tbst  (Thermo Fisher)


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  • 99
    Name:
    TBST Tris Buffered Saline Tween 20
    Description:
    Dilute to 1X with high purity H20 for a solution consisting of 25mM Tris pH 7 4 3 0mM KCl 140mM NaCl and 0 05 Tween 20
    Catalog Number:
    03500537
    Price:
    None
    Category:
    Lab Reagents and Chemicals
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    Structured Review

    Thermo Fisher tbst
    <t>CPH1</t> migrates differently when overexpressed in E. coli or C. reinhardtii . A, E. coli cells transformed with pCPH101, which contains CPH1 cDNA, were induced with isopropylthio- β -galactoside for 2.5 h and cell extracts were analyzed using SDS-PAGE and stained with Coomassie Brilliant Blue. B, Western blot of E. coli pCPH101 extract before and after induction (left) and C. reinhardtii OxG extracts before and after heat shock (right). Western blots were performed using antibodies directed against CPH1 protein as described except <t>TBST</t> plus 0.3% (v/v) Triton X-100 was used.
    Dilute to 1X with high purity H20 for a solution consisting of 25mM Tris pH 7 4 3 0mM KCl 140mM NaCl and 0 05 Tween 20
    https://www.bioz.com/result/tbst/product/Thermo Fisher
    Average 99 stars, based on 6434 article reviews
    Price from $9.99 to $1999.99
    tbst - by Bioz Stars, 2020-11
    99/100 stars

    Images

    1) Product Images from "The CPH1 Gene of Chlamydomonas reinhardtii Encodes Two Forms of Cryptochrome Whose Levels Are Controlled by Light-Induced Proteolysis 1 Encodes Two Forms of Cryptochrome Whose Levels Are Controlled by Light-Induced Proteolysis 1 [w]"

    Article Title: The CPH1 Gene of Chlamydomonas reinhardtii Encodes Two Forms of Cryptochrome Whose Levels Are Controlled by Light-Induced Proteolysis 1 Encodes Two Forms of Cryptochrome Whose Levels Are Controlled by Light-Induced Proteolysis 1 [w]

    Journal: Plant Physiology

    doi: 10.1104/pp.103.031930

    CPH1 migrates differently when overexpressed in E. coli or C. reinhardtii . A, E. coli cells transformed with pCPH101, which contains CPH1 cDNA, were induced with isopropylthio- β -galactoside for 2.5 h and cell extracts were analyzed using SDS-PAGE and stained with Coomassie Brilliant Blue. B, Western blot of E. coli pCPH101 extract before and after induction (left) and C. reinhardtii OxG extracts before and after heat shock (right). Western blots were performed using antibodies directed against CPH1 protein as described except TBST plus 0.3% (v/v) Triton X-100 was used.
    Figure Legend Snippet: CPH1 migrates differently when overexpressed in E. coli or C. reinhardtii . A, E. coli cells transformed with pCPH101, which contains CPH1 cDNA, were induced with isopropylthio- β -galactoside for 2.5 h and cell extracts were analyzed using SDS-PAGE and stained with Coomassie Brilliant Blue. B, Western blot of E. coli pCPH101 extract before and after induction (left) and C. reinhardtii OxG extracts before and after heat shock (right). Western blots were performed using antibodies directed against CPH1 protein as described except TBST plus 0.3% (v/v) Triton X-100 was used.

    Techniques Used: Transformation Assay, SDS Page, Staining, Western Blot

    2) Product Images from "The CPH1 Gene of Chlamydomonas reinhardtii Encodes Two Forms of Cryptochrome Whose Levels Are Controlled by Light-Induced Proteolysis 1 Encodes Two Forms of Cryptochrome Whose Levels Are Controlled by Light-Induced Proteolysis 1 [w]"

    Article Title: The CPH1 Gene of Chlamydomonas reinhardtii Encodes Two Forms of Cryptochrome Whose Levels Are Controlled by Light-Induced Proteolysis 1 Encodes Two Forms of Cryptochrome Whose Levels Are Controlled by Light-Induced Proteolysis 1 [w]

