tbst  (Thermo Fisher)


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    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
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    Lab Reagents and Chemicals
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    Structured Review

    Thermo Fisher tbst
    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 <t>TBST,</t> a goat-anti-human <t>IgG</t> 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.
    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 97 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    tbst - by Bioz Stars, 2021-07
    97/100 stars

    Images

    1) 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

    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 "Development and Application of Human Coronavirus Protein Microarray for Specificity Analysis"

    Article Title: Development and Application of Human Coronavirus Protein Microarray for Specificity Analysis

    Journal: Analytical Chemistry

    doi: 10.1021/acs.analchem.1c00614

    Serum IgG and IgA profiling in COVID-19 and control subjects. (A) HCoV protein microarray was blocked by HyBlock for 10 min and applied with 100 μL of 500-fold diluted serum in TBST supplement with 1% BSA (0.2 μL of original serum). After 1 h incubation, the array was washed and incubated with labeled anti-IgG/IgA antibodies for 30 min. After a final wash, the array was dried and scanned for fluorescence signals. The total procedure took about 150 min. (B, C) Representative images of the IgG in two COVID-19 patients and two healthy controls. (D, E) Representative images of IgA in two COVID-19 patients and two healthy controls. The blue arrow indicates spike protein, nucleocapsid protein, and spike S1 domain from SARS-CoV-2 (from left to right). The orange and purple arrows indicate the same order but from MERS-CoV and SARS-CoV, respectively.
    Figure Legend Snippet: Serum IgG and IgA profiling in COVID-19 and control subjects. (A) HCoV protein microarray was blocked by HyBlock for 10 min and applied with 100 μL of 500-fold diluted serum in TBST supplement with 1% BSA (0.2 μL of original serum). After 1 h incubation, the array was washed and incubated with labeled anti-IgG/IgA antibodies for 30 min. After a final wash, the array was dried and scanned for fluorescence signals. The total procedure took about 150 min. (B, C) Representative images of the IgG in two COVID-19 patients and two healthy controls. (D, E) Representative images of IgA in two COVID-19 patients and two healthy controls. The blue arrow indicates spike protein, nucleocapsid protein, and spike S1 domain from SARS-CoV-2 (from left to right). The orange and purple arrows indicate the same order but from MERS-CoV and SARS-CoV, respectively.

    Techniques Used: Microarray, Incubation, Labeling, Fluorescence

    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

    7) 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: Poleward transport of Eg5 by dynein-dynactin in Xenopus laevis egg extract spindles
    Article Snippet: Coverslips were washed with 0.1 M glycin in TBS with Tween (TBST) to quench remnants of formaldehyde, blocked with 2% BSA in TBST, and incubated for 30 min with 11 μg/ml of a purified polyclonal antibody raised against a C-terminal fragment of the dynein heavy chain corresponding to amino acids 4,179–4,415 (a gift of S. Kandels-Lewis and S. Rybina; European Molecular Biology Laboratory, Heidelberg, Germany) or with 4 ng/ml of a mouse monoclonal antibody raised against p150Glued (BD Biosciences). .. After incubation with primary antibody, coverslips were washed in TBST containing 10 μg/ml Hoechst and incubated for 30 min with 10 μg/ml of secondary antibody fused to Alexa Fluor 488 (Invitrogen), and finally washed in TBST. .. Images were taken with a confocal LSM 510 microscope with laser lines of 405, 488, 543, and 633 nm and a 63× oil immersion objective lens.

    Article Title: Lentiviral vector-mediated stable expression of sTNFR-Fc in human macrophage and neuronal cells as a potential therapy for neuroAIDS
    Article Snippet: The NCM was then incubated for 1 h at RT with cell culture media collected from either transduced or non-transduced control cells, or with recombinant sTNFR-Fc protein (R & D Systems) as a positive control. .. 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: MMP-13 enzyme and pH responsive theranostic nanoplatform for osteoarthritis
    Article Snippet: Equal amounts of protein (40 μg) were separated by 10% SDS-PAGE and transferred to PVDF membranes. .. 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.

