3050 Search Results


90
Spectrocell inc pathlength quartz cells
Pathlength Quartz Cells, supplied by Spectrocell inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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ma 10  (ATCC)
95
ATCC ma 10
Ma 10, supplied by ATCC, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Cell Signaling Technology Inc rabbit monoclonal 27d10
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R&D Systems experimental section recombinant human αvβ3 integrins
Experimental Section Recombinant Human αvβ3 Integrins, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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SouthernBiotech anti rat igg h l mouse ads
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93
SouthernBiotech biotin conjugated goat antirat immunoglobulin
(A,C,E) mHEVc cells and (B,D,F) HUVECs were incubated with isotype antibody-coated beads or anti–VCAM-1 antibody-coated beads. mHEVc cells were also incubated in the presence or absence of 10 μM GM6001. At the indicated time points, the cells were washed. Equal cell numbers were lysed, nuclei were removed by centrifugation, and supernatants were examined by zymography. (A–B) Representative zymograms of VCAM-1 activation of endothelial cell–associated MMPs. Arrows label the latent forms (pro-MMP) and smaller active forms of the MMPs. The activity of MMP-9 and MMP-2 were compared with migration by purified standards (data not shown). (C–D) Same as for panels A and B except with 0.01 M EDTA, indicating the cation dependence of MMP degradation of gelatin. (E–F) Densitometry analysis of the active forms of MMPs in zymograms from 3 experiments. Fold increase is the change in the active form of MMP activity as compared with the nonstimulated cultures. Presented are the mean ± SD. *P < .05 compared with mHEVc cells at 0 minutes. **P < .05 compared with anti–VCAM-1–bead-stimulated cells. (G) Western blots for 1 (MT1)–MMP, MMP-2, and MMP-9 expression using rabbit antihuman MT1-MMP (a kind gift from Qing-Xiang Amy Sang, Florida State University)21 (1:200), affinity-purified rabbit antihuman MMP-9 (no. SA-106; Biomol, Plymouth Meeting, PA) (1:200), or purified rabbit <t>antirat</t> MMP-2 (1:200) (no. AB19015; Chemicon) followed by a horseradish peroxidase (HRP)–conjugated donkey antirabbit secondary antibody (Amersham Pharmacia Biotech, Piscataway, NJ) (1:4000) and enhanced chemiluminescence (ECL) detection.
Biotin Conjugated Goat Antirat Immunoglobulin, supplied by SouthernBiotech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 93 stars, based on 1 article reviews
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94
R&D Systems αvβ3
(A,C,E) mHEVc cells and (B,D,F) HUVECs were incubated with isotype antibody-coated beads or anti–VCAM-1 antibody-coated beads. mHEVc cells were also incubated in the presence or absence of 10 μM GM6001. At the indicated time points, the cells were washed. Equal cell numbers were lysed, nuclei were removed by centrifugation, and supernatants were examined by zymography. (A–B) Representative zymograms of VCAM-1 activation of endothelial cell–associated MMPs. Arrows label the latent forms (pro-MMP) and smaller active forms of the MMPs. The activity of MMP-9 and MMP-2 were compared with migration by purified standards (data not shown). (C–D) Same as for panels A and B except with 0.01 M EDTA, indicating the cation dependence of MMP degradation of gelatin. (E–F) Densitometry analysis of the active forms of MMPs in zymograms from 3 experiments. Fold increase is the change in the active form of MMP activity as compared with the nonstimulated cultures. Presented are the mean ± SD. *P < .05 compared with mHEVc cells at 0 minutes. **P < .05 compared with anti–VCAM-1–bead-stimulated cells. (G) Western blots for 1 (MT1)–MMP, MMP-2, and MMP-9 expression using rabbit antihuman MT1-MMP (a kind gift from Qing-Xiang Amy Sang, Florida State University)21 (1:200), affinity-purified rabbit antihuman MMP-9 (no. SA-106; Biomol, Plymouth Meeting, PA) (1:200), or purified rabbit <t>antirat</t> MMP-2 (1:200) (no. AB19015; Chemicon) followed by a horseradish peroxidase (HRP)–conjugated donkey antirabbit secondary antibody (Amersham Pharmacia Biotech, Piscataway, NJ) (1:4000) and enhanced chemiluminescence (ECL) detection.
αvβ3, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/3050/Recombinant+Human+Integrin+alpha+V+beta+3+Protein%2C+CF/pmc05261028-237-16-25
Average 94 stars, based on 1 article reviews
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93
SouthernBiotech goat anti rat igg
(A,C,E) mHEVc cells and (B,D,F) HUVECs were incubated with isotype antibody-coated beads or anti–VCAM-1 antibody-coated beads. mHEVc cells were also incubated in the presence or absence of 10 μM GM6001. At the indicated time points, the cells were washed. Equal cell numbers were lysed, nuclei were removed by centrifugation, and supernatants were examined by zymography. (A–B) Representative zymograms of VCAM-1 activation of endothelial cell–associated MMPs. Arrows label the latent forms (pro-MMP) and smaller active forms of the MMPs. The activity of MMP-9 and MMP-2 were compared with migration by purified standards (data not shown). (C–D) Same as for panels A and B except with 0.01 M EDTA, indicating the cation dependence of MMP degradation of gelatin. (E–F) Densitometry analysis of the active forms of MMPs in zymograms from 3 experiments. Fold increase is the change in the active form of MMP activity as compared with the nonstimulated cultures. Presented are the mean ± SD. *P < .05 compared with mHEVc cells at 0 minutes. **P < .05 compared with anti–VCAM-1–bead-stimulated cells. (G) Western blots for 1 (MT1)–MMP, MMP-2, and MMP-9 expression using rabbit antihuman MT1-MMP (a kind gift from Qing-Xiang Amy Sang, Florida State University)21 (1:200), affinity-purified rabbit antihuman MMP-9 (no. SA-106; Biomol, Plymouth Meeting, PA) (1:200), or purified rabbit <t>antirat</t> MMP-2 (1:200) (no. AB19015; Chemicon) followed by a horseradish peroxidase (HRP)–conjugated donkey antirabbit secondary antibody (Amersham Pharmacia Biotech, Piscataway, NJ) (1:4000) and enhanced chemiluminescence (ECL) detection.
Goat Anti Rat Igg, supplied by SouthernBiotech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/3050/Goat+Anti-Rat+IgG(H%2BL)%2C+Mouse+ads-UNLB/10__1016_slash_S1074___7613_ascii40_03_ascii41_00305___4-165-17-20
Average 93 stars, based on 1 article reviews
goat anti rat igg - by Bioz Stars, 2026-10
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94
ATCC mouse tumor leydig cell line ma 10