    Journal: Plant Physiology

    doi: 10.1104/pp.103.031930

    CPH1 migrates differently when overexpressed in E. coli or C. reinhardtii . A, E. coli cells transformed with pCPH101, which contains CPH1 cDNA, were induced with isopropylthio- β -galactoside for 2.5 h and cell extracts were analyzed using SDS-PAGE and stained with Coomassie Brilliant Blue. B, Western blot of E. coli pCPH101 extract before and after induction (left) and C. reinhardtii OxG extracts before and after heat shock (right). Western blots were performed using antibodies directed against CPH1 protein as described except TBST plus 0.3% (v/v) Triton X-100 was used.
    Figure Legend Snippet: CPH1 migrates differently when overexpressed in E. coli or C. reinhardtii . A, E. coli cells transformed with pCPH101, which contains CPH1 cDNA, were induced with isopropylthio- β -galactoside for 2.5 h and cell extracts were analyzed using SDS-PAGE and stained with Coomassie Brilliant Blue. B, Western blot of E. coli pCPH101 extract before and after induction (left) and C. reinhardtii OxG extracts before and after heat shock (right). Western blots were performed using antibodies directed against CPH1 protein as described except TBST plus 0.3% (v/v) Triton X-100 was used.

    Techniques Used: Transformation Assay, SDS Page, Staining, Western Blot

    3) Product Images from "Lentiviral vector-mediated stable expression of sTNFR-Fc in human macrophage and neuronal cells as a potential therapy for neuroAIDS"

    Article Title: Lentiviral vector-mediated stable expression of sTNFR-Fc in human macrophage and neuronal cells as a potential therapy for neuroAIDS

    Journal: Journal of Neuroinflammation

    doi: 10.1186/1742-2094-8-48

    Specific binding of expressed sTNFR-Fc to TNF-α by dot immunoblot assay . One microgram of standard recombinant human TNF-α protein was spotted onto nitrocellular membrane (NCM) and then blocked and incubated with supernatants from normal and transduced cells. After three washes with TBST, a goat-anti-human IgG Fc-HRP conjugate was applied and incubated at RT for 1 h. Specific binding was visualized by color deposition on the NCM following incubation with diaminobenzidine (DAB) substrate. Lanes: HTB-NT = supernatant from non-transduced HTB-11 cells and CHME-NT = supernatant from non-transduced CHME-5 cells used as negative controls; HTB-T = supernatant collected from transduced HTB-11 cells and CHME-T2 = supernatant from transduced CHME-5 cells; and C + = purified recombinant sTNFR-Fc protein as a positive control.
    Figure Legend Snippet: Specific binding of expressed sTNFR-Fc to TNF-α by dot immunoblot assay . One microgram of standard recombinant human TNF-α protein was spotted onto nitrocellular membrane (NCM) and then blocked and incubated with supernatants from normal and transduced cells. After three washes with TBST, a goat-anti-human IgG Fc-HRP conjugate was applied and incubated at RT for 1 h. Specific binding was visualized by color deposition on the NCM following incubation with diaminobenzidine (DAB) substrate. Lanes: HTB-NT = supernatant from non-transduced HTB-11 cells and CHME-NT = supernatant from non-transduced CHME-5 cells used as negative controls; HTB-T = supernatant collected from transduced HTB-11 cells and CHME-T2 = supernatant from transduced CHME-5 cells; and C + = purified recombinant sTNFR-Fc protein as a positive control.

    Techniques Used: Binding Assay, Recombinant, Incubation, Purification, Positive Control

    Specific binding of expressed sTNFR-Fc to TNF-α by dot immunoblot assay . One microgram of standard recombinant human TNF-α protein was spotted onto nitrocellular membrane (NCM) and then blocked and incubated with supernatants from normal and transduced cells. After three washes with TBST, a goat-anti-human IgG Fc-HRP conjugate was applied and incubated at RT for 1 h. Specific binding was visualized by color deposition on the NCM following incubation with diaminobenzidine (DAB) substrate. Lanes: HTB-NT = supernatant from non-transduced HTB-11 cells and CHME-NT = supernatant from non-transduced CHME-5 cells used as negative controls; HTB-T = supernatant collected from transduced HTB-11 cells and CHME-T2 = supernatant from transduced CHME-5 cells; and C + = purified recombinant sTNFR-Fc protein as a positive control.
    Figure Legend Snippet: Specific binding of expressed sTNFR-Fc to TNF-α by dot immunoblot assay . One microgram of standard recombinant human TNF-α protein was spotted onto nitrocellular membrane (NCM) and then blocked and incubated with supernatants from normal and transduced cells. After three washes with TBST, a goat-anti-human IgG Fc-HRP conjugate was applied and incubated at RT for 1 h. Specific binding was visualized by color deposition on the NCM following incubation with diaminobenzidine (DAB) substrate. Lanes: HTB-NT = supernatant from non-transduced HTB-11 cells and CHME-NT = supernatant from non-transduced CHME-5 cells used as negative controls; HTB-T = supernatant collected from transduced HTB-11 cells and CHME-T2 = supernatant from transduced CHME-5 cells; and C + = purified recombinant sTNFR-Fc protein as a positive control.

