anti hla dq antibodies (Worthington Biochemical)

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Bioz vStars

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DNA Cellulose Double Stranded

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Catalog Number:

ls01120

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Size:

1 gm

Source:

Calf Thymus

Cas Number:

9007.49.2

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Worthington Biochemical anti hla dq antibodies

FACS crossmatch of B cells and T cells as shown by their histograms. The FACS crossmatch of T cells is unequivocally negative, whereas the B cells provide a histogram of weakly increased intensity. Due to the faint intensity it does not lead to an interpretable result especially in the context of a negative <t>HLA</t> class II-specific B-Screen <t>ELISA</t> and a negative conventional CDC crossmatch performed with isolated B cells.

Prepared by a method developed at Worthington in which native double stranded calf thymus DNA is covalently bound to cellulose Suitable for the purification of many DNA binding proteins such as polymerases transcription factors and terminators etc Supplied as a dry powder One gram of DNA cellulose will swell to 3 4ml when fully hydrated
https://www.bioz.com/result/anti hla dq antibodies/product/Worthington Biochemical
Average 88 stars, based on 1125 article reviews
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anti hla dq antibodies - by Bioz Stars, 2021-01

88/100 stars

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1) Product Images from "Novel solid phase-based ELISA assays contribute to an improved detection of anti-HLA antibodies and to an increased reliability of pre- and post-transplant crossmatching"

Article Title: Novel solid phase-based ELISA assays contribute to an improved detection of anti-HLA antibodies and to an increased reliability of pre- and post-transplant crossmatching

Journal: NDT Plus

doi: 10.1093/ndtplus/sfq156

Figure Legend Snippet: FACS crossmatch of B cells and T cells as shown by their histograms. The FACS crossmatch of T cells is unequivocally negative, whereas the B cells provide a histogram of weakly increased intensity. Due to the faint intensity it does not lead to an interpretable result especially in the context of a negative HLA class II-specific B-Screen ELISA and a negative conventional CDC crossmatch performed with isolated B cells.

Techniques Used: FACS, Enzyme-linked Immunosorbent Assay, Isolation

Diagram characterizing the outcome of doubtful results of the conventional CDC crossmatch after their re-evaluation using the AMS-crossmatch ELISA. Using the AMS-ELISA, more than 70% of the doubtful conventional CDC-crossmatch results unequivocally do not exhibit donor-specific anti-HLA antibodies demonstrating its higher reliability and lower susceptibility to various sources of irritation.

Figure Legend Snippet: Diagram characterizing the outcome of doubtful results of the conventional CDC crossmatch after their re-evaluation using the AMS-crossmatch ELISA. Using the AMS-ELISA, more than 70% of the doubtful conventional CDC-crossmatch results unequivocally do not exhibit donor-specific anti-HLA antibodies demonstrating its higher reliability and lower susceptibility to various sources of irritation.

Techniques Used: Affinity Magnetic Separation, Enzyme-linked Immunosorbent Assay

Flow diagram of the AMS-ELISA for the detection of HLA class I molecules. ( A ) Binding of the donor’s solubilized HLA class I molecules by monoclonal capture antibodies recognizing a monomorphic epitope on HLA class I molecules. ( B ) Binding of the donor-specific anti-HLA antibodies out of the recipient’s serum to the HLA molecules of the donor. ( C ) Binding of alkaline phosphatase-conjugated secondary antibodies to the recipient’s bound donor-specific anti-HLA class I antibodies and subsequent colour reaction. The original protocol was modified by substituting the human IgG-specific by a human IgG/M/A-specific secondary antibody. ( D ) Lysate control using an alkaline phosphatase-conjugated monoclonal antibody directed against a second monomorphic epitope for detection to confirm the immobilization of a sufficient amount of HLA molecules by the solid phase-bound capture antibody. The AMS-ELISA variant for the identification of donor-specific antibodies directed against HLA class II molecules is designed correspondingly.

Figure Legend Snippet: Flow diagram of the AMS-ELISA for the detection of HLA class I molecules. ( A ) Binding of the donor’s solubilized HLA class I molecules by monoclonal capture antibodies recognizing a monomorphic epitope on HLA class I molecules. ( B ) Binding of the donor-specific anti-HLA antibodies out of the recipient’s serum to the HLA molecules of the donor. ( C ) Binding of alkaline phosphatase-conjugated secondary antibodies to the recipient’s bound donor-specific anti-HLA class I antibodies and subsequent colour reaction. The original protocol was modified by substituting the human IgG-specific by a human IgG/M/A-specific secondary antibody. ( D ) Lysate control using an alkaline phosphatase-conjugated monoclonal antibody directed against a second monomorphic epitope for detection to confirm the immobilization of a sufficient amount of HLA molecules by the solid phase-bound capture antibody. The AMS-ELISA variant for the identification of donor-specific antibodies directed against HLA class II molecules is designed correspondingly.

Techniques Used: Flow Cytometry, Affinity Magnetic Separation, Enzyme-linked Immunosorbent Assay, Binding Assay, Modification, Variant Assay

2) Product Images from "E-Cadherin-dependent Growth Suppression is Mediated by the Cyclin-dependent Kinase Inhibitor p27KIP1"

Article Title: E-Cadherin-dependent Growth Suppression is Mediated by the Cyclin-dependent Kinase Inhibitor p27KIP1

Journal: The Journal of Cell Biology

doi:

Increased p27 binding to cyclin E mediates reduced Cyclin E–associated kinase activity in aggregated cells. ( a ) Cyclin E–associated cdk2 kinase activity, as measured by phosphorylation of Histone H1 substrate in representative neomycin-resistant control transfectants ( neo1 , neo4 , neo8 ) or E-cadherin transfectants (Ecad1, Ecad9, Ecad18) grown in three-dimensional culture. Also included are Pc5-T cells grown in monolayer (2-D) culture, or in three-dimensional culture in either the presence or absence of hyaluronidase (Hy). ( b ) Increased levels of p27 bound to cyclin E in tightly adherent EMT/6 spheroids. After immunoprecipitating cyclin E from tightly- or loosely adherent aggregates, levels of cyclin E–bound p27 were detected by immunoblotting. Cell-free lysis buffer was used for the control sample. ( c ) Immunodepletion of p27 from aggregated E-cadherin transfectants. Cell extracts immunodepleted one (1×) or two (2×) times with antibodies against p27 were probed for p27 by immunoblotting. Controls ( Con ) represent extracts before immunodepletion ( d ). Cyclin E, cyclin E–associated cdk2, and p27 are markedly reduced in p27-immunodepleted ( ID ) supernatents from E-cadherin–aggregated cells. Cyclin E immunoprecipitates from lysates with or without prior immunodepletion with p27 antibodies were probed for cyclin E, cdk2, or p27 by immunoblotting. As a control, Ecad9 lysates were immunoprecipitated with nonspecific rabbit IgG antibodies instead of cyclin E antibodies. ( e ) Cyclin E–associated cdk2 kinase activity is increased after p27-immunodepletion ( ID ) of E-cadherin–arrested cells. The representative control in this experiment was Ecad7 lysate immunoprecipitated with nonspecific rabbit IgG antibodies instead of cyclin E antibodies. In each of these experiments cells were cultured for 48 h in three-dimensional culture.

Figure Legend Snippet: Increased p27 binding to cyclin E mediates reduced Cyclin E–associated kinase activity in aggregated cells. ( a ) Cyclin E–associated cdk2 kinase activity, as measured by phosphorylation of Histone H1 substrate in representative neomycin-resistant control transfectants ( neo1 , neo4 , neo8 ) or E-cadherin transfectants (Ecad1, Ecad9, Ecad18) grown in three-dimensional culture. Also included are Pc5-T cells grown in monolayer (2-D) culture, or in three-dimensional culture in either the presence or absence of hyaluronidase (Hy). ( b ) Increased levels of p27 bound to cyclin E in tightly adherent EMT/6 spheroids. After immunoprecipitating cyclin E from tightly- or loosely adherent aggregates, levels of cyclin E–bound p27 were detected by immunoblotting. Cell-free lysis buffer was used for the control sample. ( c ) Immunodepletion of p27 from aggregated E-cadherin transfectants. Cell extracts immunodepleted one (1×) or two (2×) times with antibodies against p27 were probed for p27 by immunoblotting. Controls ( Con ) represent extracts before immunodepletion ( d ). Cyclin E, cyclin E–associated cdk2, and p27 are markedly reduced in p27-immunodepleted ( ID ) supernatents from E-cadherin–aggregated cells. Cyclin E immunoprecipitates from lysates with or without prior immunodepletion with p27 antibodies were probed for cyclin E, cdk2, or p27 by immunoblotting. As a control, Ecad9 lysates were immunoprecipitated with nonspecific rabbit IgG antibodies instead of cyclin E antibodies. ( e ) Cyclin E–associated cdk2 kinase activity is increased after p27-immunodepletion ( ID ) of E-cadherin–arrested cells. The representative control in this experiment was Ecad7 lysate immunoprecipitated with nonspecific rabbit IgG antibodies instead of cyclin E antibodies. In each of these experiments cells were cultured for 48 h in three-dimensional culture.

Techniques Used: Binding Assay, Activity Assay, Lysis, Immunoprecipitation, Cell Culture

E-cadherin suppresses growth of EMT/6 cells in three-dimensional culture. ( a ) Proliferation of EMT/6 cells transfected with E-cadherin ( Ecad 9) or neomycin vector alone ( neo1 ) as measured by BrdU incorporation into DNA. 24 h after plating in three-dimensional culture, cells were either untreated (−BrdU) or pulsed with BrdU (+BrdU) for a further 24 h. Cells were prepared as described in the Materials and Methods, and cell cycle profiles were analyzed by flow cytometry. Tightly adherent or hyaluronidase ( HYase ) dispersed Pc5-T cells were also included as an additional control. ( b ) Proliferation of neomycin-resistant control transfectants ( neo4 , neo7 , neo8 ) or E-cadherin transfectants ( Ecad3 , Ecad7 , Ecad9 , and Ecad18 ) as measured by [ 3 H]thymidine incorporation into DNA. Intercellular adhesion of E-cadherin transfectants was prevented by treatment with 2 μg/ml DECMA-1 antibody at the time of plating.

Figure Legend Snippet: E-cadherin suppresses growth of EMT/6 cells in three-dimensional culture. ( a ) Proliferation of EMT/6 cells transfected with E-cadherin ( Ecad 9) or neomycin vector alone ( neo1 ) as measured by BrdU incorporation into DNA. 24 h after plating in three-dimensional culture, cells were either untreated (−BrdU) or pulsed with BrdU (+BrdU) for a further 24 h. Cells were prepared as described in the Materials and Methods, and cell cycle profiles were analyzed by flow cytometry. Tightly adherent or hyaluronidase ( HYase ) dispersed Pc5-T cells were also included as an additional control. ( b ) Proliferation of neomycin-resistant control transfectants ( neo4 , neo7 , neo8 ) or E-cadherin transfectants ( Ecad3 , Ecad7 , Ecad9 , and Ecad18 ) as measured by [ 3 H]thymidine incorporation into DNA. Intercellular adhesion of E-cadherin transfectants was prevented by treatment with 2 μg/ml DECMA-1 antibody at the time of plating.