    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: Before use, sera containing antibodies against CPH1 and preimmune sera were partially purified using an AVID-AL column (Bioprobe, Tustin, CA) according to the manufacturer's protocol. .. 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.

    Blocking Assay:

    Article Title: MMP-13 enzyme and pH responsive theranostic nanoplatform for osteoarthritis
    Article Snippet: Equal amounts of protein (40 μg) were separated by 10% SDS-PAGE and transferred to PVDF membranes. .. 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.

    other:

    Article Title: Biogenesis of RNA-containing extracellular vesicles at endoplasmic reticulum membrane contact sites
    Article Snippet: Membranes were blocked in 3% BSA diluted in Trisbuffered saline with 0.5% Tween 20 (TBST) for 4h at room temperature.

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  • 97
    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: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/tween 20 tbst/product/Thermo Fisher
    Average 97 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    tween 20 tbst - by Bioz Stars, 2021-07
    97/100 stars
      Buy from Supplier

    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

    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.

    Journal: Journal of Neuroinflammation

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

    doi: 10.1186/1742-2094-8-48

    Figure Lengend 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.

    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.

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

    Modified forms of TNYL-RAW retain high EphB4 binding affinity and potency for inhibition of EphB4-ephrin-B2 binding. (A) Biotinylated, streptavidin-bound and PEGylated TNYL-RAW were incubated at the indicated concentrations in EphB4-coated ELISA wells. Biotinylated TNYL-RAW was detected with streptavidin-HRP, TNYL-RAW-streptavidin was detected with and anti-streptavidin antibody coupled to HRP, and PEG-TNYL-RAW was detected with an anti-PEG antibody followed by a secondary antibody conjugated to HRP. (B) The indicated concentrations of EphB4 AP were incubated in ELISA wells pre-coated with streptavidin and biotinylated TNYL-RAW (left) or an anti-IgG antibody and TNYL-RAW-Fc (right). K d values are based on EphB4 AP concentrations calculated from AP activity. (C) The different forms of TNYL-RAW were incubated at the indicated concentrations together with a constant amount of ephrin-B2 AP in ELISA wells pre-coated with EphB4 Fc. The ratio of ephrin-B2 AP bound in the presence and in the absence of peptide is shown. The graphs show averages ± SE from triplicate measurements in representative experiments, while the K d and IC 50 values are calculated from 3 to 11 experiments.

    Journal: PLoS ONE

    Article Title: PEGylation Potentiates the Effectiveness of an Antagonistic Peptide That Targets the EphB4 Receptor with Nanomolar Affinity

    doi: 10.1371/journal.pone.0028611

    Figure Lengend Snippet: Modified forms of TNYL-RAW retain high EphB4 binding affinity and potency for inhibition of EphB4-ephrin-B2 binding. (A) Biotinylated, streptavidin-bound and PEGylated TNYL-RAW were incubated at the indicated concentrations in EphB4-coated ELISA wells. Biotinylated TNYL-RAW was detected with streptavidin-HRP, TNYL-RAW-streptavidin was detected with and anti-streptavidin antibody coupled to HRP, and PEG-TNYL-RAW was detected with an anti-PEG antibody followed by a secondary antibody conjugated to HRP. (B) The indicated concentrations of EphB4 AP were incubated in ELISA wells pre-coated with streptavidin and biotinylated TNYL-RAW (left) or an anti-IgG antibody and TNYL-RAW-Fc (right). K d values are based on EphB4 AP concentrations calculated from AP activity. (C) The different forms of TNYL-RAW were incubated at the indicated concentrations together with a constant amount of ephrin-B2 AP in ELISA wells pre-coated with EphB4 Fc. The ratio of ephrin-B2 AP bound in the presence and in the absence of peptide is shown. The graphs show averages ± SE from triplicate measurements in representative experiments, while the K d and IC 50 values are calculated from 3 to 11 experiments.

