immunoblotting, FL V1-5GAG and versikine (VSK) were detected by the anti-Vc antibody. A representative immunoblot is shown (n = 2 independent experiments). B, inhibition of peptidolytic activity. TIMPs (each 25 nM) were incubated with a nominal con- centration of 25 nM ADAMTS1 for 1 h at 37 C before addition of the QF peptide substrate fluorescein-5(6)-carbonyl-Ala-Glu-Leu-Asn-Gly-Arg-Pro-Ile-Ser-Ile- Ala-Lys (5(6)-TAMRA) (3.5 μM) and digestion for 2 h. Following subtraction of the background (reactions not containing ADAMTS1), values were converted into percentage of ADAMTS1 activity in the absence of TIMPs and reported as average ± SD (n = 3, each point representing a technical replicate), p < 0.05 by Mann-Whitney test. C, titration of ADAMTS1 with TIMP3. TIMP3 (0–16 nM) was incubated with ADAMTS1 (20 nM nominal concentration) at 37 C for 1 h, and residual activity against the QF peptide FAM-AELNGRPISIAK-Tamra (3.5 μM) was determined. A representative titration curve is shown, each point representing a mean of two technical replicates. Final concentration of ADAMTS1 following titration was 10 nM. FL, full-length; No E, no enzyme; No I, no inhibitor; QF, Quenched-Fluorescent; TIMP, tissue inhibitor of metalloproteinase.
129 187 254 47 Heruntergeladen, 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
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mouse recombinant timp 1  (R&D Systems)
94
R&D Systems mouse recombinant timp 1
Figure 2. Inhibition of ADAMTS1 by TIMPs. A, inhibition of versicanase activity by TIMP family members. TIMP1, TIMP2, <t>TIMP3,</t> and TIMP4 (each at 500 nM) were incubated with ADAMTS1 (100 nM) for 1 h at 37 C before addition of V1-5GAG and digestion for 2 h. Following SDS-PAGE under reducing conditions (5% β-mercaptoethanol) and immunoblotting, FL V1-5GAG and versikine (VSK) were detected by the anti-Vc antibody. A representative immunoblot is shown (n = 2 independent experiments). B, inhibition of peptidolytic activity. TIMPs (each 25 nM) were incubated with a nominal con- centration of 25 nM ADAMTS1 for 1 h at 37 C before addition of the QF peptide substrate fluorescein-5(6)-carbonyl-Ala-Glu-Leu-Asn-Gly-Arg-Pro-Ile-Ser-Ile- Ala-Lys (5(6)-TAMRA) (3.5 μM) and digestion for 2 h. Following subtraction of the background (reactions not containing ADAMTS1), values were converted into percentage of ADAMTS1 activity in the absence of TIMPs and reported as average ± SD (n = 3, each point representing a technical replicate), p < 0.05 by Mann-Whitney test. C, titration of ADAMTS1 with TIMP3. TIMP3 (0–16 nM) was incubated with ADAMTS1 (20 nM nominal concentration) at 37 C for 1 h, and residual activity against the QF peptide FAM-AELNGRPISIAK-Tamra (3.5 μM) was determined. A representative titration curve is shown, each point representing a mean of two technical replicates. Final concentration of ADAMTS1 following titration was 10 nM. FL, full-length; No E, no enzyme; No I, no inhibitor; QF, Quenched-Fluorescent; TIMP, tissue inhibitor of metalloproteinase.
Mouse Recombinant Timp 1, 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
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recombinant rat timp1  (R&D Systems)
93
R&D Systems recombinant rat timp1
Figure 2. Inhibition of ADAMTS1 by TIMPs. A, inhibition of versicanase activity by TIMP family members. TIMP1, TIMP2, <t>TIMP3,</t> and TIMP4 (each at 500 nM) were incubated with ADAMTS1 (100 nM) for 1 h at 37 C before addition of V1-5GAG and digestion for 2 h. Following SDS-PAGE under reducing conditions (5% β-mercaptoethanol) and immunoblotting, FL V1-5GAG and versikine (VSK) were detected by the anti-Vc antibody. A representative immunoblot is shown (n = 2 independent experiments). B, inhibition of peptidolytic activity. TIMPs (each 25 nM) were incubated with a nominal con- centration of 25 nM ADAMTS1 for 1 h at 37 C before addition of the QF peptide substrate fluorescein-5(6)-carbonyl-Ala-Glu-Leu-Asn-Gly-Arg-Pro-Ile-Ser-Ile- Ala-Lys (5(6)-TAMRA) (3.5 μM) and digestion for 2 h. Following subtraction of the background (reactions not containing ADAMTS1), values were converted into percentage of ADAMTS1 activity in the absence of TIMPs and reported as average ± SD (n = 3, each point representing a technical replicate), p < 0.05 by Mann-Whitney test. C, titration of ADAMTS1 with TIMP3. TIMP3 (0–16 nM) was incubated with ADAMTS1 (20 nM nominal concentration) at 37 C for 1 h, and residual activity against the QF peptide FAM-AELNGRPISIAK-Tamra (3.5 μM) was determined. A representative titration curve is shown, each point representing a mean of two technical replicates. Final concentration of ADAMTS1 following titration was 10 nM. FL, full-length; No E, no enzyme; No I, no inhibitor; QF, Quenched-Fluorescent; TIMP, tissue inhibitor of metalloproteinase.
Recombinant Rat Timp1, 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
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tbst  (R&D Systems)
92
R&D Systems tbst