Techniques Used: Transfection, Plasmid Preparation, BrdU Incorporation Assay, Flow Cytometry, Cytometry

Changes in cell cycle molecules in response to intercellular adhesion of EMT/6 cells as detected by immunoblotting. ( a ) Three-dimensional cultures of EMT/6 neomycin–resistant control transfectants ( neo1 , neo4 ), E-cadherin transfectants ( Ecad3 , Ecad7, and Ecad9 ), EMT/6 loosely-adherent variants ( Pc10-L and Pc11-L ) or HA-dependent tightly adherent variants ( Pc5-T , PcT-7 ) were examined. Immunoblots were probed for the cell cycle molecules indicated. E-cadherin- or HA-dependent intercellular adhesion was prevented by treatment with either DECMA-1 antibody ( Dec ) or hyaluronidase ( Hy ), respectively. Note changes in pRb phosphorylation and levels of cyclin D1 and p27 in cells allowed to aggregate in three-dimensional culture. ( b ) Time course demonstrating changes in p27 and cyclin D1 protein levels as cells aggregate in three-dimensional culture. Cells transfected with E-cadherin ( Ecad3 ) grown in the presence or absence of 2 μg/ml DECMA-1 antibody for the indicated times were probed for p27 and cyclin D1 by immunoblotting. At time = 0 cells were transferred from two- to three-dimensional culture.

Figure Legend Snippet: Changes in cell cycle molecules in response to intercellular adhesion of EMT/6 cells as detected by immunoblotting. ( a ) Three-dimensional cultures of EMT/6 neomycin–resistant control transfectants ( neo1 , neo4 ), E-cadherin transfectants ( Ecad3 , Ecad7, and Ecad9 ), EMT/6 loosely-adherent variants ( Pc10-L and Pc11-L ) or HA-dependent tightly adherent variants ( Pc5-T , PcT-7 ) were examined. Immunoblots were probed for the cell cycle molecules indicated. E-cadherin- or HA-dependent intercellular adhesion was prevented by treatment with either DECMA-1 antibody ( Dec ) or hyaluronidase ( Hy ), respectively. Note changes in pRb phosphorylation and levels of cyclin D1 and p27 in cells allowed to aggregate in three-dimensional culture. ( b ) Time course demonstrating changes in p27 and cyclin D1 protein levels as cells aggregate in three-dimensional culture. Cells transfected with E-cadherin ( Ecad3 ) grown in the presence or absence of 2 μg/ml DECMA-1 antibody for the indicated times were probed for p27 and cyclin D1 by immunoblotting. At time = 0 cells were transferred from two- to three-dimensional culture.

Techniques Used: Western Blot, Transfection

Morphology of EMT/6 cells displaying either E-cadherin or HA-dependent intercellular adhesion in three-dimensional culture. ( a–c ) EMT/6 cells transfected with E-cadherin (Ecad9); ( d ) with neomycin vector alone (neo8), or ( e and f ) Pc5-T cells with HA-dependent adhesion were cultured with 1,000 U/ml hyaluronidase ( a–d, f ), 10 μg/ml DECMA-1 antibody ( c and e ), or 10 μg/ml of GoH3 anti-α6-integrin antibody ( b ). Cells were photographed after 24 h in three-dimensional culture. Bar, 50 μm.

Figure Legend Snippet: Morphology of EMT/6 cells displaying either E-cadherin or HA-dependent intercellular adhesion in three-dimensional culture. ( a–c ) EMT/6 cells transfected with E-cadherin (Ecad9); ( d ) with neomycin vector alone (neo8), or ( e and f ) Pc5-T cells with HA-dependent adhesion were cultured with 1,000 U/ml hyaluronidase ( a–d, f ), 10 μg/ml DECMA-1 antibody ( c and e ), or 10 μg/ml of GoH3 anti-α6-integrin antibody ( b ). Cells were photographed after 24 h in three-dimensional culture. Bar, 50 μm.

Techniques Used: Transfection, Plasmid Preparation, Cell Culture

3) Product Images from "Anticancer activity of paclitaxel-loaded keratin nanoparticles in two-dimensional and perfused three-dimensional breast cancer models"

Article Title: Anticancer activity of paclitaxel-loaded keratin nanoparticles in two-dimensional and perfused three-dimensional breast cancer models

Journal: International Journal of Nanomedicine

doi: 10.2147/IJN.S159942

Antiproliferative activity of PTX in a free form, HSA-NPs-PTX, and KER-NPs-PTX on MCF-7 and MDA MB 231 cell lines in 2D model. Notes: Cell viability was evaluated 72 h after exposure to increasing concentrations of PTX (0.00002, 0.02, and 5 µg/mL) by APH assay. Statistical significance versus untreated cells (100%, represented by a dotted line): ** P

Figure Legend Snippet: Antiproliferative activity of PTX in a free form, HSA-NPs-PTX, and KER-NPs-PTX on MCF-7 and MDA MB 231 cell lines in 2D model. Notes: Cell viability was evaluated 72 h after exposure to increasing concentrations of PTX (0.00002, 0.02, and 5 µg/mL) by APH assay. Statistical significance versus untreated cells (100%, represented by a dotted line): ** P

Techniques Used: Activity Assay, Multiple Displacement Amplification

BAX and BCL-2 gene expression analyses in MCF-7 and MDA MB 231 cells in p3D cultures following 24 h treatments. Notes: Cells were incubated for 24 h with PTX in a free form, HSA-NPs-PTX, or KER-NPs-PTX (PTX, 5 µg/mL). GAPDH was used as reference gene to normalize data. The effects of each treatment were compared with gene expression detectable in untreated cells (=1) as indicated by the dotted line. Statistically significant difference versus untreated cells: * P

Figure Legend Snippet: BAX and BCL-2 gene expression analyses in MCF-7 and MDA MB 231 cells in p3D cultures following 24 h treatments. Notes: Cells were incubated for 24 h with PTX in a free form, HSA-NPs-PTX, or KER-NPs-PTX (PTX, 5 µg/mL). GAPDH was used as reference gene to normalize data. The effects of each treatment were compared with gene expression detectable in untreated cells (=1) as indicated by the dotted line. Statistically significant difference versus untreated cells: * P

Techniques Used: Expressing, Multiple Displacement Amplification, Incubation

Representative H E staining of scaffold sections from p3D MCF-7 and MDA MB 231 cultures after treatments. Notes: MCF-7 (upper panels) and MDA MB 231 (lower panels) cells were initially cultured for 7 and 4 days, respectively, and then left untreated ( A ) or treated for 48 h with PTX in a free form ( B ), HSA-NPs-PTX ( C ), and KER-NPs-PTX ( D ) (PTX, 5 µg/mL). Scale bar: 100 µm. Abbreviations: H E, hematoxylin and eosin; HSA-NPs-PTX, PTX loaded in albumin nanoparticles; KER-NPs-PTX, PTX loaded in keratin nanoparticles; p3D, three-dimensional model with perfused bioreactor; PTX, paclitaxel.