    Techniques Used: Binding Assay, Recombinant, Incubation, Purification, Positive Control

    4) Product Images from "The CPH1 Gene of Chlamydomonas reinhardtii Encodes Two Forms of Cryptochrome Whose Levels Are Controlled by Light-Induced Proteolysis 1 Encodes Two Forms of Cryptochrome Whose Levels Are Controlled by Light-Induced Proteolysis 1 [w]"

    Article Title: The CPH1 Gene of Chlamydomonas reinhardtii Encodes Two Forms of Cryptochrome Whose Levels Are Controlled by Light-Induced Proteolysis 1 Encodes Two Forms of Cryptochrome Whose Levels Are Controlled by Light-Induced Proteolysis 1 [w]

    Journal: Plant Physiology

    doi: 10.1104/pp.103.031930

    CPH1 migrates differently when overexpressed in E. coli or C. reinhardtii . A, E. coli cells transformed with pCPH101, which contains CPH1 cDNA, were induced with isopropylthio- β -galactoside for 2.5 h and cell extracts were analyzed using SDS-PAGE and stained with Coomassie Brilliant Blue. B, Western blot of E. coli pCPH101 extract before and after induction (left) and C. reinhardtii OxG extracts before and after heat shock (right). Western blots were performed using antibodies directed against CPH1 protein as described except TBST plus 0.3% (v/v) Triton X-100 was used.
    Figure Legend Snippet: CPH1 migrates differently when overexpressed in E. coli or C. reinhardtii . A, E. coli cells transformed with pCPH101, which contains CPH1 cDNA, were induced with isopropylthio- β -galactoside for 2.5 h and cell extracts were analyzed using SDS-PAGE and stained with Coomassie Brilliant Blue. B, Western blot of E. coli pCPH101 extract before and after induction (left) and C. reinhardtii OxG extracts before and after heat shock (right). Western blots were performed using antibodies directed against CPH1 protein as described except TBST plus 0.3% (v/v) Triton X-100 was used.

    Techniques Used: Transformation Assay, SDS Page, Staining, Western Blot

    5) Product Images from "Lentiviral vector-mediated stable expression of sTNFR-Fc in human macrophage and neuronal cells as a potential therapy for neuroAIDS"

    Article Title: Lentiviral vector-mediated stable expression of sTNFR-Fc in human macrophage and neuronal cells as a potential therapy for neuroAIDS

    Journal: Journal of Neuroinflammation

    doi: 10.1186/1742-2094-8-48

    Specific binding of expressed sTNFR-Fc to TNF-α by dot immunoblot assay . One microgram of standard recombinant human TNF-α protein was spotted onto nitrocellular membrane (NCM) and then blocked and incubated with supernatants from normal and transduced cells. After three washes with TBST, a goat-anti-human IgG Fc-HRP conjugate was applied and incubated at RT for 1 h. Specific binding was visualized by color deposition on the NCM following incubation with diaminobenzidine (DAB) substrate. Lanes: HTB-NT = supernatant from non-transduced HTB-11 cells and CHME-NT = supernatant from non-transduced CHME-5 cells used as negative controls; HTB-T = supernatant collected from transduced HTB-11 cells and CHME-T2 = supernatant from transduced CHME-5 cells; and C + = purified recombinant sTNFR-Fc protein as a positive control.
    Figure Legend Snippet: Specific binding of expressed sTNFR-Fc to TNF-α by dot immunoblot assay . One microgram of standard recombinant human TNF-α protein was spotted onto nitrocellular membrane (NCM) and then blocked and incubated with supernatants from normal and transduced cells. After three washes with TBST, a goat-anti-human IgG Fc-HRP conjugate was applied and incubated at RT for 1 h. Specific binding was visualized by color deposition on the NCM following incubation with diaminobenzidine (DAB) substrate. Lanes: HTB-NT = supernatant from non-transduced HTB-11 cells and CHME-NT = supernatant from non-transduced CHME-5 cells used as negative controls; HTB-T = supernatant collected from transduced HTB-11 cells and CHME-T2 = supernatant from transduced CHME-5 cells; and C + = purified recombinant sTNFR-Fc protein as a positive control.