    Article Snippet: Bound biotinylated TNYL-RAW was detected with horseradish peroxidase (HRP)-conjugated streptavidin (1∶2,000 dilution in TBST, Pierce Biotechnology, Rockford, IL) and bound TNYL-RAW-streptavidin was detected with an anti-streptavidin antibody coupled with HRP (1∶1,000 dilution in TBST, Life Technologies-Invitrogen).

    Techniques: Modification, Binding Assay, Inhibition, Incubation, Enzyme-linked Immunosorbent Assay, Activity Assay

    The TNYL-RAW peptide is rapidly lost in cell culture medium and from the mouse circulation. (A) Biotinylated TNYL-RAW peptide was incubated with cultured PC3 prostate cancer cells grown in the same medium for 3 days or in the culture medium freshly replaced just before adding the peptide. Functional (EphB4- and streptavidin-binding) peptide remaining at the indicated times was captured in ELISA plates coated with EphB4 Fc and detected with streptavidin-HRP. (B) TNYL-RAW was incubated at 37°C in PC3 cell conditioned medium (without cells) with and without a mixture of protease inhibitors including aprotinin, leupeptin, pepstatin and PMSF, and detected as in (A). (C) TNYL-RAW was incubated with PC3 cell conditioned medium for 4 hours and added together with ephrin-B2 AP to ELISA wells pre-coated with EphB4 Fc. TNYL-RAW mixed with conditioned medium right before the ELISA assay (0 hrs) was used as a control. The graph shows the ratio of ephrin-B2 AP bound in the presence and in the absence of peptide. (D) Serum from 3 mice injected intravenously with 6 nmoles biotinylated TNYL-RAW was collected 30 min after peptide administration and incubated at a dilution of 1∶20 in ELISA wells pre-coated with EphB4 Fc. Based on the amount of injected TNYL-RAW and an estimated mouse serum volume of 2.5 ml, the peptide concentration in the wells would be 120 nM. TNYL-RAW at a concentration of 5 nM in similarly diluted mouse serum was used for comparison. Bound peptide was detected with streptavidin-HRP. (E) TNYL-RAW was incubated in undiluted mouse serum ex vivo for the indicated times and detected as described in (A). Averages from 3 measurements ± SE are shown in all the panels.

    Journal: PLoS ONE

    Article Title: PEGylation Potentiates the Effectiveness of an Antagonistic Peptide That Targets the EphB4 Receptor with Nanomolar Affinity

    doi: 10.1371/journal.pone.0028611

    Figure Lengend Snippet: The TNYL-RAW peptide is rapidly lost in cell culture medium and from the mouse circulation. (A) Biotinylated TNYL-RAW peptide was incubated with cultured PC3 prostate cancer cells grown in the same medium for 3 days or in the culture medium freshly replaced just before adding the peptide. Functional (EphB4- and streptavidin-binding) peptide remaining at the indicated times was captured in ELISA plates coated with EphB4 Fc and detected with streptavidin-HRP. (B) TNYL-RAW was incubated at 37°C in PC3 cell conditioned medium (without cells) with and without a mixture of protease inhibitors including aprotinin, leupeptin, pepstatin and PMSF, and detected as in (A). (C) TNYL-RAW was incubated with PC3 cell conditioned medium for 4 hours and added together with ephrin-B2 AP to ELISA wells pre-coated with EphB4 Fc. TNYL-RAW mixed with conditioned medium right before the ELISA assay (0 hrs) was used as a control. The graph shows the ratio of ephrin-B2 AP bound in the presence and in the absence of peptide. (D) Serum from 3 mice injected intravenously with 6 nmoles biotinylated TNYL-RAW was collected 30 min after peptide administration and incubated at a dilution of 1∶20 in ELISA wells pre-coated with EphB4 Fc. Based on the amount of injected TNYL-RAW and an estimated mouse serum volume of 2.5 ml, the peptide concentration in the wells would be 120 nM. TNYL-RAW at a concentration of 5 nM in similarly diluted mouse serum was used for comparison. Bound peptide was detected with streptavidin-HRP. (E) TNYL-RAW was incubated in undiluted mouse serum ex vivo for the indicated times and detected as described in (A). Averages from 3 measurements ± SE are shown in all the panels.