Figure Legend Snippet: Representative H E staining of scaffold sections from p3D MCF-7 and MDA MB 231 cultures after treatments. Notes: MCF-7 (upper panels) and MDA MB 231 (lower panels) cells were initially cultured for 7 and 4 days, respectively, and then left untreated ( A ) or treated for 48 h with PTX in a free form ( B ), HSA-NPs-PTX ( C ), and KER-NPs-PTX ( D ) (PTX, 5 µg/mL). Scale bar: 100 µm. Abbreviations: H E, hematoxylin and eosin; HSA-NPs-PTX, PTX loaded in albumin nanoparticles; KER-NPs-PTX, PTX loaded in keratin nanoparticles; p3D, three-dimensional model with perfused bioreactor; PTX, paclitaxel.

Techniques Used: Staining, Multiple Displacement Amplification, Cell Culture

BAX and BCL-2 gene expression analyses in MCF-7 and MDA MB 231 cells cultured in 2D model upon 12 h treatment. Notes: Cells were incubated for 12 h with PTX in a free form, HSA-NPs-PTX, or KER-NPs-PTX (PTX, 5 µg/mL). GAPDH was used as reference gene to normalize data. Effects of each treatment on gene expression levels were compared with those detectable in untreated cells (n=1) as indicated by the dotted line. Statistically significant difference versus untreated cells: * P

Figure Legend Snippet: BAX and BCL-2 gene expression analyses in MCF-7 and MDA MB 231 cells cultured in 2D model upon 12 h treatment. Notes: Cells were incubated for 12 h with PTX in a free form, HSA-NPs-PTX, or KER-NPs-PTX (PTX, 5 µg/mL). GAPDH was used as reference gene to normalize data. Effects of each treatment on gene expression levels were compared with those detectable in untreated cells (n=1) as indicated by the dotted line. Statistically significant difference versus untreated cells: * P

Techniques Used: Expressing, Multiple Displacement Amplification, Cell Culture, Incubation

Effects of PTX in a free form or vehiculated by HSA-NPs or by KER-NPs on cell death in p3D cultures. Notes: MCF-7 and MDA MB 231 cells were exposed to PTX in a free form, HSA-NPs-PTX, and KER-NPs-PTX (PTX, 5 µg/mL) for 24 and 48 h. Apoptosis assays were carried out by flow cytometry, following APC-Annexin V and PI staining. Representative dot plots of MCF-7 ( A ) and MDA MB 231 ( B ) cell lines after each treatment. Percentages of early apoptotic cells (positive to APC-Annexin V and negative to PI) and late apoptotic cells (positive to APC-Annexin V and PI) were evaluated 24 and 48 h after treatment ( C ). Statistical significance versus untreated cells: * P

Figure Legend Snippet: Effects of PTX in a free form or vehiculated by HSA-NPs or by KER-NPs on cell death in p3D cultures. Notes: MCF-7 and MDA MB 231 cells were exposed to PTX in a free form, HSA-NPs-PTX, and KER-NPs-PTX (PTX, 5 µg/mL) for 24 and 48 h. Apoptosis assays were carried out by flow cytometry, following APC-Annexin V and PI staining. Representative dot plots of MCF-7 ( A ) and MDA MB 231 ( B ) cell lines after each treatment. Percentages of early apoptotic cells (positive to APC-Annexin V and negative to PI) and late apoptotic cells (positive to APC-Annexin V and PI) were evaluated 24 and 48 h after treatment ( C ). Statistical significance versus untreated cells: * P

Techniques Used: Multiple Displacement Amplification, Flow Cytometry, Cytometry, Staining

KER-NPs-PTX analysis. Notes: Transmission electron microscopy images of fixed KER-NPs-PTX at two magnifications: scale bar 2 µm ( A ) and scale bar 200 nm ( B ). Morphological analysis showed particles spherical in shape, smooth surface, and an average dry diameter of ~80 nm. Stability of KER-NPs-PTX in physiological conditions ( C ). Fluorescence spectra of KER-NPs-PTX at different PTX loading percentages ( D ). Abbreviations: KER-NPs-PTX, PTX loaded in keratin nanoparticles; PDI, polydispersity index; PTX, paclitaxel.

Figure Legend Snippet: KER-NPs-PTX analysis. Notes: Transmission electron microscopy images of fixed KER-NPs-PTX at two magnifications: scale bar 2 µm ( A ) and scale bar 200 nm ( B ). Morphological analysis showed particles spherical in shape, smooth surface, and an average dry diameter of ~80 nm. Stability of KER-NPs-PTX in physiological conditions ( C ). Fluorescence spectra of KER-NPs-PTX at different PTX loading percentages ( D ). Abbreviations: KER-NPs-PTX, PTX loaded in keratin nanoparticles; PDI, polydispersity index; PTX, paclitaxel.

Techniques Used: Transmission Assay, Electron Microscopy, Fluorescence

Figure Legend Snippet: Profiles and mechanisms of PTX release from KER-NPs in vitro. Notes: Profile of PTX release from KER-NPs ( A ). Correlation coefficient values ( R 2 ) used to determine the best fitting model among zero-order, first-order, and Higuchi modes ( B ). Abbreviations: KER-NPs, keratin nanoparticles; PTX, paclitaxel.