(A,C,E) mHEVc cells and (B,D,F) HUVECs were incubated with isotype antibody-coated beads or anti–VCAM-1 antibody-coated beads. mHEVc cells were also incubated in the presence or absence of 10 μM GM6001. At the indicated time points, the cells were washed. Equal cell numbers were lysed, nuclei were removed by centrifugation, and supernatants were examined by zymography. (A–B) Representative zymograms of VCAM-1 activation of endothelial cell–associated MMPs. Arrows label the latent forms (pro-MMP) and smaller active forms of the MMPs. The activity of MMP-9 and MMP-2 were compared with migration by purified standards (data not shown). (C–D) Same as for panels A and B except with 0.01 M EDTA, indicating the cation dependence of MMP degradation of gelatin. (E–F) Densitometry analysis of the active forms of MMPs in zymograms from 3 experiments. Fold increase is the change in the active form of MMP activity as compared with the nonstimulated cultures. Presented are the mean ± SD. *P < .05 compared with mHEVc cells at 0 minutes. **P < .05 compared with anti–VCAM-1–bead-stimulated cells. (G) Western blots for 1 (MT1)–MMP, MMP-2, and MMP-9 expression using rabbit antihuman MT1-MMP (a kind gift from Qing-Xiang Amy Sang, Florida State University)21 (1:200), affinity-purified rabbit antihuman MMP-9 (no. SA-106; Biomol, Plymouth Meeting, PA) (1:200), or purified rabbit <t>antirat</t> MMP-2 (1:200) (no. AB19015; Chemicon) followed by a horseradish peroxidase (HRP)–conjugated donkey antirabbit secondary antibody (Amersham Pharmacia Biotech, Piscataway, NJ) (1:4000) and enhanced chemiluminescence (ECL) detection.
Mouse Tumor Leydig Cell Line Ma 10, supplied by ATCC, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/3050/MA-10%3B+Leydig+Cell+Tumor%3B+Mouse/pmc09219706-67-0-9
Average 94 stars, based on 1 article reviews
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94
Mini-Circuits minicircuits pos 150 vco reference
(A,C,E) mHEVc cells and (B,D,F) HUVECs were incubated with isotype antibody-coated beads or anti–VCAM-1 antibody-coated beads. mHEVc cells were also incubated in the presence or absence of 10 μM GM6001. At the indicated time points, the cells were washed. Equal cell numbers were lysed, nuclei were removed by centrifugation, and supernatants were examined by zymography. (A–B) Representative zymograms of VCAM-1 activation of endothelial cell–associated MMPs. Arrows label the latent forms (pro-MMP) and smaller active forms of the MMPs. The activity of MMP-9 and MMP-2 were compared with migration by purified standards (data not shown). (C–D) Same as for panels A and B except with 0.01 M EDTA, indicating the cation dependence of MMP degradation of gelatin. (E–F) Densitometry analysis of the active forms of MMPs in zymograms from 3 experiments. Fold increase is the change in the active form of MMP activity as compared with the nonstimulated cultures. Presented are the mean ± SD. *P < .05 compared with mHEVc cells at 0 minutes. **P < .05 compared with anti–VCAM-1–bead-stimulated cells. (G) Western blots for 1 (MT1)–MMP, MMP-2, and MMP-9 expression using rabbit antihuman MT1-MMP (a kind gift from Qing-Xiang Amy Sang, Florida State University)21 (1:200), affinity-purified rabbit antihuman MMP-9 (no. SA-106; Biomol, Plymouth Meeting, PA) (1:200), or purified rabbit <t>antirat</t> MMP-2 (1:200) (no. AB19015; Chemicon) followed by a horseradish peroxidase (HRP)–conjugated donkey antirabbit secondary antibody (Amersham Pharmacia Biotech, Piscataway, NJ) (1:4000) and enhanced chemiluminescence (ECL) detection.
Minicircuits Pos 150 Vco Reference, supplied by Mini-Circuits, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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90
SouthernBiotech goat anti rat igg h l txrd
(A,C,E) mHEVc cells and (B,D,F) HUVECs were incubated with isotype antibody-coated beads or anti–VCAM-1 antibody-coated beads. mHEVc cells were also incubated in the presence or absence of 10 μM GM6001. At the indicated time points, the cells were washed. Equal cell numbers were lysed, nuclei were removed by centrifugation, and supernatants were examined by zymography. (A–B) Representative zymograms of VCAM-1 activation of endothelial cell–associated MMPs. Arrows label the latent forms (pro-MMP) and smaller active forms of the MMPs. The activity of MMP-9 and MMP-2 were compared with migration by purified standards (data not shown). (C–D) Same as for panels A and B except with 0.01 M EDTA, indicating the cation dependence of MMP degradation of gelatin. (E–F) Densitometry analysis of the active forms of MMPs in zymograms from 3 experiments. Fold increase is the change in the active form of MMP activity as compared with the nonstimulated cultures. Presented are the mean ± SD. *P < .05 compared with mHEVc cells at 0 minutes. **P < .05 compared with anti–VCAM-1–bead-stimulated cells. (G) Western blots for 1 (MT1)–MMP, MMP-2, and MMP-9 expression using rabbit antihuman MT1-MMP (a kind gift from Qing-Xiang Amy Sang, Florida State University)21 (1:200), affinity-purified rabbit antihuman MMP-9 (no. SA-106; Biomol, Plymouth Meeting, PA) (1:200), or purified rabbit <t>antirat</t> MMP-2 (1:200) (no. AB19015; Chemicon) followed by a horseradish peroxidase (HRP)–conjugated donkey antirabbit secondary antibody (Amersham Pharmacia Biotech, Piscataway, NJ) (1:4000) and enhanced chemiluminescence (ECL) detection.
Goat Anti Rat Igg H L Txrd, supplied by SouthernBiotech, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/3050/Goat+Anti-Rat+IgG(H%2BL)%2C+Mouse+ads-TXRD/pmc05074851-85-42-51
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95
World Precision Instruments liquid waveguide capillary cell
(A,C,E) mHEVc cells and (B,D,F) HUVECs were incubated with isotype antibody-coated beads or anti–VCAM-1 antibody-coated beads. mHEVc cells were also incubated in the presence or absence of 10 μM GM6001. At the indicated time points, the cells were washed. Equal cell numbers were lysed, nuclei were removed by centrifugation, and supernatants were examined by zymography. (A–B) Representative zymograms of VCAM-1 activation of endothelial cell–associated MMPs. Arrows label the latent forms (pro-MMP) and smaller active forms of the MMPs. The activity of MMP-9 and MMP-2 were compared with migration by purified standards (data not shown). (C–D) Same as for panels A and B except with 0.01 M EDTA, indicating the cation dependence of MMP degradation of gelatin. (E–F) Densitometry analysis of the active forms of MMPs in zymograms from 3 experiments. Fold increase is the change in the active form of MMP activity as compared with the nonstimulated cultures. Presented are the mean ± SD. *P < .05 compared with mHEVc cells at 0 minutes. **P < .05 compared with anti–VCAM-1–bead-stimulated cells. (G) Western blots for 1 (MT1)–MMP, MMP-2, and MMP-9 expression using rabbit antihuman MT1-MMP (a kind gift from Qing-Xiang Amy Sang, Florida State University)21 (1:200), affinity-purified rabbit antihuman MMP-9 (no. SA-106; Biomol, Plymouth Meeting, PA) (1:200), or purified rabbit <t>antirat</t> MMP-2 (1:200) (no. AB19015; Chemicon) followed by a horseradish peroxidase (HRP)–conjugated donkey antirabbit secondary antibody (Amersham Pharmacia Biotech, Piscataway, NJ) (1:4000) and enhanced chemiluminescence (ECL) detection.
Liquid Waveguide Capillary Cell, supplied by World Precision Instruments, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