Figure 2. Inhibition of ADAMTS1 by TIMPs. A, inhibition of versicanase activity by TIMP family members. TIMP1, TIMP2, <t>TIMP3,</t> and TIMP4 (each at 500 nM) were incubated with ADAMTS1 (100 nM) for 1 h at 37 C before addition of V1-5GAG and digestion for 2 h. Following SDS-PAGE under reducing conditions (5% β-mercaptoethanol) and immunoblotting, FL V1-5GAG and versikine (VSK) were detected by the anti-Vc antibody. A representative immunoblot is shown (n = 2 independent experiments). B, inhibition of peptidolytic activity. TIMPs (each 25 nM) were incubated with a nominal con- centration of 25 nM ADAMTS1 for 1 h at 37 C before addition of the QF peptide substrate fluorescein-5(6)-carbonyl-Ala-Glu-Leu-Asn-Gly-Arg-Pro-Ile-Ser-Ile- Ala-Lys (5(6)-TAMRA) (3.5 μM) and digestion for 2 h. Following subtraction of the background (reactions not containing ADAMTS1), values were converted into percentage of ADAMTS1 activity in the absence of TIMPs and reported as average ± SD (n = 3, each point representing a technical replicate), p < 0.05 by Mann-Whitney test. C, titration of ADAMTS1 with TIMP3. TIMP3 (0–16 nM) was incubated with ADAMTS1 (20 nM nominal concentration) at 37 C for 1 h, and residual activity against the QF peptide FAM-AELNGRPISIAK-Tamra (3.5 μM) was determined. A representative titration curve is shown, each point representing a mean of two technical replicates. Final concentration of ADAMTS1 following titration was 10 nM. FL, full-length; No E, no enzyme; No I, no inhibitor; QF, Quenched-Fluorescent; TIMP, tissue inhibitor of metalloproteinase.
Tbst, supplied by R&D Systems, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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recombinant timp 1  (Aviva Systems)
86
Aviva Systems recombinant timp 1
Figure 2. Inhibition of ADAMTS1 by TIMPs. A, inhibition of versicanase activity by TIMP family members. TIMP1, TIMP2, <t>TIMP3,</t> and TIMP4 (each at 500 nM) were incubated with ADAMTS1 (100 nM) for 1 h at 37 C before addition of V1-5GAG and digestion for 2 h. Following SDS-PAGE under reducing conditions (5% β-mercaptoethanol) and immunoblotting, FL V1-5GAG and versikine (VSK) were detected by the anti-Vc antibody. A representative immunoblot is shown (n = 2 independent experiments). B, inhibition of peptidolytic activity. TIMPs (each 25 nM) were incubated with a nominal con- centration of 25 nM ADAMTS1 for 1 h at 37 C before addition of the QF peptide substrate fluorescein-5(6)-carbonyl-Ala-Glu-Leu-Asn-Gly-Arg-Pro-Ile-Ser-Ile- Ala-Lys (5(6)-TAMRA) (3.5 μM) and digestion for 2 h. Following subtraction of the background (reactions not containing ADAMTS1), values were converted into percentage of ADAMTS1 activity in the absence of TIMPs and reported as average ± SD (n = 3, each point representing a technical replicate), p < 0.05 by Mann-Whitney test. C, titration of ADAMTS1 with TIMP3. TIMP3 (0–16 nM) was incubated with ADAMTS1 (20 nM nominal concentration) at 37 C for 1 h, and residual activity against the QF peptide FAM-AELNGRPISIAK-Tamra (3.5 μM) was determined. A representative titration curve is shown, each point representing a mean of two technical replicates. Final concentration of ADAMTS1 following titration was 10 nM. FL, full-length; No E, no enzyme; No I, no inhibitor; QF, Quenched-Fluorescent; TIMP, tissue inhibitor of metalloproteinase.
Recombinant Timp 1, supplied by Aviva Systems, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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mouse recombinant mr timp 1  (R&D Systems)
90
R&D Systems mouse recombinant mr timp 1
Figure 2. Inhibition of ADAMTS1 by TIMPs. A, inhibition of versicanase activity by TIMP family members. TIMP1, TIMP2, <t>TIMP3,</t> and TIMP4 (each at 500 nM) were incubated with ADAMTS1 (100 nM) for 1 h at 37 C before addition of V1-5GAG and digestion for 2 h. Following SDS-PAGE under reducing conditions (5% β-mercaptoethanol) and immunoblotting, FL V1-5GAG and versikine (VSK) were detected by the anti-Vc antibody. A representative immunoblot is shown (n = 2 independent experiments). B, inhibition of peptidolytic activity. TIMPs (each 25 nM) were incubated with a nominal con- centration of 25 nM ADAMTS1 for 1 h at 37 C before addition of the QF peptide substrate fluorescein-5(6)-carbonyl-Ala-Glu-Leu-Asn-Gly-Arg-Pro-Ile-Ser-Ile- Ala-Lys (5(6)-TAMRA) (3.5 μM) and digestion for 2 h. Following subtraction of the background (reactions not containing ADAMTS1), values were converted into percentage of ADAMTS1 activity in the absence of TIMPs and reported as average ± SD (n = 3, each point representing a technical replicate), p < 0.05 by Mann-Whitney test. C, titration of ADAMTS1 with TIMP3. TIMP3 (0–16 nM) was incubated with ADAMTS1 (20 nM nominal concentration) at 37 C for 1 h, and residual activity against the QF peptide FAM-AELNGRPISIAK-Tamra (3.5 μM) was determined. A representative titration curve is shown, each point representing a mean of two technical replicates. Final concentration of ADAMTS1 following titration was 10 nM. FL, full-length; No E, no enzyme; No I, no inhibitor; QF, Quenched-Fluorescent; TIMP, tissue inhibitor of metalloproteinase.
Mouse Recombinant Mr Timp 1, supplied by R&D Systems, 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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human timp 1  (R&D Systems)
90
R&D Systems human timp 1
