Mab911

Manufactured by R&D Systems

Sourced in United States

MAB911 is a mouse monoclonal antibody that recognizes human CD11b. CD11b is an integrin alpha subunit that forms the complement receptor 3 (CR3) complex with CD18. CR3 plays a role in the adhesion and migration of immune cells.

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Lab products found in correlation

5 protocols using mab911

Antibody Panel for TGF-β1 and MMPs

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The recombinant protein for human TGF-β1 (#P01137) and mouse monoclonal antibodies against human TIMP-1 (#MAB970), TIMP-3 (#MAB973), MMP-2 (#MAB9022), and MMP-9 (#MAB911) were acquired from R&D Systems, Inc (MN, USA). The rabbit polyclonal antibodies against CTGF (#ab6992), fibronectin (#ab2413), and α-SMA (#ab5694) were acquired from Abcam Inc. (Cambridge, UK). The mouse monoclonal antibodies against p38 (#ab31828), p38 phosphorylation (p-p38, #ab4822), JNK (#ab208035), JNK phosphorylation (p-p38, #ab76572), ERK (#ab184699), and ERK phosphorylation (p-p38, #ab201015) were all acquired from Abcam Inc. (Cambridge, UK). The secondary antibodies against rabbit (#A5795) and mouse (#A9044), as well as GAPDH (#G5262) and β-actin (#A5441), were acquired from Sigma-Aldrich (St. Louis, MO, USA) [6 (link)].

Hou T.Y., Wu S.B., Kau H.C, & Tsai C.C. (2021). JNK and p38 Inhibitors Prevent Transforming Growth Factor-β1-Induced Myofibroblast Transdifferentiation in Human Graves’ Orbital Fibroblasts. International Journal of Molecular Sciences, 22(6), 2952.

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Immunoblot Analysis of MMP-9 Secretion

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Media from the apical compartment were collected and electrophoresed on SDS-polyacrylamide gels and electroblotted onto Immobilon-P PVDF membranes. Membranes were blocked in Tris buffer (pH = 7.4) containing 5% powdered milk for one hour, washed, and incubated with primary MMP-9 antibody (MAB 911; R/D Systems) overnight at 4 °C. After incubation, samples were washed with borate saline (100 mM boric acid, 25 mM Na borate, 75 mM NaCl) and incubated with species-specific IgG horseradish peroxidase conjugates (at dilutions of 1:5000) for one hour. Immunoblots were then developed using ECL chemiluminescent kits (GE Healthcare, Piscataway, NJ, USA). 50 ng of recombinant MMP-9 (R/D Systems; Catalog #WBC018) was used as positive control. As a loading control, 50 μg protein/ sample was loaded for each immunoblot lane.

Kong M.Y., Whitley R.J., Peng N., Oster R., Schoeb T.R., Sullender W., Ambalavanan N., Clancy J.P., Gaggar A, & Blalock J.E. (2015). Matrix Metalloproteinase-9 Mediates RSV Infection in Vitro and in Vivo. Viruses, 7(8), 4230-4253.

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Western Blot Analysis of MMP1 and MMP9

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Protein samples were run on SDS-PAGE and transferred to nitrocellulose membranes. Membranes were blocked with 5% non-fat dry milk for 1 h at room temperature, and then incubated with primary rabbit monoclonal anti-MMP1 (Ab134184, AbCam, Waltham, MA, USA) or mouse monoclonal anti-MMP9 (MAB911; R&D Systems, Minneapolis, MN, USA) antibody (1:1000) at 4 °C overnight. Membranes were then washed three times in TBS-Tween and incubated with HRP-conjugated anti-mouse (W4021; Cytiva, Marlborough, MA, USA) or anti-rabbit (NA934V, Cytiva, Marlborough, MA, USA) secondary antibody (1:5000–1:10,000) for 1 h at room temperature. Membranes were then washed three times and imaged on a FluorChemR Imager (ProteinSimple, Minneapolis, MN, USA) using Western Lightning™ ECL solution (PerkinElmer, Akron, OH, USA). Images were semi-quantified using ImageJ (NIH).

Mlakar L., Garrett S.M., Watanabe T., Sanderson M., Nishimoto T., Heywood J., Helke K.L., Pilewski J.M., Herzog E.L, & Feghali-Bostwick C. (2022). Ameliorating Fibrosis in Murine and Human Tissues with END55, an Endostatin-Derived Fusion Protein Made in Plants. Biomedicines, 10(11), 2861.

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Analysis of MMP Expression and Activity

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MMP expression was analyzed by immunoblot in conditioned medium of LX‐2 cells, generated by cultivating the cells in serum‐deprived medium for 48 h, followed by protein concentration using vivaspin centrifugal concentrator columns (MWCO 3,0 kD, Sartorius GmbH). Protein contents were analyzed according to Bradford using Rotiquant (Roth, Karlsruhe, Germany). Either 20 or 40 μg of protein was loaded on 10% polyacrylamide gels and subsequently blotted on PVDF membranes. For the detection of specific proteins, the following antibodies were used: anti‐MMP‐2 (AF902, 2 μg·mL⁻¹; R&D Systems); anti‐MMP‐9 (MAB‐911, 4 μg·mL⁻¹, R&D); MMP‐7 (IMG‐3873; 0.5 μg·mL⁻¹, IMGENEX); MT1‐MMP/MMP‐14 (D1E4, 1 : 1000, Epitomics); TIMP‐2 (MAB971, 1 : 500, R&D). Protein contents were visualized on a ChemiDoc MP system using the imagelab software for quantification (both from Bio‐Rad Laboratories GmbH, Munich, Germany). For the demonstration of equal loading, the membranes were subsequently stained with Ponceau S (Sigma‐Aldrich). MMP‐2 and ‐9 activity was determined using gelatine containing zymography gels (Thermo Fisher Scientific, Karlsbad, CA, USA) as previously described [41 (link)].

El‐Ayoubi A., Arakelyan A., Klawitter M., Merk L., Hakobyan S., Gonzalez‐Menendez I., Quintanilla Fend L., Holm P.S., Mikulits W., Schwab M., Danielyan L, & Naumann U. (2023). Development of an optimized, non‐stem cell line for intranasal delivery of therapeutic cargo to the central nervous system. Molecular Oncology, 18(3), 528-546.

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Quantifying Myocardial MMP-9 Expression

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The cardiac infarct area was excised and lysed in RIPA buffer (50 mM Tris, 150 mM NaCl, 1% Triton X-100, 0.5% sodium deoxycholate, 0.1% SDS, pH 8.0) supplemented with a protease inhibitor cocktail (Complete Mini, Roche) using a tissue homogenizer (TissueLyser LT, Qiagen). Aliquots (30 μg) of total protein were separated by SDS-polyacrylamide gel electrophoresis and transferred to nitrocellulose membranes. After blocking for 1 h in Trisbuffered saline containing 0.1% Tween 20 and 5% skim milk (Carl Roth), membranes were probed overnight at 4°C with primary antibody against MMP-9 (R&D, MAB911; 1/2000 dilution) or 60 min for GAPDH (Sigma-Aldrich, G954; 1/10000). Densitometric quantification of protein bands was performed using ImageJ software (NIH, Bethesda, MD, USA) and MMP9 expression was normalized to GAPDH.

Schloss M.J., Horckmans M., Guillamat-Prats R., Hering D., Lauer E., Lenglet S., Weber C., Thomas A, & Steffens S. (2019). 2-Arachidonoylglycerol mobilizes myeloid cells and worsens heart function after acute myocardial infarction. Cardiovascular research, 115(3).

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