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aavpro purification kit aav2  (TaKaRa)


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    Structured Review

    TaKaRa aavpro purification kit aav2
    ( a ) <t>AAV2</t> expressing LIMK2-inactive (IA)-mutant-GFP and AAV2 expressing GFP (control) were used to infect normal HDFs. Expression levels of LIMK2 and GFP were analyzed by Western blotting. The original blots are presented in Supplementary Fig. 7. ( b ) Decreased baseline cofilin phosphorylation 48 h after LIMK2-IA-mutant-GFP infection. In HDFs and GFP-HDFs (both controls), mechanical stimulation for 30 min increased p-cofilin levels, whereas in LIMK2-IA-mutant-GFP-HDFs, p-cofilin levels remained unchanged. ( c ) In LIMK2-IA-mutant-GFP-HDFs, α-SMA expression was not changed at 24 h after mechanical stimulation. In contrast, in HDFs and GFP-HDFs, α-SMA expression was significantly increased by mechanical stimulation. ( d ) LIMK2 activation increased, whereas LIMK2 inactivation decreased, cofilin phosphorylation in HDFs and KDFs. ( e ) LIMK2 activation increased α-SMA expression in both HDFs and KDFs, whereas LIMK2 inactivation decreased α-SMA expression only in KDFs. ( f ) LIMK2 activation increased, whereas LIMK2 inactivation decreased, collagen type I expression in HDFs and KDFs. ** p < 0.01. * p < 0.05. ## p < 0.01 vs HDFs and GFP-HDFs. The original blots are presented in Supplementary Figs. 8, 9, 10, 11 and 12.
    Aavpro Purification Kit Aav2, supplied by TaKaRa, used in various techniques. Bioz Stars score: 96/100, based on 304 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/aavpro+purification+kit+aav2/AAVpro+Purification+Kit/pmc12929562-193-10-14
    Average 96 stars, based on 304 article reviews
    aavpro purification kit aav2 - by Bioz Stars, 2026-09
    96/100 stars

    Images

    1) Product Images from "LIMK2 inactivation suppresses mechanical stimulation-induced dermal fibroblast differentiation and resistance to apoptosis"

    Article Title: LIMK2 inactivation suppresses mechanical stimulation-induced dermal fibroblast differentiation and resistance to apoptosis

    Journal: Scientific Reports

    doi: 10.1038/s41598-026-37610-y

    ( a ) AAV2 expressing LIMK2-inactive (IA)-mutant-GFP and AAV2 expressing GFP (control) were used to infect normal HDFs. Expression levels of LIMK2 and GFP were analyzed by Western blotting. The original blots are presented in Supplementary Fig. 7. ( b ) Decreased baseline cofilin phosphorylation 48 h after LIMK2-IA-mutant-GFP infection. In HDFs and GFP-HDFs (both controls), mechanical stimulation for 30 min increased p-cofilin levels, whereas in LIMK2-IA-mutant-GFP-HDFs, p-cofilin levels remained unchanged. ( c ) In LIMK2-IA-mutant-GFP-HDFs, α-SMA expression was not changed at 24 h after mechanical stimulation. In contrast, in HDFs and GFP-HDFs, α-SMA expression was significantly increased by mechanical stimulation. ( d ) LIMK2 activation increased, whereas LIMK2 inactivation decreased, cofilin phosphorylation in HDFs and KDFs. ( e ) LIMK2 activation increased α-SMA expression in both HDFs and KDFs, whereas LIMK2 inactivation decreased α-SMA expression only in KDFs. ( f ) LIMK2 activation increased, whereas LIMK2 inactivation decreased, collagen type I expression in HDFs and KDFs. ** p < 0.01. * p < 0.05. ## p < 0.01 vs HDFs and GFP-HDFs. The original blots are presented in Supplementary Figs. 8, 9, 10, 11 and 12.
    Figure Legend Snippet: ( a ) AAV2 expressing LIMK2-inactive (IA)-mutant-GFP and AAV2 expressing GFP (control) were used to infect normal HDFs. Expression levels of LIMK2 and GFP were analyzed by Western blotting. The original blots are presented in Supplementary Fig. 7. ( b ) Decreased baseline cofilin phosphorylation 48 h after LIMK2-IA-mutant-GFP infection. In HDFs and GFP-HDFs (both controls), mechanical stimulation for 30 min increased p-cofilin levels, whereas in LIMK2-IA-mutant-GFP-HDFs, p-cofilin levels remained unchanged. ( c ) In LIMK2-IA-mutant-GFP-HDFs, α-SMA expression was not changed at 24 h after mechanical stimulation. In contrast, in HDFs and GFP-HDFs, α-SMA expression was significantly increased by mechanical stimulation. ( d ) LIMK2 activation increased, whereas LIMK2 inactivation decreased, cofilin phosphorylation in HDFs and KDFs. ( e ) LIMK2 activation increased α-SMA expression in both HDFs and KDFs, whereas LIMK2 inactivation decreased α-SMA expression only in KDFs. ( f ) LIMK2 activation increased, whereas LIMK2 inactivation decreased, collagen type I expression in HDFs and KDFs. ** p < 0.01. * p < 0.05. ## p < 0.01 vs HDFs and GFP-HDFs. The original blots are presented in Supplementary Figs. 8, 9, 10, 11 and 12.