Figure 2. Inhibition of ADAMTS1 by TIMPs. A, inhibition of versicanase activity by TIMP family members. TIMP1, TIMP2, <t>TIMP3,</t> and TIMP4 (each at 500 nM) were incubated with ADAMTS1 (100 nM) for 1 h at 37 C before addition of V1-5GAG and digestion for 2 h. Following SDS-PAGE under reducing conditions (5% β-mercaptoethanol) and immunoblotting, FL V1-5GAG and versikine (VSK) were detected by the anti-Vc antibody. A representative immunoblot is shown (n = 2 independent experiments). B, inhibition of peptidolytic activity. TIMPs (each 25 nM) were incubated with a nominal con- centration of 25 nM ADAMTS1 for 1 h at 37 C before addition of the QF peptide substrate fluorescein-5(6)-carbonyl-Ala-Glu-Leu-Asn-Gly-Arg-Pro-Ile-Ser-Ile- Ala-Lys (5(6)-TAMRA) (3.5 μM) and digestion for 2 h. Following subtraction of the background (reactions not containing ADAMTS1), values were converted into percentage of ADAMTS1 activity in the absence of TIMPs and reported as average ± SD (n = 3, each point representing a technical replicate), p < 0.05 by Mann-Whitney test. C, titration of ADAMTS1 with TIMP3. TIMP3 (0–16 nM) was incubated with ADAMTS1 (20 nM nominal concentration) at 37 C for 1 h, and residual activity against the QF peptide FAM-AELNGRPISIAK-Tamra (3.5 μM) was determined. A representative titration curve is shown, each point representing a mean of two technical replicates. Final concentration of ADAMTS1 following titration was 10 nM. FL, full-length; No E, no enzyme; No I, no inhibitor; QF, Quenched-Fluorescent; TIMP, tissue inhibitor of metalloproteinase.
Human Timp 1, supplied by R&D Systems, 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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murine timp1 r d systems  (R&D Systems)
93
R&D Systems murine timp1 r d systems
Figure 2. Inhibition of ADAMTS1 by TIMPs. A, inhibition of versicanase activity by TIMP family members. TIMP1, TIMP2, <t>TIMP3,</t> and TIMP4 (each at 500 nM) were incubated with ADAMTS1 (100 nM) for 1 h at 37 C before addition of V1-5GAG and digestion for 2 h. Following SDS-PAGE under reducing conditions (5% β-mercaptoethanol) and immunoblotting, FL V1-5GAG and versikine (VSK) were detected by the anti-Vc antibody. A representative immunoblot is shown (n = 2 independent experiments). B, inhibition of peptidolytic activity. TIMPs (each 25 nM) were incubated with a nominal con- centration of 25 nM ADAMTS1 for 1 h at 37 C before addition of the QF peptide substrate fluorescein-5(6)-carbonyl-Ala-Glu-Leu-Asn-Gly-Arg-Pro-Ile-Ser-Ile- Ala-Lys (5(6)-TAMRA) (3.5 μM) and digestion for 2 h. Following subtraction of the background (reactions not containing ADAMTS1), values were converted into percentage of ADAMTS1 activity in the absence of TIMPs and reported as average ± SD (n = 3, each point representing a technical replicate), p < 0.05 by Mann-Whitney test. C, titration of ADAMTS1 with TIMP3. TIMP3 (0–16 nM) was incubated with ADAMTS1 (20 nM nominal concentration) at 37 C for 1 h, and residual activity against the QF peptide FAM-AELNGRPISIAK-Tamra (3.5 μM) was determined. A representative titration curve is shown, each point representing a mean of two technical replicates. Final concentration of ADAMTS1 following titration was 10 nM. FL, full-length; No E, no enzyme; No I, no inhibitor; QF, Quenched-Fluorescent; TIMP, tissue inhibitor of metalloproteinase.
Murine Timp1 R D Systems, 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
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recombinant mouse timp 1  (R&D Systems)
86
R&D Systems recombinant mouse timp 1
Schematic illustration of experimental plan for in vitro evaluation of NPs: The Coumarin 6 dye-loaded NPs (Dye NPs) and <t>TIMP-1</t> loaded NPs (TIMP-1 NPs) without Ps80 coating and with Ps80 coating (Dye NPs + Ps80 and TIMP-1 NPs + Ps80) were evaluated in vitro. The NPs were evaluated using a rat brain endothelial cell line (RBE4) and primary rat brain capillary endothelial cells (RBCEC) co-cultured with glial cells. The NPs were evaluated for toxicity, uptake/binding and penetration. For toxicity studies, LDH assay, LY assay, and ZO1 (tight junction marker) immunocytochemistry were performed. The uptake and binding studies were done on RBCEC. For penetration studies, fluorescence spectrophotometry was used for dye-loaded NPs and ELISA for TIMP-1 NPs. Abbreviations: NPs, nanoparticles; TIMP, <t>tissue</t> <t>inhibitor</t> of matrix metalloproteinases; Ps80, polysorbate 80; LDH, lactate dehydrogenase; LY, Lucifer yellow; ELISA, enzyme-linked immunosorbent assay; immuno, immunocytochemistry; RBE4, rat brain endothelial cell line; RBCEC, rat brain capillary endothelial cells; ZO1, zona occludens 1.
Recombinant Mouse Timp 1, supplied by R&D Systems, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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recombinant protein timp 1  (ProSci Incorporated)
94
ProSci Incorporated recombinant protein timp 1
Schematic illustration of experimental plan for in vitro evaluation of NPs: The Coumarin 6 dye-loaded NPs (Dye NPs) and <t>TIMP-1</t> loaded NPs (TIMP-1 NPs) without Ps80 coating and with Ps80 coating (Dye NPs + Ps80 and TIMP-1 NPs + Ps80) were evaluated in vitro. The NPs were evaluated using a rat brain endothelial cell line (RBE4) and primary rat brain capillary endothelial cells (RBCEC) co-cultured with glial cells. The NPs were evaluated for toxicity, uptake/binding and penetration. For toxicity studies, LDH assay, LY assay, and ZO1 (tight junction marker) immunocytochemistry were performed. The uptake and binding studies were done on RBCEC. For penetration studies, fluorescence spectrophotometry was used for dye-loaded NPs and ELISA for TIMP-1 NPs. Abbreviations: NPs, nanoparticles; TIMP, <t>tissue</t> <t>inhibitor</t> of matrix metalloproteinases; Ps80, polysorbate 80; LDH, lactate dehydrogenase; LY, Lucifer yellow; ELISA, enzyme-linked immunosorbent assay; immuno, immunocytochemistry; RBE4, rat brain endothelial cell line; RBCEC, rat brain capillary endothelial cells; ZO1, zona occludens 1.
Recombinant Protein Timp 1, supplied by ProSci Incorporated, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


