Mmp 9 antibody

Manufactured by Santa Cruz Biotechnology

Sourced in United States, Hong Kong, China

The MMP-9 antibody is a laboratory tool used for the detection and quantification of the matrix metalloproteinase-9 (MMP-9) protein. MMP-9 is an enzyme involved in the breakdown of extracellular matrix components, which plays a role in various physiological and pathological processes. The antibody can be used in techniques such as Western blotting, ELISA, and immunohistochemistry to measure MMP-9 levels in biological samples.

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Lab products found in correlation

Mmp 2 antibody, by Santa Cruz Biotechnology (2 mentions) Taq pcr mastermix, by Tiangen Biotech (1 mentions) Collagen 4 antibody, by Abcam (1 mentions) Cdna synthesis kit, by Takara Bio (1 mentions) Total rna extraction kit, by Tiangen Biotech (1 mentions) Horseradish peroxidase conjugated secondary antibody, by Zhongshan Golden Bridge Biotechnology (1 mentions) Proteinase inhibitor, by Roche (1 mentions) Vascular endothelial growth factor (vegf), by Santa Cruz Biotechnology (1 mentions) Lysis buffer, by Beyotime (1 mentions) Radioimmunoprecipitation assay buffer, by Thermo Fisher Scientific (1 mentions) Goat anti mouse secondary antibody, by Beyotime (1 mentions) Pvdf membrane, by Thermo Fisher Scientific (1 mentions) Gapdh antibody, by Santa Cruz Biotechnology (1 mentions) Tween 20, by Merck Group (1 mentions) Mmp 9 inhibitor 1, by Merck Group (1 mentions) Quikchange 2 site directed mutagenesis kit, by Agilent Technologies (1 mentions) Normal rabbit serum, by Santa Cruz Biotechnology (1 mentions) Protein a g agarose bead, by Santa Cruz Biotechnology (1 mentions) Image studio lite version 4, by LI COR (1 mentions) Vimentin antibody, by Santa Cruz Biotechnology (1 mentions)

Close spelling variants of this product

Anti-MMP-9 antibody Rabbit anti-MMP-9 antibody Goat polyclonal MMP-9 antibody Rabbit MMP-9 antibody MMP-9

8 protocols using mmp 9 antibody

Immunohistochemical Analysis of MMP-9 in Liver Tissue

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For immunohistochemistry, liver sections (4 μm) were deparaffinized and then boiled to unmask antigen sites; the endogenous activity of peroxidase was quenched with 0.03% H₂O₂ in absolute methanol. Liver sections were incubated overnight at 4°C with a 1 : 200 dilution of goat polyclonal MMP-9 antibodies (Santa Cruz CA, USA) in phosphate buffered saline (PBS). After removal of the unbound primary antibodies by rinsing with PBS, slides were incubated with a 1 : 500 dilution of biotinylated anti-goat secondary antibody. Bound antibodies were detected with avidin biotinylated peroxidase complex ABC-kit Vectastain and the chromogen 3,3′ diaminobenzidine tetrachloride (DAB) is used as substrate. After appropriate washing in PBS, slides were counterstained with hematoxylin. All sections were incubated under the same conditions with the same concentration of antibodies and at the same time; so the immunostaining was comparable among the different experimental groups.

Al-Olayan E.M., El-Khadragy M.F., Aref A.M., Othman M.S., Kassab R.B, & Abdel Moneim A.E. (2014). The Potential Protective Effect of Physalis peruviana L. against Carbon Tetrachloride-Induced Hepatotoxicity in Rats Is Mediated by Suppression of Oxidative Stress and Downregulation of MMP-9 Expression. Oxidative Medicine and Cellular Longevity, 2014, 381413.

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Investigating Matrix Metalloproteinase Regulation

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Bleomycin was purchased from Zhejiang Hisun Pharmaceutical Co., Ltd. (Taizhou, China). Artesunate was purchased from Guilin Pharmaceutical Co., Ltd. (Guilin, China). Primers were synthesized by Invitrogen Life Technologies (Shanghai, China). The cDNA synthesis kit was purchased from Takara Biotechnology Co., Ltd. (Dalian, China). The total RNA extraction kit and 2x Taq PCR Master mix were obtained from Tiangen Biotech Co., Ltd. (Beijing, China). The TIMP-1 and TIMP-2 antibodies and horseradish peroxidase-conjugated secondary antibodies were purchased from Beijing Zhongshan Golden Bridge Biotechnology Co., Ltd. (Beijing, China). Collagen-IV antibody was purchased from Abcam Ltd. (Hong Kong, China). MMP-2 antibody and MMP-9 antibodies were purchased from Santa Cruz Biotechnology, Inc. (Hong Kong, China).