    Techniques Used: Binding Assay, Recombinant, Incubation, Purification, Positive Control

    Specific binding of expressed sTNFR-Fc to TNF-α by dot immunoblot assay . One microgram of standard recombinant human TNF-α protein was spotted onto nitrocellular membrane (NCM) and then blocked and incubated with supernatants from normal and transduced cells. After three washes with TBST, a goat-anti-human IgG Fc-HRP conjugate was applied and incubated at RT for 1 h. Specific binding was visualized by color deposition on the NCM following incubation with diaminobenzidine (DAB) substrate. Lanes: HTB-NT = supernatant from non-transduced HTB-11 cells and CHME-NT = supernatant from non-transduced CHME-5 cells used as negative controls; HTB-T = supernatant collected from transduced HTB-11 cells and CHME-T2 = supernatant from transduced CHME-5 cells; and C + = purified recombinant sTNFR-Fc protein as a positive control.
    Figure Legend Snippet: Specific binding of expressed sTNFR-Fc to TNF-α by dot immunoblot assay . One microgram of standard recombinant human TNF-α protein was spotted onto nitrocellular membrane (NCM) and then blocked and incubated with supernatants from normal and transduced cells. After three washes with TBST, a goat-anti-human IgG Fc-HRP conjugate was applied and incubated at RT for 1 h. Specific binding was visualized by color deposition on the NCM following incubation with diaminobenzidine (DAB) substrate. Lanes: HTB-NT = supernatant from non-transduced HTB-11 cells and CHME-NT = supernatant from non-transduced CHME-5 cells used as negative controls; HTB-T = supernatant collected from transduced HTB-11 cells and CHME-T2 = supernatant from transduced CHME-5 cells; and C + = purified recombinant sTNFR-Fc protein as a positive control.

    Techniques Used: Binding Assay, Recombinant, Incubation, Purification, Positive Control

    6) Product Images from "The CPH1 Gene of Chlamydomonas reinhardtii Encodes Two Forms of Cryptochrome Whose Levels Are Controlled by Light-Induced Proteolysis 1 Encodes Two Forms of Cryptochrome Whose Levels Are Controlled by Light-Induced Proteolysis 1 [w]"

    Article Title: The CPH1 Gene of Chlamydomonas reinhardtii Encodes Two Forms of Cryptochrome Whose Levels Are Controlled by Light-Induced Proteolysis 1 Encodes Two Forms of Cryptochrome Whose Levels Are Controlled by Light-Induced Proteolysis 1 [w]

    Journal: Plant Physiology

    doi: 10.1104/pp.103.031930

    CPH1 migrates differently when overexpressed in E. coli or C. reinhardtii . A, E. coli cells transformed with pCPH101, which contains CPH1 cDNA, were induced with isopropylthio- β -galactoside for 2.5 h and cell extracts were analyzed using SDS-PAGE and stained with Coomassie Brilliant Blue. B, Western blot of E. coli pCPH101 extract before and after induction (left) and C. reinhardtii OxG extracts before and after heat shock (right). Western blots were performed using antibodies directed against CPH1 protein as described except TBST plus 0.3% (v/v) Triton X-100 was used.
    Figure Legend Snippet: CPH1 migrates differently when overexpressed in E. coli or C. reinhardtii . A, E. coli cells transformed with pCPH101, which contains CPH1 cDNA, were induced with isopropylthio- β -galactoside for 2.5 h and cell extracts were analyzed using SDS-PAGE and stained with Coomassie Brilliant Blue. B, Western blot of E. coli pCPH101 extract before and after induction (left) and C. reinhardtii OxG extracts before and after heat shock (right). Western blots were performed using antibodies directed against CPH1 protein as described except TBST plus 0.3% (v/v) Triton X-100 was used.