Techniques Used: In Vitro

KER-NPs-PTX preparation. Notes: ( A ) KER-NPs-PTX preparation by aggregation method, starting from a solution of pure keratin powder. ( B ) Correlation between PTX loading and KER-NPs-PTX size. Abbreviations: KER-NPs-PTX, PTX loaded in keratin nanoparticles; PDI, polydispersity index; PTX, paclitaxel; RT, room temperature.

Figure Legend Snippet: KER-NPs-PTX preparation. Notes: ( A ) KER-NPs-PTX preparation by aggregation method, starting from a solution of pure keratin powder. ( B ) Correlation between PTX loading and KER-NPs-PTX size. Abbreviations: KER-NPs-PTX, PTX loaded in keratin nanoparticles; PDI, polydispersity index; PTX, paclitaxel; RT, room temperature.

Techniques Used:

Immunofluorescence staining of CC3 in MCF-7 (upper panels) and MDA MB 231 (lower panels) scaffold sections. Notes: Images show DAPI (blue) and CC3 (green) staining in MCF-7 ( A ) and MDA MB 231 ( B ) p3D scaffold sections upon treatment with PTX in a free form (b), HSA-NPs-PTX (c), and KER-NPs-PTX (d) (PTX, 5 µg/mL) for 48 h or untreated (a). Scale bar: 100 µm. Abbreviations: CC3, cleaved caspase 3; DAPI, 4′,6-diamidino-2-phenylindole; HSA-NPs-PTX, PTX loaded in albumin nanoparticles; KER-NPs-PTX, PTX loaded in keratin nanoparticles; p3D, three-dimensional model with perfused bioreactor; PTX, paclitaxel.

Figure Legend Snippet: Immunofluorescence staining of CC3 in MCF-7 (upper panels) and MDA MB 231 (lower panels) scaffold sections. Notes: Images show DAPI (blue) and CC3 (green) staining in MCF-7 ( A ) and MDA MB 231 ( B ) p3D scaffold sections upon treatment with PTX in a free form (b), HSA-NPs-PTX (c), and KER-NPs-PTX (d) (PTX, 5 µg/mL) for 48 h or untreated (a). Scale bar: 100 µm. Abbreviations: CC3, cleaved caspase 3; DAPI, 4′,6-diamidino-2-phenylindole; HSA-NPs-PTX, PTX loaded in albumin nanoparticles; KER-NPs-PTX, PTX loaded in keratin nanoparticles; p3D, three-dimensional model with perfused bioreactor; PTX, paclitaxel.

Techniques Used: Immunofluorescence, Staining, Multiple Displacement Amplification

Induction of apoptosis in tumor cells cultured in 2D by PTX in a free form, HSA-NPs-PTX, or KER-NPs-PTX in 2D model. Notes: MCF-7 and MDA MB 231 cells were exposed to PTX, HSA-NPs-PTX, and KER-NPs-PTX (PTX, 5 µg/mL) for 24 and 48 h. Apoptosis assays were carried out by flow cytometry, following APC-Annexin V and PI staining. Representative dot plots of MCF-7 ( A ) and MDA MB 231 ( B ) cell lines after each treatment. Percentage of early apoptotic cells (positive to APC-Annexin V and negative to PI) and late apoptotic cells (positive to APC-Annexin V and PI) was evaluated 24 and 48 h after treatment ( C ). Statistical significance versus untreated cells: * P

Figure Legend Snippet: Induction of apoptosis in tumor cells cultured in 2D by PTX in a free form, HSA-NPs-PTX, or KER-NPs-PTX in 2D model. Notes: MCF-7 and MDA MB 231 cells were exposed to PTX, HSA-NPs-PTX, and KER-NPs-PTX (PTX, 5 µg/mL) for 24 and 48 h. Apoptosis assays were carried out by flow cytometry, following APC-Annexin V and PI staining. Representative dot plots of MCF-7 ( A ) and MDA MB 231 ( B ) cell lines after each treatment. Percentage of early apoptotic cells (positive to APC-Annexin V and negative to PI) and late apoptotic cells (positive to APC-Annexin V and PI) was evaluated 24 and 48 h after treatment ( C ). Statistical significance versus untreated cells: * P

Techniques Used: Cell Culture, Multiple Displacement Amplification, Flow Cytometry, Cytometry, Staining

4) Product Images from "Anticancer activity of paclitaxel-loaded keratin nanoparticles in two-dimensional and perfused three-dimensional breast cancer models"

Article Title: Anticancer activity of paclitaxel-loaded keratin nanoparticles in two-dimensional and perfused three-dimensional breast cancer models

Journal: International Journal of Nanomedicine

doi: 10.2147/IJN.S159942

Techniques Used: Expressing, Multiple Displacement Amplification, Incubation

Techniques Used: Staining, Multiple Displacement Amplification, Cell Culture

Techniques Used: Multiple Displacement Amplification, Flow Cytometry, Cytometry, Staining

Techniques Used: Immunofluorescence, Staining, Multiple Displacement Amplification

5) Product Images from "Downstream of Mutant KRAS, the Transcription Regulator YAP Is Essential for Neoplastic Progression to Pancreatic Ductal Adenocarcinoma"

Article Title: Downstream of Mutant KRAS, the Transcription Regulator YAP Is Essential for Neoplastic Progression to Pancreatic Ductal Adenocarcinoma

Journal: Science signaling

doi: 10.1126/scisignal.2005049

Figure Legend Snippet: Deletion of Yap dampens the stromal response in Kras and Kras:Trp53 mutant pancreata

Techniques Used: Mutagenesis

6) Product Images from "Reagentless biosensor based on layer-by-layer assembly of functional multiwall carbon nanotubes and enzyme-mediator biocomposite *"

Article Title: Reagentless biosensor based on layer-by-layer assembly of functional multiwall carbon nanotubes and enzyme-mediator biocomposite *

Journal: Journal of Zhejiang University. Science. B

doi: 10.1631/jzus.B1000280

Schematic illustration of LBL assembly of PAH-MWNTs and HRP-MB on an Au electrode modified with a polyelectrolyte precursor film