(A,C,E) mHEVc cells and (B,D,F) HUVECs were incubated with isotype antibody-coated beads or anti–VCAM-1 antibody-coated beads. mHEVc cells were also incubated in the presence or absence of 10 μM GM6001. At the indicated time points, the cells were washed. Equal cell numbers were lysed, nuclei were removed by centrifugation, and supernatants were examined by zymography. (A–B) Representative zymograms of VCAM-1 activation of endothelial cell–associated MMPs. Arrows label the latent forms (pro-MMP) and smaller active forms of the MMPs. The activity of MMP-9 and MMP-2 were compared with migration by purified standards (data not shown). (C–D) Same as for panels A and B except with 0.01 M EDTA, indicating the cation dependence of MMP degradation of gelatin. (E–F) Densitometry analysis of the active forms of MMPs in zymograms from 3 experiments. Fold increase is the change in the active form of MMP activity as compared with the nonstimulated cultures. Presented are the mean ± SD. *P < .05 compared with mHEVc cells at 0 minutes. **P < .05 compared with anti–VCAM-1–bead-stimulated cells. (G) Western blots for 1 (MT1)–MMP, MMP-2, and MMP-9 expression using rabbit antihuman MT1-MMP (a kind gift from Qing-Xiang Amy Sang, Florida State University)21 (1:200), affinity-purified rabbit antihuman MMP-9 (no. SA-106; Biomol, Plymouth Meeting, PA) (1:200), or purified rabbit antirat MMP-2 (1:200) (no. AB19015; Chemicon) followed by a horseradish peroxidase (HRP)–conjugated donkey antirabbit secondary antibody (Amersham Pharmacia Biotech, Piscataway, NJ) (1:4000) and enhanced chemiluminescence (ECL) detection.