Figure 2. Inhibition of ADAMTS1 by TIMPs. A, inhibition of versicanase activity by TIMP family members. TIMP1, TIMP2, TIMP3, and TIMP4 (each at 500 nM) were incubated with ADAMTS1 (100 nM) for 1 h at 37 C before addition of V1-5GAG and digestion for 2 h. Following SDS-PAGE under reducing conditions (5% β-mercaptoethanol) and immunoblotting, FL V1-5GAG and versikine (VSK) were detected by the anti-Vc antibody. A representative immunoblot is shown (n = 2 independent experiments). B, inhibition of peptidolytic activity. TIMPs (each 25 nM) were incubated with a nominal con- centration of 25 nM ADAMTS1 for 1 h at 37 C before addition of the QF peptide substrate fluorescein-5(6)-carbonyl-Ala-Glu-Leu-Asn-Gly-Arg-Pro-Ile-Ser-Ile- Ala-Lys (5(6)-TAMRA) (3.5 μM) and digestion for 2 h. Following subtraction of the background (reactions not containing ADAMTS1), values were converted into percentage of ADAMTS1 activity in the absence of TIMPs and reported as average ± SD (n = 3, each point representing a technical replicate), p < 0.05 by Mann-Whitney test. C, titration of ADAMTS1 with TIMP3. TIMP3 (0–16 nM) was incubated with ADAMTS1 (20 nM nominal concentration) at 37 C for 1 h, and residual activity against the QF peptide FAM-AELNGRPISIAK-Tamra (3.5 μM) was determined. A representative titration curve is shown, each point representing a mean of two technical replicates. Final concentration of ADAMTS1 following titration was 10 nM. FL, full-length; No E, no enzyme; No I, no inhibitor; QF, Quenched-Fluorescent; TIMP, tissue inhibitor of metalloproteinase.