Figure Legend Snippet: Schematic illustration of LBL assembly of PAH-MWNTs and HRP-MB on an Au electrode modified with a polyelectrolyte precursor film

Techniques Used: Modification

Figure Legend Snippet: UV-Vis absorption spectra of six bilayers of PAH/HRP-MB (a) and PAH-MWNTs/HRP-MB (b) on PET films

Techniques Used: Positron Emission Tomography

SEM images of one bilayer (a), three bilayers (b), and six bilayers (c) of PAH-MWNTs/HRP-MB on the Si-wafer surface, and six bilayers of PAH-MWNTs/HRP-MB at high-magnification (d)

Figure Legend Snippet: SEM images of one bilayer (a), three bilayers (b), and six bilayers (c) of PAH-MWNTs/HRP-MB on the Si-wafer surface, and six bilayers of PAH-MWNTs/HRP-MB at high-magnification (d)

Techniques Used:

Cyclic voltammograms of Au electrodes modified with six bilayers of PAH-MWNTs/HRP (a) and PAH-MWNTs/HRP-MB in the absence (b) and presence (c) of 3.0 mmol/L hydrogen peroxide in 0.2 mol/L PBS (pH 7.0) at a scan rate of 100 mV/s

Figure Legend Snippet: Cyclic voltammograms of Au electrodes modified with six bilayers of PAH-MWNTs/HRP (a) and PAH-MWNTs/HRP-MB in the absence (b) and presence (c) of 3.0 mmol/L hydrogen peroxide in 0.2 mol/L PBS (pH 7.0) at a scan rate of 100 mV/s

Techniques Used: Modification

7) Product Images from "Self-Organized Criticality Theory of Autoimmunity"

Article Title: Self-Organized Criticality Theory of Autoimmunity

Journal: PLoS ONE

doi: 10.1371/journal.pone.0008382

$TCR revision upon repeated immunization with antigen. (A) TCR CDR3 length profiles of mice immunized 8× with PBS, 2× or 8× with SEB. TCR repertoire of splenic CD4 + T cell was skewed only after immunization 8× with SEB. (B) Expression of V(D)J recombinase complex and related molecules in the spleen of PBS- or SEB-injected BALB/c mice. (C) GFP + cells in the Vβ8 + CD4 + T population of rag1/gfp knock-in mice. IgG-RF as induced in rag1/gfp knock-in mice after immunization 8× with SEB (lower left). The GFP + T cell fraction was also increased among Vβ8 + CD4 + T cells (mean ± SD, 4–5 mice/group). (D) TCRα chain revision in the spleen of mice immunized 8× with SEB was determined by LM-PCR detection of dsDNA breaks at the RSS flanking the TCRAV2 , with PCR-amplified TCRα constant region ( TCRAC ) as a DNA quality control.$
Figure Legend Snippet: TCR revision upon repeated immunization with antigen. (A) TCR CDR3 length profiles of mice immunized 8× with PBS, 2× or 8× with SEB. TCR repertoire of splenic CD4 + T cell was skewed only after immunization 8× with SEB. (B) Expression of V(D)J recombinase complex and related molecules in the spleen of PBS- or SEB-injected BALB/c mice. (C) GFP + cells in the Vβ8 + CD4 + T population of rag1/gfp knock-in mice. IgG-RF as induced in rag1/gfp knock-in mice after immunization 8× with SEB (lower left). The GFP + T cell fraction was also increased among Vβ8 + CD4 + T cells (mean ± SD, 4–5 mice/group). (D) TCRα chain revision in the spleen of mice immunized 8× with SEB was determined by LM-PCR detection of dsDNA breaks at the RSS flanking the TCRAV2 , with PCR-amplified TCRα constant region ( TCRAC ) as a DNA quality control.

Techniques Used: Mouse Assay, Expressing, Injection, Knock-In, Polymerase Chain Reaction, Amplification

8) Product Images from "Anticancer activity of paclitaxel-loaded keratin nanoparticles in two-dimensional and perfused three-dimensional breast cancer models"

Article Title: Anticancer activity of paclitaxel-loaded keratin nanoparticles in two-dimensional and perfused three-dimensional breast cancer models

Journal: International Journal of Nanomedicine

doi: 10.2147/IJN.S159942

Techniques Used: Activity Assay, Multiple Displacement Amplification

Techniques Used: Staining, Multiple Displacement Amplification, Cell Culture

Techniques Used: Expressing, Multiple Displacement Amplification, Cell Culture, Incubation

Techniques Used: Multiple Displacement Amplification, Flow Cytometry, Cytometry, Staining

Techniques Used: Transmission Assay, Electron Microscopy, Fluorescence

Techniques Used: In Vitro

Techniques Used:

Techniques Used: Immunofluorescence, Staining, Multiple Displacement Amplification

Techniques Used: Cell Culture, Multiple Displacement Amplification, Flow Cytometry, Cytometry, Staining

9) Product Images from "Anticancer activity of paclitaxel-loaded keratin nanoparticles in two-dimensional and perfused three-dimensional breast cancer models"

Article Title: Anticancer activity of paclitaxel-loaded keratin nanoparticles in two-dimensional and perfused three-dimensional breast cancer models

Journal: International Journal of Nanomedicine

doi: 10.2147/IJN.S159942

Techniques Used: Activity Assay, Multiple Displacement Amplification

Techniques Used: Expressing, Multiple Displacement Amplification, Incubation

Techniques Used: Staining, Multiple Displacement Amplification, Cell Culture

Techniques Used: Expressing, Multiple Displacement Amplification, Cell Culture, Incubation

Techniques Used: Multiple Displacement Amplification, Flow Cytometry, Cytometry, Staining

Techniques Used: Transmission Assay, Electron Microscopy, Fluorescence

Techniques Used: In Vitro

Techniques Used:

Techniques Used: Immunofluorescence, Staining, Multiple Displacement Amplification

Techniques Used: Cell Culture, Multiple Displacement Amplification, Flow Cytometry, Cytometry, Staining