Wang Y., Huang G., Mo B, & Wang C. (2016). Artesunate modulates expression of matrix metalloproteinases and their inhibitors as well as collagen-IV to attenuate pulmonary fibrosis in rats. Genetics and molecular research : GMR, 15(2).

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Western Blot Analysis of Protein Expression

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Cells (1 × 10⁶) were collected and washed with PBS three times. The total protein was extracted by lysis buffer (Beyotime) containing 1X proteinase inhibitor (Roche) for 30 minutes on ice. The supernatants were collected by centrifugation. 20 μg of protein was loaded on SDS-PAGE (12.5%) and transferred onto the PVDF membranes. After being blocked by notfat milk, diluted primary antibodies and relevant HRP conjugated secondary antibodies were incubated, ECL detection reagents and X-ray film espousing were used to detect the protein expression. The GOLM1, B7-H3 antibody (Abcam), actin, VEGF, MMP-9 antibody (Santa Cruz), and E-cadherin antibody (CST) were used according to the manufacturer's recommendations.

Guan J., Qin Y., Deng G, & Zhao H. (2022). GOLM1 as a Potential Therapeutic Target Modulates B7-H3 Secretion to Drive Ovarian Cancer Metastasis. Evidence-based Complementary and Alternative Medicine : eCAM, 2022, 5151065.

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Western Blot Analysis of TIMP2, MMP2, and MMP9

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Cells were lysed in cold radioimmunoprecipitation assay buffer (Thermo Fisher Scientific, Inc.) and the protein concentration was determined using a bicinchoninic acid protein assay kit (Pierce; Thermo Fisher Scientific, Inc.). Proteins (30 µg) were separated by 10% SDS-PAGE and then transferred to a polyvinylidene difluoride (PVDF) membrane (Thermo Fisher Scientific, Inc.) The PVDF membrane was blocked with 5% non-fat milk in PBS containing 0.1% Tween-20 (Sigma-Aldrich; Merck KGaA) at room temperature for 3 h. Subsequently, the PVDF membrane was incubated with TIMP2 antibody (cat. no. sc-21735; 1:200; Santa Cruz Biotechnology, Inc.), MMP2 antibody (cat. no. sc-13594; 1:200; Santa Cruz Biotechnology, Inc.), MMP9 antibody (cat. no. sc-21733; 1:200; Santa Cruz Biotechnology, Inc.) and GAPDH antibody (cat. no. AF0006; 1:500; Beyotime Institute of Biotechnology) at room temperature for 3 h. Following washing with PBS for 10 min, the PVDF membrane was incubated with a goat anti-mouse secondary antibody (cat. no. ab64255; 1:1,000; Abcam) at room temperature for 1 h. Following further washing with PBS for 10 min, the protein bands were detected using an Enhanced Chemiluminescence Western Blotting kit (Pierce; Thermo Fisher Scientific, Inc.), according to the manufacturer's protocols.

, & Yuan C. (2019). miR-616 promotes breast cancer migration and invasion by targeting TIMP2 and regulating MMP signaling. Oncology Letters, 18(3), 2348-2355.

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Recombinant Histone and MMP-9 Expression

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Core histones and MMP-9 proteins were expressed in Escherichia coli Rosetta 2 (DE3) pLysS cells (Novagen) and purified from inclusion bodies as described recently [20 (link)]. To generate mutant H3 and MMP-9 expression vectors, H3 and MMP-9 cDNAs were mutated by the QuikChange II site-directed mutagenesis kit (Agilent Technologies) before the construction. Further details of plasmid constructions are available upon request. G9a inhibitor BIX01294 is from Santa Cruz Biotech, and EZH1/2 inhibitor UNC1999 and MMP-9 Inhibitor I are from Sigma. Antibodies used in this study are as follows: H2A, H2B, H3, H4, and EZH2 antibodies from Abcam; H3K27me1 and EZH1 antibodies from Millipore; G9a, actin, and FLAG antibodies from Sigma; His antibody from Novagen; and MMP-9 antibody from Santa Cruz Biotech.

Kim K., Shin Y., Kim J., Ulmer T.S, & An W. (2018). H3K27me1 is essential for MMP-9-dependent H3N-terminal tail proteolysis during osteoclastogenesis. Epigenetics & Chromatin, 11, 23.