Journal: The Journal of biological chemistry

Article Title: The C-terminal domains of ADAMTS1 contain exosites involved in its proteoglycanase activity.

doi: 10.1016/j.jbc.2023.103048

Figure Lengend Snippet: Figure 2. Inhibition of ADAMTS1 by TIMPs. A, inhibition of versicanase activity by TIMP family members. TIMP1, TIMP2, TIMP3, and TIMP4 (each at 500 nM) were incubated with ADAMTS1 (100 nM) for 1 h at 37 C before addition of V1-5GAG and digestion for 2 h. Following SDS-PAGE under reducing conditions (5% β-mercaptoethanol) and immunoblotting, FL V1-5GAG and versikine (VSK) were detected by the anti-Vc antibody. A representative immunoblot is shown (n = 2 independent experiments). B, inhibition of peptidolytic activity. TIMPs (each 25 nM) were incubated with a nominal con- centration of 25 nM ADAMTS1 for 1 h at 37 C before addition of the QF peptide substrate fluorescein-5(6)-carbonyl-Ala-Glu-Leu-Asn-Gly-Arg-Pro-Ile-Ser-Ile- Ala-Lys (5(6)-TAMRA) (3.5 μM) and digestion for 2 h. Following subtraction of the background (reactions not containing ADAMTS1), values were converted into percentage of ADAMTS1 activity in the absence of TIMPs and reported as average ± SD (n = 3, each point representing a technical replicate), p < 0.05 by Mann-Whitney test. C, titration of ADAMTS1 with TIMP3. TIMP3 (0–16 nM) was incubated with ADAMTS1 (20 nM nominal concentration) at 37 C for 1 h, and residual activity against the QF peptide FAM-AELNGRPISIAK-Tamra (3.5 μM) was determined. A representative titration curve is shown, each point representing a mean of two technical replicates. Final concentration of ADAMTS1 following titration was 10 nM. FL, full-length; No E, no enzyme; No I, no inhibitor; QF, Quenched-Fluorescent; TIMP, tissue inhibitor of metalloproteinase.

Article Snippet: Semiquantitative proteoglycan cleavage assays Purified V1-5GAG (100 nM) was digested with ADAMTS1, in TNC-B buffer at 37 C for 2 h. Where indicated, 500 μM recombinant human TIMP1, TIMP2, TIMP3, or TIMP4 (R&D Systems, Cat. n.: 970-TM, 971-TM, 973-TM, 974-TSF) were preincubated with 100 nM ADAMTS1 for 1 h at 37 C before digestion.