Journal:

Article Title: Vascular cell adhesion molecule 1 (VCAM-1) activation of endothelial cell matrix metalloproteinases: role of reactive oxygen species

doi: 10.1182/blood-2004-02-0665

Figure Lengend Snippet: (A,C,E) mHEVc cells and (B,D,F) HUVECs were incubated with isotype antibody-coated beads or anti–VCAM-1 antibody-coated beads. mHEVc cells were also incubated in the presence or absence of 10 μM GM6001. At the indicated time points, the cells were washed. Equal cell numbers were lysed, nuclei were removed by centrifugation, and supernatants were examined by zymography. (A–B) Representative zymograms of VCAM-1 activation of endothelial cell–associated MMPs. Arrows label the latent forms (pro-MMP) and smaller active forms of the MMPs. The activity of MMP-9 and MMP-2 were compared with migration by purified standards (data not shown). (C–D) Same as for panels A and B except with 0.01 M EDTA, indicating the cation dependence of MMP degradation of gelatin. (E–F) Densitometry analysis of the active forms of MMPs in zymograms from 3 experiments. Fold increase is the change in the active form of MMP activity as compared with the nonstimulated cultures. Presented are the mean ± SD. *P < .05 compared with mHEVc cells at 0 minutes. **P < .05 compared with anti–VCAM-1–bead-stimulated cells. (G) Western blots for 1 (MT1)–MMP, MMP-2, and MMP-9 expression using rabbit antihuman MT1-MMP (a kind gift from Qing-Xiang Amy Sang, Florida State University)21 (1:200), affinity-purified rabbit antihuman MMP-9 (no. SA-106; Biomol, Plymouth Meeting, PA) (1:200), or purified rabbit antirat MMP-2 (1:200) (no. AB19015; Chemicon) followed by a horseradish peroxidase (HRP)–conjugated donkey antirabbit secondary antibody (Amersham Pharmacia Biotech, Piscataway, NJ) (1:4000) and enhanced chemiluminescence (ECL) detection.

Article Snippet: Antibody-coated beads Streptavidin-coated 9.9-μm diameter beads (40 μL; Bangs Laboratories, Fishers, IN) were labeled with 6 μg biotin-conjugated goat antirat immunoglobulin (no. 3050-08; Southern Biotech, Birmingham, AL) in 75 μL phosphate-buffered saline (PBS) with gentle rocking for 1 hour at 4°C and then washed 3 times.

Techniques: Incubation, Centrifugation, Zymography, Activation Assay, Activity Assay, Migration, Purification, Western Blot, Expressing, Affinity Purification