10) Product Images from "Reagentless biosensor based on layer-by-layer assembly of functional multiwall carbon nanotubes and enzyme-mediator biocomposite *"

Article Title: Reagentless biosensor based on layer-by-layer assembly of functional multiwall carbon nanotubes and enzyme-mediator biocomposite *

Journal: Journal of Zhejiang University. Science. B

doi: 10.1631/jzus.B1000280

Figure Legend Snippet: Schematic illustration of LBL assembly of PAH-MWNTs and HRP-MB on an Au electrode modified with a polyelectrolyte precursor film

Techniques Used: Modification

Figure Legend Snippet: UV-Vis absorption spectra of six bilayers of PAH/HRP-MB (a) and PAH-MWNTs/HRP-MB (b) on PET films

Techniques Used: Positron Emission Tomography

Techniques Used:

Techniques Used: Modification

11) Product Images from "Neutrophil Extracellular Traps Contain Calprotectin, a Cytosolic Protein Complex Involved in Host Defense against Candida albicans"

Article Title: Neutrophil Extracellular Traps Contain Calprotectin, a Cytosolic Protein Complex Involved in Host Defense against Candida albicans

Journal: PLoS Pathogens

doi: 10.1371/journal.ppat.1000639

Identification of NET-associated proteins. (A) Silver stained SDS-PAGE and (B) immunoblots with samples from NET protein purification procedure. Human neutrophils were stimulated to form NETs. Supernatants from unstimulated (lane 1) and stimulated (lane 2) neutrophils; first wash (lane 3); second wash (lane 4); medium containing DNase-1 incubated with unstimulated neutrophils (lane 5); DNase-1-free medium incubated with washed NETs (lane 6); medium containing DNase-1 incubated with washed NETs (lane 7); medium containing DNase-1 incubated with washed NETs including protease inhibitor cocktail (lane 8).

Figure Legend Snippet: Identification of NET-associated proteins. (A) Silver stained SDS-PAGE and (B) immunoblots with samples from NET protein purification procedure. Human neutrophils were stimulated to form NETs. Supernatants from unstimulated (lane 1) and stimulated (lane 2) neutrophils; first wash (lane 3); second wash (lane 4); medium containing DNase-1 incubated with unstimulated neutrophils (lane 5); DNase-1-free medium incubated with washed NETs (lane 6); medium containing DNase-1 incubated with washed NETs (lane 7); medium containing DNase-1 incubated with washed NETs including protease inhibitor cocktail (lane 8).

Techniques Used: Staining, SDS Page, Western Blot, Protein Purification, Incubation, Protease Inhibitor

$Histones are altered during NET formation. NETs from human neutrophils were washed and digested with DNase-1. (A) The NET-fraction (N) and the remaining pellet after DNase-1 digest (P) were analyzed by immunoblotting at the indicated time points. Unstimulated neutrophils served as controls. All core histones have a reduced molecular mass (2–5 kDa less) in NETs compared to the pellet fraction and the unstimulated control. A representative experiment out of three in total is shown. (B) High-resolution SEM analysis of NETs which consist of smooth fibers (white box) and globular domains (diameter 25–50 nm, arrows), scale bar = 100 nm. (C) High-resolution FESEM analysis of smooth stretch of a singular NET-fiber. Signal intensities were profiled vertically and horizontally showing similar diameters to nucleosomes (depicted as cartoon structure models taken from [41] , with approximate horizontal and vertical diameters of 5 nm and 10 nm, respectively). One experiment out of two is shown.$
Figure Legend Snippet: Histones are altered during NET formation. NETs from human neutrophils were washed and digested with DNase-1. (A) The NET-fraction (N) and the remaining pellet after DNase-1 digest (P) were analyzed by immunoblotting at the indicated time points. Unstimulated neutrophils served as controls. All core histones have a reduced molecular mass (2–5 kDa less) in NETs compared to the pellet fraction and the unstimulated control. A representative experiment out of three in total is shown. (B) High-resolution SEM analysis of NETs which consist of smooth fibers (white box) and globular domains (diameter 25–50 nm, arrows), scale bar = 100 nm. (C) High-resolution FESEM analysis of smooth stretch of a singular NET-fiber. Signal intensities were profiled vertically and horizontally showing similar diameters to nucleosomes (depicted as cartoon structure models taken from [41] , with approximate horizontal and vertical diameters of 5 nm and 10 nm, respectively). One experiment out of two is shown.

Techniques Used:

12) Product Images from "Anticancer activity of paclitaxel-loaded keratin nanoparticles in two-dimensional and perfused three-dimensional breast cancer models"

Article Title: Anticancer activity of paclitaxel-loaded keratin nanoparticles in two-dimensional and perfused three-dimensional breast cancer models

Journal: International Journal of Nanomedicine

doi: 10.2147/IJN.S159942

Techniques Used: Activity Assay, Multiple Displacement Amplification

Techniques Used: Staining, Multiple Displacement Amplification, Cell Culture

Techniques Used: Expressing, Multiple Displacement Amplification, Cell Culture, Incubation

Techniques Used: Multiple Displacement Amplification, Flow Cytometry, Cytometry, Staining

Techniques Used: Transmission Assay, Electron Microscopy, Fluorescence

Techniques Used: In Vitro

Techniques Used:

Techniques Used: Immunofluorescence, Staining, Multiple Displacement Amplification

Techniques Used: Cell Culture, Multiple Displacement Amplification, Flow Cytometry, Cytometry, Staining

13) Product Images from "Anticancer activity of paclitaxel-loaded keratin nanoparticles in two-dimensional and perfused three-dimensional breast cancer models"

Article Title: Anticancer activity of paclitaxel-loaded keratin nanoparticles in two-dimensional and perfused three-dimensional breast cancer models