    Techniques Used: Expressing, Mutagenesis, Control, Western Blot, Phospho-proteomics, Infection, Activation Assay

    Related Articles

    Purification:

    Article Title: LIMK2 inactivation suppresses mechanical stimulation-induced dermal fibroblast differentiation and resistance to apoptosis.
    Article Snippet: .. AR TIC LE IN PR ES S ARTICLE IN PRESS was purified using the AAVpro® Purification Kit (AAV2) (Takara Bio). ..

    Article Title: Improved Intravitreal AAV-Mediated Inner Retinal Gene Transduction after Surgical Internal Limiting Membrane Peeling in Cynomolgus Monkeys
    Article Snippet: .. 11 , 23 The AAV vector particles were harvested from the transfected cells using an AAVpro Purification Kit (AAV2) (TakaRa Bio) according to the manufacturer’s instructions. .. Thereafter, the buffer containing the AAV vector was changed to PBS (−) using an Amicon Ultra-15 Centrifugal Filter Unit (molecular weight cutoff, 30 kDa) (Merck Millipore), which was centrifuged for 5 min at 5,000 × g . The particle titers of the AAV vector were determined by qPCR analysis using a 7500 Fast Real-Time PCR Instrument (Applied Biosystems).

    Article Title: Altered actin dynamics is possibly implicated in the inhibition of mechanical stimulation-induced dermal fibroblast differentiation into myofibroblasts.
    Article Snippet: © 2023 John Wiley & Sons A/S.. Published by John Wiley & Sons Ltd. Kazuya Kuroda and Koichiro Kiya contributed equally to this work.. 1Department of Plastic Surgery, Osaka University Graduate School of Medicine, Osaka, Japan 2Department of Child Development and Molecular Brain Science, United Graduate School of Child Development, Osaka University, Osaka, Japan 3Department of Radiological Sciences, Faculty of Medical Science Technology, Morinomiya University of Medical Sciences, Osaka, Japan 4Department of Plastic Surgery, Hyogo College of Medicine, Nishinomiya, Japan 5Department of Plastic and Reconstructive Surgery, University of Fukui Hospital, Fukui, Japan 6Inclusive Medical Science Research Institute, Morinomiya University of Medical Sciences, Osaka, Japan

    Article Title: LIMK2 inactivation suppresses mechanical stimulation-induced dermal fibroblast differentiation and resistance to apoptosis
    Article Snippet: HEK293 cells were transfected with pRC2-mi342 vector and pHelper vector (Takara Bio) in conjunction with either the pAAV-CMV-LIMK2-IA-mutant-GFP vector, the pAAV-CMV-LIMK2-A-mutant-GFP vector, or the pAAV-CMV-GFP vector. .. After 72 h, each AAV2 vector was purified using the AAVpro® Purification Kit (AAV2) (Takara Bio). ..

    Bioprocessing:

    Article Title: Improved Intravitreal AAV-Mediated Inner Retinal Gene Transduction after Surgical Internal Limiting Membrane Peeling in Cynomolgus Monkeys
    Article Snippet: .. 11 , 23 The AAV vector particles were harvested from the transfected cells using an AAVpro Purification Kit (AAV2) (TakaRa Bio) according to the manufacturer’s instructions. .. Thereafter, the buffer containing the AAV vector was changed to PBS (−) using an Amicon Ultra-15 Centrifugal Filter Unit (molecular weight cutoff, 30 kDa) (Merck Millipore), which was centrifuged for 5 min at 5,000 × g . The particle titers of the AAV vector were determined by qPCR analysis using a 7500 Fast Real-Time PCR Instrument (Applied Biosystems).