Techniques: Inhibition, Activity Assay, Incubation, SDS Page, Western Blot, MANN-WHITNEY, Titration, Concentration Assay

Schematic illustration of experimental plan for in vitro evaluation of NPs: The Coumarin 6 dye-loaded NPs (Dye NPs) and TIMP-1 loaded NPs (TIMP-1 NPs) without Ps80 coating and with Ps80 coating (Dye NPs + Ps80 and TIMP-1 NPs + Ps80) were evaluated in vitro. The NPs were evaluated using a rat brain endothelial cell line (RBE4) and primary rat brain capillary endothelial cells (RBCEC) co-cultured with glial cells. The NPs were evaluated for toxicity, uptake/binding and penetration. For toxicity studies, LDH assay, LY assay, and ZO1 (tight junction marker) immunocytochemistry were performed. The uptake and binding studies were done on RBCEC. For penetration studies, fluorescence spectrophotometry was used for dye-loaded NPs and ELISA for TIMP-1 NPs. Abbreviations: NPs, nanoparticles; TIMP, tissue inhibitor of matrix metalloproteinases; Ps80, polysorbate 80; LDH, lactate dehydrogenase; LY, Lucifer yellow; ELISA, enzyme-linked immunosorbent assay; immuno, immunocytochemistry; RBE4, rat brain endothelial cell line; RBCEC, rat brain capillary endothelial cells; ZO1, zona occludens 1.

Journal: International Journal of Nanomedicine

Article Title: Tissue inhibitor of matrix metalloproteinases-1 loaded poly(lactic-co-glycolic acid) nanoparticles for delivery across the blood–brain barrier

doi: 10.2147/IJN.S54750

Figure Lengend Snippet: Schematic illustration of experimental plan for in vitro evaluation of NPs: The Coumarin 6 dye-loaded NPs (Dye NPs) and TIMP-1 loaded NPs (TIMP-1 NPs) without Ps80 coating and with Ps80 coating (Dye NPs + Ps80 and TIMP-1 NPs + Ps80) were evaluated in vitro. The NPs were evaluated using a rat brain endothelial cell line (RBE4) and primary rat brain capillary endothelial cells (RBCEC) co-cultured with glial cells. The NPs were evaluated for toxicity, uptake/binding and penetration. For toxicity studies, LDH assay, LY assay, and ZO1 (tight junction marker) immunocytochemistry were performed. The uptake and binding studies were done on RBCEC. For penetration studies, fluorescence spectrophotometry was used for dye-loaded NPs and ELISA for TIMP-1 NPs. Abbreviations: NPs, nanoparticles; TIMP, tissue inhibitor of matrix metalloproteinases; Ps80, polysorbate 80; LDH, lactate dehydrogenase; LY, Lucifer yellow; ELISA, enzyme-linked immunosorbent assay; immuno, immunocytochemistry; RBE4, rat brain endothelial cell line; RBCEC, rat brain capillary endothelial cells; ZO1, zona occludens 1.

Article Snippet: Recombinant mouse TIMP-1 with a 6× Histag (WBC022; R&D Systems) was used as a standard for both Western blots.

Techniques: In Vitro, Cell Culture, Binding Assay, Lactate Dehydrogenase Assay, Marker, Immunocytochemistry, Fluorescence, Spectrophotometry, Enzyme-linked Immunosorbent Assay

Formulation optimization. Abbreviations: TIMP, tissue inhibitor of matrix metalloproteinases; PLGA, poly(lactic-co-glycolic acid); PDI, polydispersity index.

Journal: International Journal of Nanomedicine

Article Title: Tissue inhibitor of matrix metalloproteinases-1 loaded poly(lactic-co-glycolic acid) nanoparticles for delivery across the blood–brain barrier

doi: 10.2147/IJN.S54750

Figure Lengend Snippet: Formulation optimization. Abbreviations: TIMP, tissue inhibitor of matrix metalloproteinases; PLGA, poly(lactic-co-glycolic acid); PDI, polydispersity index.

Article Snippet: Recombinant mouse TIMP-1 with a 6× Histag (WBC022; R&D Systems) was used as a standard for both Western blots.

Techniques: Formulation

( A – C ) Characterization results of PLGA3 NPs loaded with TIMP-1. ( A ) Representative scanning electron micrograph of TIMP-1-loaded PLGA NPs. ( B ) Representative transmission electron micrograph of TIMP-1-loaded PLGA NPs; scale bar 500 nm. ( C ) Particle-size analysis by dynamic light scattering. Abbreviations: NPs, nanoparticles; TIMP, tissue inhibitor of matrix metalloproteinases; PLGA, poly(lactic-co-glycolic acid).

Journal: International Journal of Nanomedicine

Article Title: Tissue inhibitor of matrix metalloproteinases-1 loaded poly(lactic-co-glycolic acid) nanoparticles for delivery across the blood–brain barrier

doi: 10.2147/IJN.S54750

Figure Lengend Snippet: ( A – C ) Characterization results of PLGA3 NPs loaded with TIMP-1. ( A ) Representative scanning electron micrograph of TIMP-1-loaded PLGA NPs. ( B ) Representative transmission electron micrograph of TIMP-1-loaded PLGA NPs; scale bar 500 nm. ( C ) Particle-size analysis by dynamic light scattering. Abbreviations: NPs, nanoparticles; TIMP, tissue inhibitor of matrix metalloproteinases; PLGA, poly(lactic-co-glycolic acid).