    Techniques Used: Transformation Assay, SDS Page, Staining, Western Blot

    Related Articles

    Incubation:

    Article Title: Lentiviral vector-mediated stable expression of sTNFR-Fc in human macrophage and neuronal cells as a potential therapy for neuroAIDS
    Article Snippet: .. Following washing with TBST, the membranes were incubated with goat-anti-human IgG Fc-HRP conjugate (KPL) at RT for 1 h. After three washes with TBST, the bound antibody was visualized by incubation with diaminobenzidine (DAB) substrate (Pierce) according to the manufacturer's instruction. .. Specific binding was visualized by the color deposition on the NCM.

    Article Title: The CPH1 Gene of Chlamydomonas reinhardtii Encodes Two Forms of Cryptochrome Whose Levels Are Controlled by Light-Induced Proteolysis 1 Encodes Two Forms of Cryptochrome Whose Levels Are Controlled by Light-Induced Proteolysis 1 [w]
    Article Snippet: .. Primary antibodies against CPH1 were diluted to 1:1,000 in 1% (w/v) bovine serum albumin in TBST and incubated with the membrane for 1 h. M2 monoclonal antibodies against FLAG (Invitrogen, Carlsbad, CA) were diluted 1:1000 in 1% bovine serum albumin, 2.5% NFDM in TBST, and incubated with the membrane for 1 h. Regardless of the primary antibody used, membranes were subsequently washed for 30 min in TBST or TBST plus 0.3% (v/v) Triton X-100. .. Secondary antibodies (goat anti-rabbit or goat anti-mouse, Santa Cruz Biotechnology, Santa Cruz, CA) were diluted to 1:10,000 in TBST with 5% (w/v) NFDM and incubated with the membrane for 45 min. Membranes were again washed in TBST for 30 min. Chemiluminescent reagents (Amersham, Piscataway, NJ) were added according to manufacturer's protocol and the membranes were exposed to film.

    Article Title: MMP-13 enzyme and pH responsive theranostic nanoplatform for osteoarthritis
    Article Snippet: .. The membranes were incubated with blocking buffer 5% non-fat milk in TBS containing 0.1% Tween-20 (TBST) for 2 h at room temperature and then probed with the primary antibodies against p65, Akt and p-Akt, P38, p-P38 (dilution 1:1000) overnight at 4 °C. .. After washing three times with TBS containing 0.1% Tween-20 for 5 min, the membranes were then incubated with the secondary antibody (Invitrogen, USA) and visualized using the Odyssey Infrared Imaging System (LI-COR USA) according to the manufacturer’s instructions.

    Blocking Assay:

    Article Title: MMP-13 enzyme and pH responsive theranostic nanoplatform for osteoarthritis
    Article Snippet: .. The membranes were incubated with blocking buffer 5% non-fat milk in TBS containing 0.1% Tween-20 (TBST) for 2 h at room temperature and then probed with the primary antibodies against p65, Akt and p-Akt, P38, p-P38 (dilution 1:1000) overnight at 4 °C. .. After washing three times with TBS containing 0.1% Tween-20 for 5 min, the membranes were then incubated with the secondary antibody (Invitrogen, USA) and visualized using the Odyssey Infrared Imaging System (LI-COR USA) according to the manufacturer’s instructions.