    Article Title: Altered actin dynamics is possibly implicated in the inhibition of mechanical stimulation-induced dermal fibroblast differentiation into myofibroblasts.
    Article Snippet: © 2023 John Wiley & Sons A/S.. Published by John Wiley & Sons Ltd. Kazuya Kuroda and Koichiro Kiya contributed equally to this work.. 1Department of Plastic Surgery, Osaka University Graduate School of Medicine, Osaka, Japan 2Department of Child Development and Molecular Brain Science, United Graduate School of Child Development, Osaka University, Osaka, Japan 3Department of Radiological Sciences, Faculty of Medical Science Technology, Morinomiya University of Medical Sciences, Osaka, Japan 4Department of Plastic Surgery, Hyogo College of Medicine, Nishinomiya, Japan 5Department of Plastic and Reconstructive Surgery, University of Fukui Hospital, Fukui, Japan 6Inclusive Medical Science Research Institute, Morinomiya University of Medical Sciences, Osaka, Japan

    Plasmid Preparation:

    Article Title: Improved Intravitreal AAV-Mediated Inner Retinal Gene Transduction after Surgical Internal Limiting Membrane Peeling in Cynomolgus Monkeys
    Article Snippet: .. 11 , 23 The AAV vector particles were harvested from the transfected cells using an AAVpro Purification Kit (AAV2) (TakaRa Bio) according to the manufacturer’s instructions. .. Thereafter, the buffer containing the AAV vector was changed to PBS (−) using an Amicon Ultra-15 Centrifugal Filter Unit (molecular weight cutoff, 30 kDa) (Merck Millipore), which was centrifuged for 5 min at 5,000 × g . The particle titers of the AAV vector were determined by qPCR analysis using a 7500 Fast Real-Time PCR Instrument (Applied Biosystems).

    Article Title: LIMK2 inactivation suppresses mechanical stimulation-induced dermal fibroblast differentiation and resistance to apoptosis
    Article Snippet: HEK293 cells were transfected with pRC2-mi342 vector and pHelper vector (Takara Bio) in conjunction with either the pAAV-CMV-LIMK2-IA-mutant-GFP vector, the pAAV-CMV-LIMK2-A-mutant-GFP vector, or the pAAV-CMV-GFP vector. .. After 72 h, each AAV2 vector was purified using the AAVpro® Purification Kit (AAV2) (Takara Bio). ..

    Transfection:

    Article Title: Improved Intravitreal AAV-Mediated Inner Retinal Gene Transduction after Surgical Internal Limiting Membrane Peeling in Cynomolgus Monkeys
    Article Snippet: .. 11 , 23 The AAV vector particles were harvested from the transfected cells using an AAVpro Purification Kit (AAV2) (TakaRa Bio) according to the manufacturer’s instructions. .. Thereafter, the buffer containing the AAV vector was changed to PBS (−) using an Amicon Ultra-15 Centrifugal Filter Unit (molecular weight cutoff, 30 kDa) (Merck Millipore), which was centrifuged for 5 min at 5,000 × g . The particle titers of the AAV vector were determined by qPCR analysis using a 7500 Fast Real-Time PCR Instrument (Applied Biosystems).

    Article Title: Altered actin dynamics is possibly implicated in the inhibition of mechanical stimulation-induced dermal fibroblast differentiation into myofibroblasts.
    Article Snippet: © 2023 John Wiley & Sons A/S.. Published by John Wiley & Sons Ltd. Kazuya Kuroda and Koichiro Kiya contributed equally to this work.. 1Department of Plastic Surgery, Osaka University Graduate School of Medicine, Osaka, Japan 2Department of Child Development and Molecular Brain Science, United Graduate School of Child Development, Osaka University, Osaka, Japan 3Department of Radiological Sciences, Faculty of Medical Science Technology, Morinomiya University of Medical Sciences, Osaka, Japan 4Department of Plastic Surgery, Hyogo College of Medicine, Nishinomiya, Japan 5Department of Plastic and Reconstructive Surgery, University of Fukui Hospital, Fukui, Japan 6Inclusive Medical Science Research Institute, Morinomiya University of Medical Sciences, Osaka, Japan

    Expressing:

    Article Title: Altered actin dynamics is possibly implicated in the inhibition of mechanical stimulation-induced dermal fibroblast differentiation into myofibroblasts.
    Article Snippet: © 2023 John Wiley & Sons A/S.. Published by John Wiley & Sons Ltd. Kazuya Kuroda and Koichiro Kiya contributed equally to this work.. 1Department of Plastic Surgery, Osaka University Graduate School of Medicine, Osaka, Japan 2Department of Child Development and Molecular Brain Science, United Graduate School of Child Development, Osaka University, Osaka, Japan 3Department of Radiological Sciences, Faculty of Medical Science Technology, Morinomiya University of Medical Sciences, Osaka, Japan 4Department of Plastic Surgery, Hyogo College of Medicine, Nishinomiya, Japan 5Department of Plastic and Reconstructive Surgery, University of Fukui Hospital, Fukui, Japan 6Inclusive Medical Science Research Institute, Morinomiya University of Medical Sciences, Osaka, Japan

    Virus:

    Article Title: Altered actin dynamics is possibly implicated in the inhibition of mechanical stimulation-induced dermal fibroblast differentiation into myofibroblasts.
    Article Snippet: © 2023 John Wiley & Sons A/S.. Published by John Wiley & Sons Ltd. Kazuya Kuroda and Koichiro Kiya contributed equally to this work.. 1Department of Plastic Surgery, Osaka University Graduate School of Medicine, Osaka, Japan 2Department of Child Development and Molecular Brain Science, United Graduate School of Child Development, Osaka University, Osaka, Japan 3Department of Radiological Sciences, Faculty of Medical Science Technology, Morinomiya University of Medical Sciences, Osaka, Japan 4Department of Plastic Surgery, Hyogo College of Medicine, Nishinomiya, Japan 5Department of Plastic and Reconstructive Surgery, University of Fukui Hospital, Fukui, Japan 6Inclusive Medical Science Research Institute, Morinomiya University of Medical Sciences, Osaka, Japan

    Mutagenesis:

    Article Title: Altered actin dynamics is possibly implicated in the inhibition of mechanical stimulation-induced dermal fibroblast differentiation into myofibroblasts.
    Article Snippet: © 2023 John Wiley & Sons A/S.. Published by John Wiley & Sons Ltd. Kazuya Kuroda and Koichiro Kiya contributed equally to this work.. 1Department of Plastic Surgery, Osaka University Graduate School of Medicine, Osaka, Japan 2Department of Child Development and Molecular Brain Science, United Graduate School of Child Development, Osaka University, Osaka, Japan 3Department of Radiological Sciences, Faculty of Medical Science Technology, Morinomiya University of Medical Sciences, Osaka, Japan 4Department of Plastic Surgery, Hyogo College of Medicine, Nishinomiya, Japan 5Department of Plastic and Reconstructive Surgery, University of Fukui Hospital, Fukui, Japan 6Inclusive Medical Science Research Institute, Morinomiya University of Medical Sciences, Osaka, Japan