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Immunoprecipitation and Western Blotting

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Leukocytes were lysed with lysis buffer containing 25mM Tris/HCl (pH 7.5), 50mM KCl, 2mM MgCl₂, 1mM EDTA, 0.5% Triton X-100, 0.5 mM PMSF and Complete protease inhibitor cocktail (Roche). The lysate was pre-cleared with 50 μl of normal rabbit serum (Santa Cruz) and protein A/G agarose beads (Santa Cruz) (20 μL). AMPKα antibody (1:150) (Santa Cruz) or MMP9 antibody (1:50) (Santa Cruz) were added to the cell lysate and incubated with gentle rocking overnight at 4°C. Afterwards, protein A/G agarose beads (20 μL) were added to the lysates, and the samples were incubated with gentle rocking for 3 hours at 4°C. Lysate was spun down and the pellet was washed 5 times with 500 μL of cell lysis buffer. The pellet was resuspended in 20 μL 4× sodium dodecyl sulfate sample buffer and heated to 97°C for 5 minutes. Subsequently, the samples were analyzed by western blotting. The PVDF membrane was blocked with 10% skim milk and incubated overnight with the specified antibodies. The specific signal was amplified by HRP-conjugated secondary antibodies, developed by ECL substrate (Pierce) and visualized by autoradiography.

Zhang Z., Amorosa L.F., Coyle S.M., Macor M.A., Lubitz S.E., Carson J.L., Birnbaum M.J., Lee L.Y, & Haimovich B. (2015). Proteolytic cleavage of AMPKα and intracellular MMP9 expression are both required for TLR4-mediated mTORC1 activation and HIF-1α expression in leukocytes. Journal of immunology (Baltimore, Md. : 1950), 195(5), 2452-2460.

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Quantification of Matrix Metalloproteinase Expression

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To confirm effects of OA treatment and OA knock down on MMP expression, protein extracts (10 μg) were resolved by SDS-PAGE, transferred to PVDF membranes and probed with antibodies to MMP-2 (72-kDa type IV collagenase, gelatinase A), -3 (stromelysin-1), -7 (matrilysin-1), -9 (92-kDa type IV collagenase, gelatinase B), -10 (stromelysin-2) and -13 (stromelysin-3). The MMP-9 antibody was obtained from Santa Cruz Biotechnology. The remaining MMP antibodies were obtained from R&D Systems (Minneapolis, Minnesota).
Blots were developed by enhanced chemiluminescence or infrared fluorescence imaging. At least three independent experiments were performed for Western blot analyses and densitometry was performed with LI-COR (Lincoln, Nebraska) Image Studio Lite version 4.0 software. β-actin was used as the endogenous control, and MMP band densities were normalized to β-actin. Representative experiments are presented.

Arosarena O.A., Barr E.W., Thorpe R., Yankey H., Tarr J.T, & Safadi F.F. (2017). OSTEOACTIVIN REGULATES HEAD AND NECK SQUAMOUS CELL CARCINOMA INVASION BY MODULATING MATRIX METALLOPROTEASES. Journal of cellular physiology, 233(1), 409-421.

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Western Blot Analysis of Cellular Proteins

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Total cellular protein was extracted using RIPA (#P0013B, Beyotime) and the protein concentration was determined by BCA assay (#BL521A, Biosharp). Subsequently, proteins present in the cell lysate were resolved using 10% SDS-PAGE gels and then transferred to PVDF membranes. To prevent non-specific interactions, the membranes were blocked with 5% milk for 1 h and then were stripped and incubated overnight at 4 °C with different primary antibodies: Mettl3 antibody (#ab66660 or #ab195352, Abcam), SOCS3 antibody (#ab280884, Abcam), SNAI1 antibody (#ab216347, Abcam), STAT3 antibody (#9139, CST), p-STAT3 antibody (#9145, CST), E-cadherin antibody (#ab133597, Abcam), Vimentin antibody (#sc-6260, Santa Cruz), MMP-9 antibody (#sc-21733, Santa Cruz), β-actin antibody (#AF5003, Beyotime, China) and GAPDH antibody (#AF1186, Beyotime, China). Afterward, the signals were visualized with ECL reagents (#P0018S, Beyotime) using ImageQuant LAS 4000 after incubating with the second antibody for 1 h. The grayscale of protein bands was determined by Image J.

Zhang Y., Wang L., Yan F., Yang M., Gao H, & Zeng Y. (2023). Mettl3 Mediated m6A Methylation Involved in Epithelial-Mesenchymal Transition by Targeting SOCS3/STAT3/SNAI1 in Cigarette Smoking-Induced COPD. International Journal of Chronic Obstructive Pulmonary Disease, 18, 1007-1017.

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