Article Snippet: Recombinant mouse TIMP-1 with a 6× Histag (WBC022; R&D Systems) was used as a standard for both Western blots.

Techniques: Transmission Assay, Particle Size Analysis

TIMP-1 release and stability: release of TIMP-1 from optimal PLGA3 NPs under in vitro conditions. Inset is representative Western blot of the protein released from the NPs, suggesting that release of TIMP-1 is stable after 48 hours. Data are means ± standard error of mean; n=3. Abbreviations: NPs, nanoparticles; TIMP, tissue inhibitor of matrix metalloproteinases; PLGA, poly(lactic-co-glycolic acid); Std, standard.

Journal: International Journal of Nanomedicine

Article Title: Tissue inhibitor of matrix metalloproteinases-1 loaded poly(lactic-co-glycolic acid) nanoparticles for delivery across the blood–brain barrier

doi: 10.2147/IJN.S54750

Figure Lengend Snippet: TIMP-1 release and stability: release of TIMP-1 from optimal PLGA3 NPs under in vitro conditions. Inset is representative Western blot of the protein released from the NPs, suggesting that release of TIMP-1 is stable after 48 hours. Data are means ± standard error of mean; n=3. Abbreviations: NPs, nanoparticles; TIMP, tissue inhibitor of matrix metalloproteinases; PLGA, poly(lactic-co-glycolic acid); Std, standard.

Article Snippet: Recombinant mouse TIMP-1 with a 6× Histag (WBC022; R&D Systems) was used as a standard for both Western blots.

Techniques: In Vitro, Western Blot

( A – C ) Toxicity studies. ( A ) LY assay on RBCEC, showing no significant impact of NPs on endothelial cell permeability for LY compared to control (no NPs), indicating that NPs caused no significant opening of the endothelial cell monolayer. Ps80 alone and TIMP-1 alone were used as controls. ( B ) LDH assay, also showing that NPs were not toxic to the RBCEC compared to control. Ps80 alone and TIMP-1 alone were used as controls. ( C ) Representative fluorescence photomicrographs of ZO1 immunocytochemistry on RBCEC treated with TIMP-1 NPs and TIMP-1 NPs + Ps80, indicating no significant difference between the groups. Note: Values represent means ± standard error of mean of three independent experiments. Abbreviations: LY, Lucifer yellow; RBCEC, primary rat brain capillary endothelial cells; NPs, nanoparticles; TIMP, tissue inhibitor of matrix metalloproteinases; Ps80, polysorbate 80; LDH, lactate dehydrogenase; LY, Lucifer yellow.

Journal: International Journal of Nanomedicine

Article Title: Tissue inhibitor of matrix metalloproteinases-1 loaded poly(lactic-co-glycolic acid) nanoparticles for delivery across the blood–brain barrier

doi: 10.2147/IJN.S54750

Figure Lengend Snippet: ( A – C ) Toxicity studies. ( A ) LY assay on RBCEC, showing no significant impact of NPs on endothelial cell permeability for LY compared to control (no NPs), indicating that NPs caused no significant opening of the endothelial cell monolayer. Ps80 alone and TIMP-1 alone were used as controls. ( B ) LDH assay, also showing that NPs were not toxic to the RBCEC compared to control. Ps80 alone and TIMP-1 alone were used as controls. ( C ) Representative fluorescence photomicrographs of ZO1 immunocytochemistry on RBCEC treated with TIMP-1 NPs and TIMP-1 NPs + Ps80, indicating no significant difference between the groups. Note: Values represent means ± standard error of mean of three independent experiments. Abbreviations: LY, Lucifer yellow; RBCEC, primary rat brain capillary endothelial cells; NPs, nanoparticles; TIMP, tissue inhibitor of matrix metalloproteinases; Ps80, polysorbate 80; LDH, lactate dehydrogenase; LY, Lucifer yellow.

Article Snippet: Recombinant mouse TIMP-1 with a 6× Histag (WBC022; R&D Systems) was used as a standard for both Western blots.