Journal: International Journal of Nanomedicine

doi: 10.2147/IJN.S159942

Techniques Used: Activity Assay, Multiple Displacement Amplification

Techniques Used: Expressing, Multiple Displacement Amplification, Incubation

Techniques Used: Staining, Multiple Displacement Amplification, Cell Culture

Techniques Used: Expressing, Multiple Displacement Amplification, Cell Culture, Incubation

Techniques Used: Multiple Displacement Amplification, Flow Cytometry, Cytometry, Staining

Techniques Used: Immunofluorescence, Staining, Multiple Displacement Amplification

Techniques Used: Cell Culture, Multiple Displacement Amplification, Flow Cytometry, Cytometry, Staining

Fluorescence:

Article Title: The Properties of Microparticles from RAW 264.7 Macrophage Cells Undergoing in vitro Activation or Apoptosis
Article Snippet: .. The concentration of DNA (ng/ml) was calculated according to fluorescence values for a standard solution of double-stranded DNA from calf thymus (Worthington Biochemical Corporation, Lakewood, NJ). .. Briefly, actively growing RAW 264.7 cells were plated at a density of 2-3 × 106 cells per T175 tissue culture flask in complete medium and incubated overnight at 37°C, 5% CO2 .

Isolation:

Article Title: Characterization of Valvular Interstitial Cell Function in Three Dimensional Matrix Metalloproteinase Degradable PEG Hydrogels
Article Snippet: .. Double stranded DNA (dsDNA) was isolated from similarly sized hydrogel constructs by papainase (Worthington) digestion at 60°C overnight. .. The resulting digestion solution was analyzed for dsDNA content using the Quant-It PicoGreen dsDNA assay (Invitrogen) per manufacturer's instructions.

Construct:

Enzyme-linked Immunosorbent Assay:

Article Title: The Inhibition of Anti-DNA Binding to DNA by Nucleic Acid Binding Polymers
Article Snippet: .. For the direct binding assay, wells of ELISA plates were coated with 5 µg/ml native double stranded calf thymus (CT) DNA (Worthington Biochemical, Lakewood, NJ) in 1 x SSC (150 mM NaCl, 15 mM Na citrate, pH 7) overnight at 4°C. .. For assays involving biotinylated DNA, native CT DNA was purified by phenol:chloroform extraction and then diluted to 0.5 mg/ml in 10 mM Tris, 1 mM EDTA buffer pH 8.0 (TE buffer).

Concentration Assay:

Article Title: Solution Structure of the B3 DNA Binding Domain of the Arabidopsis Cold-Responsive Transcription Factor RAV1 W⃞
Article Snippet: .. The concentration of the double-stranded DNA was determined using an extinction coefficient calculated after digestion of the strands with phosphodiesterase I (Worthington Biochemical, Lakewood, NJ). .. The HOMOLOGY module of Insight II (Accelrys, San Diego, CA) was used for the structural modeling of the ARF1- and ABI3-B3 domains based on the sequence homology to RAV1-B3.

Article Title: Structural Basis for Sequence-specific DNA Recognition by an Arabidopsis WRKY Transcription Factor *
Article Snippet: .. The concentration of the protein was determined at A 280 with an extinction coefficient estimated from the amino acid sequence , whereas that of the double-stranded DNA was determined at A 260 using an extinction coefficient that was calculated after digestion of the strands with phosphodiesterase I (Worthington). .. For the NMR measurements, 0.4–1.0 m m 1:1 protein-DNA complex was dissolved in 20 m m potassium phosphate buffer (pH 6.0) containing 200 m m KCl, 20 μ m ZnCl2 , 1 m m deuterated dithiothreitol (Isotec Inc.), 0.05 m m sodium 2,2-dimethyl-2-silapentane-5-sulfonate, and 5% D2 O unless stated otherwise.

other:

Article Title: The Mycoplasma pneumoniae MPN229 gene encodes a protein that selectively binds single-stranded DNA and stimulates Recombinase A-mediated DNA strand exchange
Article Snippet: The DNA-cellulose was poured into a column, and protein was eluted stepwise by the addition of 0.5 ml of a buffer (20 mM Tris-HCl pH 7.5, 1 mM DTT) containing increasing concentrations of NaCl (from 200 to 1500 mM).

anti hla dq antibodies (Worthington Biochemical)

Structured Review

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Images

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3) Product Images from "Anticancer activity of paclitaxel-loaded keratin nanoparticles in two-dimensional and perfused three-dimensional breast cancer models"

4) Product Images from "Anticancer activity of paclitaxel-loaded keratin nanoparticles in two-dimensional and perfused three-dimensional breast cancer models"

5) Product Images from "Downstream of Mutant KRAS, the Transcription Regulator YAP Is Essential for Neoplastic Progression to Pancreatic Ductal Adenocarcinoma"

6) Product Images from "Reagentless biosensor based on layer-by-layer assembly of functional multiwall carbon nanotubes and enzyme-mediator biocomposite *"

7) Product Images from "Self-Organized Criticality Theory of Autoimmunity"

8) Product Images from "Anticancer activity of paclitaxel-loaded keratin nanoparticles in two-dimensional and perfused three-dimensional breast cancer models"

9) Product Images from "Anticancer activity of paclitaxel-loaded keratin nanoparticles in two-dimensional and perfused three-dimensional breast cancer models"

10) Product Images from "Reagentless biosensor based on layer-by-layer assembly of functional multiwall carbon nanotubes and enzyme-mediator biocomposite *"

11) Product Images from "Neutrophil Extracellular Traps Contain Calprotectin, a Cytosolic Protein Complex Involved in Host Defense against Candida albicans"

12) Product Images from "Anticancer activity of paclitaxel-loaded keratin nanoparticles in two-dimensional and perfused three-dimensional breast cancer models"

13) Product Images from "Anticancer activity of paclitaxel-loaded keratin nanoparticles in two-dimensional and perfused three-dimensional breast cancer models"

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Fluorescence:

Isolation:

Construct:

Enzyme-linked Immunosorbent Assay:

Concentration Assay:

other:

Sequencing:

Binding Assay:

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