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    ( a ) <t>AAV2</t> expressing LIMK2-inactive (IA)-mutant-GFP and AAV2 expressing GFP (control) were used to infect normal HDFs. Expression levels of LIMK2 and GFP were analyzed by Western blotting. The original blots are presented in Supplementary Fig. 7. ( b ) Decreased baseline cofilin phosphorylation 48 h after LIMK2-IA-mutant-GFP infection. In HDFs and GFP-HDFs (both controls), mechanical stimulation for 30 min increased p-cofilin levels, whereas in LIMK2-IA-mutant-GFP-HDFs, p-cofilin levels remained unchanged. ( c ) In LIMK2-IA-mutant-GFP-HDFs, α-SMA expression was not changed at 24 h after mechanical stimulation. In contrast, in HDFs and GFP-HDFs, α-SMA expression was significantly increased by mechanical stimulation. ( d ) LIMK2 activation increased, whereas LIMK2 inactivation decreased, cofilin phosphorylation in HDFs and KDFs. ( e ) LIMK2 activation increased α-SMA expression in both HDFs and KDFs, whereas LIMK2 inactivation decreased α-SMA expression only in KDFs. ( f ) LIMK2 activation increased, whereas LIMK2 inactivation decreased, collagen type I expression in HDFs and KDFs. ** p < 0.01. * p < 0.05. ## p < 0.01 vs HDFs and GFP-HDFs. The original blots are presented in Supplementary Figs. 8, 9, 10, 11 and 12.
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    ( a ) <t>AAV2</t> expressing LIMK2-inactive (IA)-mutant-GFP and AAV2 expressing GFP (control) were used to infect normal HDFs. Expression levels of LIMK2 and GFP were analyzed by Western blotting. The original blots are presented in Supplementary Fig. 7. ( b ) Decreased baseline cofilin phosphorylation 48 h after LIMK2-IA-mutant-GFP infection. In HDFs and GFP-HDFs (both controls), mechanical stimulation for 30 min increased p-cofilin levels, whereas in LIMK2-IA-mutant-GFP-HDFs, p-cofilin levels remained unchanged. ( c ) In LIMK2-IA-mutant-GFP-HDFs, α-SMA expression was not changed at 24 h after mechanical stimulation. In contrast, in HDFs and GFP-HDFs, α-SMA expression was significantly increased by mechanical stimulation. ( d ) LIMK2 activation increased, whereas LIMK2 inactivation decreased, cofilin phosphorylation in HDFs and KDFs. ( e ) LIMK2 activation increased α-SMA expression in both HDFs and KDFs, whereas LIMK2 inactivation decreased α-SMA expression only in KDFs. ( f ) LIMK2 activation increased, whereas LIMK2 inactivation decreased, collagen type I expression in HDFs and KDFs. ** p < 0.01. * p < 0.05. ## p < 0.01 vs HDFs and GFP-HDFs. The original blots are presented in Supplementary Figs. 8, 9, 10, 11 and 12.
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    ( a ) <t>AAV2</t> expressing LIMK2-inactive (IA)-mutant-GFP and AAV2 expressing GFP (control) were used to infect normal HDFs. Expression levels of LIMK2 and GFP were analyzed by Western blotting. The original blots are presented in Supplementary Fig. 7. ( b ) Decreased baseline cofilin phosphorylation 48 h after LIMK2-IA-mutant-GFP infection. In HDFs and GFP-HDFs (both controls), mechanical stimulation for 30 min increased p-cofilin levels, whereas in LIMK2-IA-mutant-GFP-HDFs, p-cofilin levels remained unchanged. ( c ) In LIMK2-IA-mutant-GFP-HDFs, α-SMA expression was not changed at 24 h after mechanical stimulation. In contrast, in HDFs and GFP-HDFs, α-SMA expression was significantly increased by mechanical stimulation. ( d ) LIMK2 activation increased, whereas LIMK2 inactivation decreased, cofilin phosphorylation in HDFs and KDFs. ( e ) LIMK2 activation increased α-SMA expression in both HDFs and KDFs, whereas LIMK2 inactivation decreased α-SMA expression only in KDFs. ( f ) LIMK2 activation increased, whereas LIMK2 inactivation decreased, collagen type I expression in HDFs and KDFs. ** p < 0.01. * p < 0.05. ## p < 0.01 vs HDFs and GFP-HDFs. The original blots are presented in Supplementary Figs. 8, 9, 10, 11 and 12.
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    ( a ) <t>AAV2</t> expressing LIMK2-inactive (IA)-mutant-GFP and AAV2 expressing GFP (control) were used to infect normal HDFs. Expression levels of LIMK2 and GFP were analyzed by Western blotting. The original blots are presented in Supplementary Fig. 7. ( b ) Decreased baseline cofilin phosphorylation 48 h after LIMK2-IA-mutant-GFP infection. In HDFs and GFP-HDFs (both controls), mechanical stimulation for 30 min increased p-cofilin levels, whereas in LIMK2-IA-mutant-GFP-HDFs, p-cofilin levels remained unchanged. ( c ) In LIMK2-IA-mutant-GFP-HDFs, α-SMA expression was not changed at 24 h after mechanical stimulation. In contrast, in HDFs and GFP-HDFs, α-SMA expression was significantly increased by mechanical stimulation. ( d ) LIMK2 activation increased, whereas LIMK2 inactivation decreased, cofilin phosphorylation in HDFs and KDFs. ( e ) LIMK2 activation increased α-SMA expression in both HDFs and KDFs, whereas LIMK2 inactivation decreased α-SMA expression only in KDFs. ( f ) LIMK2 activation increased, whereas LIMK2 inactivation decreased, collagen type I expression in HDFs and KDFs. ** p < 0.01. * p < 0.05. ## p < 0.01 vs HDFs and GFP-HDFs. The original blots are presented in Supplementary Figs. 8, 9, 10, 11 and 12.
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    ( a ) <t>AAV2</t> expressing LIMK2-inactive (IA)-mutant-GFP and AAV2 expressing GFP (control) were used to infect normal HDFs. Expression levels of LIMK2 and GFP were analyzed by Western blotting. The original blots are presented in Supplementary Fig. 7. ( b ) Decreased baseline cofilin phosphorylation 48 h after LIMK2-IA-mutant-GFP infection. In HDFs and GFP-HDFs (both controls), mechanical stimulation for 30 min increased p-cofilin levels, whereas in LIMK2-IA-mutant-GFP-HDFs, p-cofilin levels remained unchanged. ( c ) In LIMK2-IA-mutant-GFP-HDFs, α-SMA expression was not changed at 24 h after mechanical stimulation. In contrast, in HDFs and GFP-HDFs, α-SMA expression was significantly increased by mechanical stimulation. ( d ) LIMK2 activation increased, whereas LIMK2 inactivation decreased, cofilin phosphorylation in HDFs and KDFs. ( e ) LIMK2 activation increased α-SMA expression in both HDFs and KDFs, whereas LIMK2 inactivation decreased α-SMA expression only in KDFs. ( f ) LIMK2 activation increased, whereas LIMK2 inactivation decreased, collagen type I expression in HDFs and KDFs. ** p < 0.01. * p < 0.05. ## p < 0.01 vs HDFs and GFP-HDFs. The original blots are presented in Supplementary Figs. 8, 9, 10, 11 and 12.
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    Image Search Results