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  • 99
    Thermo Fisher tween 20 tbst
    Characterization of MRC-PPL nano-micelles.  a  TEM images of MRC-PPL and MRC-PPL@PSO micelles. Scale bare = 500 nm.  b  Size distribution of MRC-PPL micelles based on dynamic light scattering.  c  Zeta potentials of PSO, PPL, MRC-PPL micelles and MRC-PPL@PSO micelles.  d  UV–Vis absorbance.  e  Fluorescence intensity of MRC-PPL micelles and Cy5.5.  f  Fluorescence intensity of MRC-PPL micelles, without or with MMP-13 (0.01  μ M), in the absence or presence of MMP-13 inhibitor (0.45  μ M).  g In vitro  release of PSO from MRC-PPL micelles in PBS (pH 6.5 and 7.4) with 0.1% Tween 80 (mean ± SD, n = 3)
    Tween 20 Tbst, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 221 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/tween 20 tbst/product/Thermo Fisher
    Average 99 stars, based on 221 article reviews
    Price from $9.99 to $1999.99
    tween 20 tbst - by Bioz Stars, 2020-11
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    90
    Thermo Fisher skim milk tbst
    Characterization of MRC-PPL nano-micelles.  a  TEM images of MRC-PPL and MRC-PPL@PSO micelles. Scale bare = 500 nm.  b  Size distribution of MRC-PPL micelles based on dynamic light scattering.  c  Zeta potentials of PSO, PPL, MRC-PPL micelles and MRC-PPL@PSO micelles.  d  UV–Vis absorbance.  e  Fluorescence intensity of MRC-PPL micelles and Cy5.5.  f  Fluorescence intensity of MRC-PPL micelles, without or with MMP-13 (0.01  μ M), in the absence or presence of MMP-13 inhibitor (0.45  μ M).  g In vitro  release of PSO from MRC-PPL micelles in PBS (pH 6.5 and 7.4) with 0.1% Tween 80 (mean ± SD, n = 3)
    Skim Milk Tbst, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 6437 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/skim milk tbst/product/Thermo Fisher
    Average 90 stars, based on 6437 article reviews
    Price from $9.99 to $1999.99
    skim milk tbst - by Bioz Stars, 2020-11
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    92
    millipore tbst
    Characterization of MRC-PPL nano-micelles.  a  TEM images of MRC-PPL and MRC-PPL@PSO micelles. Scale bare = 500 nm.  b  Size distribution of MRC-PPL micelles based on dynamic light scattering.  c  Zeta potentials of PSO, PPL, MRC-PPL micelles and MRC-PPL@PSO micelles.  d  UV–Vis absorbance.  e  Fluorescence intensity of MRC-PPL micelles and Cy5.5.  f  Fluorescence intensity of MRC-PPL micelles, without or with MMP-13 (0.01  μ M), in the absence or presence of MMP-13 inhibitor (0.45  μ M).  g In vitro  release of PSO from MRC-PPL micelles in PBS (pH 6.5 and 7.4) with 0.1% Tween 80 (mean ± SD, n = 3)
    Tbst, supplied by millipore, used in various techniques. Bioz Stars score: 92/100, based on 167 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/tbst/product/millipore
    Average 92 stars, based on 167 article reviews
    Price from $9.99 to $1999.99
    tbst - by Bioz Stars, 2020-11
    92/100 stars
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    Image Search Results


    Characterization of MRC-PPL nano-micelles.  a  TEM images of MRC-PPL and MRC-PPL@PSO micelles. Scale bare = 500 nm.  b  Size distribution of MRC-PPL micelles based on dynamic light scattering.  c  Zeta potentials of PSO, PPL, MRC-PPL micelles and MRC-PPL@PSO micelles.  d  UV–Vis absorbance.  e  Fluorescence intensity of MRC-PPL micelles and Cy5.5.  f  Fluorescence intensity of MRC-PPL micelles, without or with MMP-13 (0.01  μ M), in the absence or presence of MMP-13 inhibitor (0.45  μ M).  g In vitro  release of PSO from MRC-PPL micelles in PBS (pH 6.5 and 7.4) with 0.1% Tween 80 (mean ± SD, n = 3)

    Journal: Journal of Nanobiotechnology

    Article Title: MMP-13 enzyme and pH responsive theranostic nanoplatform for osteoarthritis

    doi: 10.1186/s12951-020-00666-7

    Figure Lengend Snippet: Characterization of MRC-PPL nano-micelles. a TEM images of MRC-PPL and MRC-PPL@PSO micelles. Scale bare = 500 nm. b Size distribution of MRC-PPL micelles based on dynamic light scattering. c Zeta potentials of PSO, PPL, MRC-PPL micelles and MRC-PPL@PSO micelles. d UV–Vis absorbance. e Fluorescence intensity of MRC-PPL micelles and Cy5.5. f Fluorescence intensity of MRC-PPL micelles, without or with MMP-13 (0.01  μ M), in the absence or presence of MMP-13 inhibitor (0.45  μ M). g In vitro release of PSO from MRC-PPL micelles in PBS (pH 6.5 and 7.4) with 0.1% Tween 80 (mean ± SD, n = 3)

    Article Snippet: The membranes were incubated with blocking buffer 5% non-fat milk in TBS containing 0.1% Tween-20 (TBST) for 2 h at room temperature and then probed with the primary antibodies against p65, Akt and p-Akt, P38, p-P38 (dilution 1:1000) overnight at 4 °C.

    Techniques: Transmission Electron Microscopy, Fluorescence, In Vitro