goat anti mouse polyclonal antibodies against mmp2  (R&D Systems)

Journal: Frontiers in Immunology

Article Title: C-reactive protein deficiency ameliorates experimental abdominal aortic aneurysms

doi: 10.3389/fimmu.2023.1233807

Figure Lengend Snippet: CRP deficiency reduces aneurysmal aortic MMP2 expression. (A) : Representative immunostaining images for MMP2 and MMP9 in non-aneurysmal normal or aneurysmal (WT and CRP -/- ) aortas. (B, C) : Quantification of MMP2 and MMP9 expression (mean ± standard for the percentage of positively stained area in total aortic cross section area) in wild type and CRP -/- aneurysmal aortas. Student’s t tests, n=10-11 mice per group, ** p <0.01 compared to wild type mice.

Article Snippet: Reagents used in this study were monoclonal antibodies against CD68 (macrophages, 1:200, clone #: FA-11, Cat#: 137002), CD4 (CD4 + T cells, 1:200, clone #: GK1.5, Cat#: 100402), CD8 (CD8 + T cells, 1:200, clone #: 53-6.7, Cat#: 100702), B220 (B cells, 1:200, clone #: RA3-6B2, Cat#: 103202) and CD31 (1:200, clone#: 390, Cat#: 102402) (all above mentioned primary antibodies from Biolegend Inc, San Diego, CA, USA), goat anti-mouse polyclonal antibodies against MMP2 (1:200, Cat#: AF1488, R&D Systems) and MMP9 (1:200, Cat#: AF909, R&D Systems), a biotinylated goat anti-rat secondary antibody (1:400, Cat#: BA-9400, Vector Laboratories, Inc) or rabbit anti-goat IgG secondary antibody (1:400, Cat#: BA-5000, Vector Laboratories, Inc), and streptavidin-peroxidase conjugate (1:200, Cat#: 016-030-084, Jackson ImmunoResearch) ( – ).

Techniques: Expressing, Immunostaining, Staining

Journal:

Article Title: Expression of Matrix Metalloproteinases Subsequent to Urogenital Chlamydia muridarum Infection of Mice

doi: 10.1128/IAI.73.10.6962-6973.2005

Figure Lengend Snippet: Transcriptional analysis of MMP and TIMP genes

Article Snippet: To detect MMP-2 (gelatinase A) protein, PVDF membranes were probed with 0.25 μg/ml polyclonal goat anti-mouse MMP-2 (R&D Systems, Inc., Minneapolis, MN) and binding was detected using a 2 × 10 −4 dilution of peroxidase-conjugated rabbit anti-goat immunoglobulin G (IgG; Pierce-Endogen, Rockford, IL).

Techniques: Expressing

Journal:

Article Title: Expression of Matrix Metalloproteinases Subsequent to Urogenital Chlamydia muridarum Infection of Mice

doi: 10.1128/IAI.73.10.6962-6973.2005

Figure Lengend Snippet: Gelatin zymography for total MMP-2. Panel A shows typical zymograms of homogenized upper genital tract tissues from infected and uninfected C57BL/6 (top) and C3H/HeN (bottom) mice at various days postinfection. Both the 72-kDa latent and 68-kDa active forms have gelatinolytic activity on zymography (arrows, first lane in zymograms with uninfected mice). Abbreviations: Std, recombinant human MMP-2 standards. Panel B shows the results of gelatin zymography relative to total MMP-2 in upper genital tract homogenates. The top half of panel B represents the composite zymography results for infected mice, whereas the bottom half of panel B represents the same for uninfected controls followed in parallel with the infected mice. The black and gray bars represent the mean total MMP-2 gelatinolytic activity for tissues derived from C57BL/6 and C3H/HeN mice, respectively (six to eight samples per time point; results are composites of three or four experiments), plus or minus the standard deviation of the mean for each (error bars). Other than days 7 (P < 0.01, two-way t test) and 28 (P < 0.04, two-way t test) for infected C3H/HeN mice and day 14 (P < 0.02, two-way t test) for uninfected C3H/HeN mice, there was no significant elevation in MMP-2 activity relative to the C57BL/6 strain or to the uninfected mice in either strain. Asterisks indicate significant differences between strains of mice.

Article Snippet: To detect MMP-2 (gelatinase A) protein, PVDF membranes were probed with 0.25 μg/ml polyclonal goat anti-mouse MMP-2 (R&D Systems, Inc., Minneapolis, MN) and binding was detected using a 2 × 10 −4 dilution of peroxidase-conjugated rabbit anti-goat immunoglobulin G (IgG; Pierce-Endogen, Rockford, IL).

Techniques: Zymography, Infection, Activity Assay, Recombinant, Derivative Assay, Standard Deviation

Journal:

Article Title: Expression of Matrix Metalloproteinases Subsequent to Urogenital Chlamydia muridarum Infection of Mice

doi: 10.1128/IAI.73.10.6962-6973.2005

Figure Lengend Snippet: Detection of total MMP-2 and proMMP-9 by antigen capture EIA. (A) These data represent the mean nanograms (ng) of total MMP-2 per mg protein in upper urogenital tissue homogenates derived from C57BL/6 (black bars) or C3H/HeN (gray bars) mice plus or minus the standard deviation (error bars). There was no significant elevation in total MMP-2 by this assay in either strain at any time point postinfection relative to day 0. However, total MMP-2 was elevated in C3H/HeN relative to C57BL/6 mice on days 0, 21, and 28 postinfection (P < 0.04 in each case by a two-way t test). (B) These data represent the ng of proMMP-9 per mg total protein in the same upper genital tract homogenates shown for total MMP-2 in panel A. Significant elevation in proMMP-9 relative to day 0 was first observed in C57BL/6 mice at day 4 and for C3H/HeN mice at day 7 and persisted through day 56 for both strains (P < 0.05 by a two-way t test in each case). A significant elevation of proMMP-9 in the C57BL/6 mice relative to the C3H/HeN mice was observed on day 21 postinfection (P < 0.02).

Article Snippet: To detect MMP-2 (gelatinase A) protein, PVDF membranes were probed with 0.25 μg/ml polyclonal goat anti-mouse MMP-2 (R&D Systems, Inc., Minneapolis, MN) and binding was detected using a 2 × 10 −4 dilution of peroxidase-conjugated rabbit anti-goat immunoglobulin G (IgG; Pierce-Endogen, Rockford, IL).

Techniques: Derivative Assay, Standard Deviation