    ( a ) AAV2 expressing LIMK2-inactive (IA)-mutant-GFP and AAV2 expressing GFP (control) were used to infect normal HDFs. Expression levels of LIMK2 and GFP were analyzed by Western blotting. The original blots are presented in Supplementary Fig. 7. ( b ) Decreased baseline cofilin phosphorylation 48 h after LIMK2-IA-mutant-GFP infection. In HDFs and GFP-HDFs (both controls), mechanical stimulation for 30 min increased p-cofilin levels, whereas in LIMK2-IA-mutant-GFP-HDFs, p-cofilin levels remained unchanged. ( c ) In LIMK2-IA-mutant-GFP-HDFs, α-SMA expression was not changed at 24 h after mechanical stimulation. In contrast, in HDFs and GFP-HDFs, α-SMA expression was significantly increased by mechanical stimulation. ( d ) LIMK2 activation increased, whereas LIMK2 inactivation decreased, cofilin phosphorylation in HDFs and KDFs. ( e ) LIMK2 activation increased α-SMA expression in both HDFs and KDFs, whereas LIMK2 inactivation decreased α-SMA expression only in KDFs. ( f ) LIMK2 activation increased, whereas LIMK2 inactivation decreased, collagen type I expression in HDFs and KDFs. ** p < 0.01. * p < 0.05. ## p < 0.01 vs HDFs and GFP-HDFs. The original blots are presented in Supplementary Figs. 8, 9, 10, 11 and 12.

    Journal: Scientific Reports

    Article Title: LIMK2 inactivation suppresses mechanical stimulation-induced dermal fibroblast differentiation and resistance to apoptosis

    doi: 10.1038/s41598-026-37610-y

    Figure Lengend Snippet: ( a ) AAV2 expressing LIMK2-inactive (IA)-mutant-GFP and AAV2 expressing GFP (control) were used to infect normal HDFs. Expression levels of LIMK2 and GFP were analyzed by Western blotting. The original blots are presented in Supplementary Fig. 7. ( b ) Decreased baseline cofilin phosphorylation 48 h after LIMK2-IA-mutant-GFP infection. In HDFs and GFP-HDFs (both controls), mechanical stimulation for 30 min increased p-cofilin levels, whereas in LIMK2-IA-mutant-GFP-HDFs, p-cofilin levels remained unchanged. ( c ) In LIMK2-IA-mutant-GFP-HDFs, α-SMA expression was not changed at 24 h after mechanical stimulation. In contrast, in HDFs and GFP-HDFs, α-SMA expression was significantly increased by mechanical stimulation. ( d ) LIMK2 activation increased, whereas LIMK2 inactivation decreased, cofilin phosphorylation in HDFs and KDFs. ( e ) LIMK2 activation increased α-SMA expression in both HDFs and KDFs, whereas LIMK2 inactivation decreased α-SMA expression only in KDFs. ( f ) LIMK2 activation increased, whereas LIMK2 inactivation decreased, collagen type I expression in HDFs and KDFs. ** p < 0.01. * p < 0.05. ## p < 0.01 vs HDFs and GFP-HDFs. The original blots are presented in Supplementary Figs. 8, 9, 10, 11 and 12.

    Article Snippet: After 72 h, each AAV2 vector was purified using the AAVpro® Purification Kit (AAV2) (Takara Bio).

    Techniques: Expressing, Mutagenesis, Control, Western Blot, Phospho-proteomics, Infection, Activation Assay