Techniques: Permeability, Lactate Dehydrogenase Assay, Fluorescence, Immunocytochemistry

In vitro blood–brain barrier penetration. Notes: (A ) Spectrophotometric assay suggests that Coumarin 6 dye-loaded NPs (Dye NPs) + Ps80 (coated with Ps80) had higher penetration, while uncoated Dye NPs did not cross the cell monolayer. Values represent means ± standard error of mean of three independent experiments, where asterisk represents P <0.05 versus group with Dye NPs + Ps80 (40 ug/mL). ( B ) For TIMP-1-loaded NPs, a TIMP-1 ELISA showed that TIMP-1 NPs + Ps80 (coated with Ps80) had much higher penetration compared to TIMP-1 NPs (uncoated NPs). Moreover, the penetration was time-dependent. After 120 minutes, there was a higher amount of TIMP-1 detected in the lower compartment compared to 30 minutes. Values represent mean ± standard error of mean of three independent experiments, where asterisks represent P <0.05 versus group with TIMP-1 NPs after 120 min of incubation and # P <0.05 versus group with TIMP-1 NPs + Ps80 after 30 minutes. Abbreviations: NPs, nanoparticles; Ps80, polysorbate 80; TIMP, tissue inhibitor of matrix metalloproteinases; ELISA, enzyme-linked immunosorbent assay.

Journal: International Journal of Nanomedicine

Article Title: Tissue inhibitor of matrix metalloproteinases-1 loaded poly(lactic-co-glycolic acid) nanoparticles for delivery across the blood–brain barrier

doi: 10.2147/IJN.S54750

Figure Lengend Snippet: In vitro blood–brain barrier penetration. Notes: (A ) Spectrophotometric assay suggests that Coumarin 6 dye-loaded NPs (Dye NPs) + Ps80 (coated with Ps80) had higher penetration, while uncoated Dye NPs did not cross the cell monolayer. Values represent means ± standard error of mean of three independent experiments, where asterisk represents P <0.05 versus group with Dye NPs + Ps80 (40 ug/mL). ( B ) For TIMP-1-loaded NPs, a TIMP-1 ELISA showed that TIMP-1 NPs + Ps80 (coated with Ps80) had much higher penetration compared to TIMP-1 NPs (uncoated NPs). Moreover, the penetration was time-dependent. After 120 minutes, there was a higher amount of TIMP-1 detected in the lower compartment compared to 30 minutes. Values represent mean ± standard error of mean of three independent experiments, where asterisks represent P <0.05 versus group with TIMP-1 NPs after 120 min of incubation and # P <0.05 versus group with TIMP-1 NPs + Ps80 after 30 minutes. Abbreviations: NPs, nanoparticles; Ps80, polysorbate 80; TIMP, tissue inhibitor of matrix metalloproteinases; ELISA, enzyme-linked immunosorbent assay.

Article Snippet: Recombinant mouse TIMP-1 with a 6× Histag (WBC022; R&D Systems) was used as a standard for both Western blots.

Techniques: In Vitro, Spectrophotometric Assay, Enzyme-linked Immunosorbent Assay, Incubation

In vivo blood–brain barrier (BBB) penetration. Notes: Representative fluorescence photomicrographs of immunohistochemistry on brain sections, of the specified area (marked with orange box) using a 6× Histag antibody to detect the TIMP-1-Histag fusion protein. The nucleus was labeled with DAPI. The TIMP-1 NPs + Ps80 group shows labeling indicating BBB penetration of TIMP-1 NPs + Ps80 as indicated by white arrows. Abbreviations: TIMP, tissue inhibitor of matrix metalloproteinases; DAPI, 4′,6-diamidino-2-phenylindole; NPs, nanoparticles; Ps80, polysorbate 80; PBS, phosphate-buffered saline.

Journal: International Journal of Nanomedicine

Article Title: Tissue inhibitor of matrix metalloproteinases-1 loaded poly(lactic-co-glycolic acid) nanoparticles for delivery across the blood–brain barrier

doi: 10.2147/IJN.S54750

Figure Lengend Snippet: In vivo blood–brain barrier (BBB) penetration. Notes: Representative fluorescence photomicrographs of immunohistochemistry on brain sections, of the specified area (marked with orange box) using a 6× Histag antibody to detect the TIMP-1-Histag fusion protein. The nucleus was labeled with DAPI. The TIMP-1 NPs + Ps80 group shows labeling indicating BBB penetration of TIMP-1 NPs + Ps80 as indicated by white arrows. Abbreviations: TIMP, tissue inhibitor of matrix metalloproteinases; DAPI, 4′,6-diamidino-2-phenylindole; NPs, nanoparticles; Ps80, polysorbate 80; PBS, phosphate-buffered saline.

Article Snippet: Recombinant mouse TIMP-1 with a 6× Histag (WBC022; R&D Systems) was used as a standard for both Western blots.

Techniques: In Vivo, Fluorescence, Immunohistochemistry, Labeling, Saline