    Article Snippet: Bound biotinylated TNYL-RAW was detected with horseradish peroxidase (HRP)-conjugated streptavidin (1∶2,000 dilution in TBST, Pierce Biotechnology, Rockford, IL) and bound TNYL-RAW-streptavidin was detected with an anti-streptavidin antibody coupled with HRP (1∶1,000 dilution in TBST, Life Technologies-Invitrogen).

    Techniques: Cell Culture, Incubation, Functional Assay, Binding Assay, Enzyme-linked Immunosorbent Assay, Mouse Assay, Injection, Concentration Assay, Ex Vivo

    Modified forms of TNYL-RAW have increased stability in cell culture medium and in the mouse circulation. (A, B) Biotinylated, streptavidin-bound, fused to Fc and PEGylated TNYL-RAW were incubated in medium conditioned by PC3 prostate cancer cells (A) or mouse serum (B). Functional peptide remaining at the indicated times was captured in ELISA plates and quantified. Biotinylated TNYL-RAW was captured on ELISA wells pre-coated with EphB4 Fc and detected with Streptavidin-HRP. TNYL-RAW-streptavidin was captured on wells pre-coated with EphB4 Fc and detected with an anti-streptavidin antibody coupled to HRP. TNYL-RAW-Fc was captured on wells coated with an anti-Fc antibody and detected with EphB4 AP. PEG-TNYL-RAW was captured on wells coated with EphB4 Fc and detected with anti-PEG antibody followed by a secondary antibody conjugated to HRP. Normalized averages from 6–9 measurements ± SE are shown. Peptide amounts at different time points were compared to those at time 0 by one-way ANOVA and Dunnett's post test. *P

    Journal: PLoS ONE

    Article Title: PEGylation Potentiates the Effectiveness of an Antagonistic Peptide That Targets the EphB4 Receptor with Nanomolar Affinity

    doi: 10.1371/journal.pone.0028611

    Figure Lengend Snippet: Modified forms of TNYL-RAW have increased stability in cell culture medium and in the mouse circulation. (A, B) Biotinylated, streptavidin-bound, fused to Fc and PEGylated TNYL-RAW were incubated in medium conditioned by PC3 prostate cancer cells (A) or mouse serum (B). Functional peptide remaining at the indicated times was captured in ELISA plates and quantified. Biotinylated TNYL-RAW was captured on ELISA wells pre-coated with EphB4 Fc and detected with Streptavidin-HRP. TNYL-RAW-streptavidin was captured on wells pre-coated with EphB4 Fc and detected with an anti-streptavidin antibody coupled to HRP. TNYL-RAW-Fc was captured on wells coated with an anti-Fc antibody and detected with EphB4 AP. PEG-TNYL-RAW was captured on wells coated with EphB4 Fc and detected with anti-PEG antibody followed by a secondary antibody conjugated to HRP. Normalized averages from 6–9 measurements ± SE are shown. Peptide amounts at different time points were compared to those at time 0 by one-way ANOVA and Dunnett's post test. *P

    Article Snippet: Bound biotinylated TNYL-RAW was detected with horseradish peroxidase (HRP)-conjugated streptavidin (1∶2,000 dilution in TBST, Pierce Biotechnology, Rockford, IL) and bound TNYL-RAW-streptavidin was detected with an anti-streptavidin antibody coupled with HRP (1∶1,000 dilution in TBST, Life Technologies-Invitrogen).

    Techniques: Modification, Cell Culture, Incubation, Functional Assay, Enzyme-linked Immunosorbent Assay

    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.

    Journal: Plant Physiology

    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]

    doi: 10.1104/pp.103.031930

    Figure Lengend 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.

    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.

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