Anti mmp 9

Manufactured by Bioworld Technology

Sourced in United States

Anti-MMP-9 is a laboratory reagent used for the detection and quantification of the Matrix Metalloproteinase-9 (MMP-9) protein. MMP-9 is an enzyme involved in the degradation of the extracellular matrix and is associated with various physiological and pathological processes. The Anti-MMP-9 reagent can be used in various analytical techniques, such as ELISA and Western blotting, to measure MMP-9 levels in biological samples.

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Lab products found in correlation

Anti mmp 2, by Bioworld Technology (5 mentions) Anti e cadherin, by Bioworld Technology (3 mentions) Anti vimentin, by Bioworld Technology (3 mentions) Anti ngf, by Abcam (2 mentions) Anti β actin, by Cell Signaling Technology (1 mentions) Anti c met, by Cell Signaling Technology (1 mentions) Anti p c met, by Cell Signaling Technology (1 mentions) Sb431542, by Merck Group (1 mentions) Anti bdnf, by Abcam (1 mentions) Anti gdnf, by Abcam (1 mentions) Rhnodal, by R&D Systems (1 mentions) Mouse anti flag m2, by Merck Group (1 mentions) Anti smad2, by Bioworld Technology (1 mentions) Rabbit anti phospho smad3, by Cell Signaling Technology (1 mentions) Lysis buffer, by Beyotime (1 mentions) Anti β actin, by Bioworld Technology (1 mentions) β actin, by Beyotime (1 mentions) Horseradish peroxidase conjugated goat anti rabbit or anti mouse igg, by Beyotime (1 mentions) Anti cdc2, by Bioworld Technology (1 mentions) Ix81 microscope, by Olympus (1 mentions)

7 protocols using anti mmp 9

Culturing and Characterizing Human Pancreatic Cell Lines

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Human PC cell lines (AsPC-1, BxPC-3, CFPAC-1, Panc-1, and SW1990) and rat Schwann cells
(RSC96) were purchased from the Chinese Academy of Sciences Cell Bank of Type Culture
Collection (CBTCCCAS). All cell lines were cultured in the proper medium (HyClone, Logan,
UT, USA) supplemented with 10% fetal bovine serum (FBS), 100 μg/mL ampicillin, and 100
μg/mL streptomycin under a humidified atmosphere at 37°C with 5% CO₂.
Recombinant human HGF (rhHGF) was purchased from ProSpec (ProSpec-Tany TechnoGene,
Rehovot, Israel). Antibodies were purchased from the following sources: anti-c-Met,
anti-p-c-met, and anti-β-actin (Cell Signaling Technology, Danvers, MA, USA); anti-MMP-9
(Bioworld, Minneapolis, MN, USA); and anti-NGF, (Abcam, Cambridge, MA, USA).

Nan L., Qin T., Xiao Y., Qian W., Li J., Wang Z., Ma J., Ma Q, & Wu Z. (2019). Pancreatic Stellate Cells Facilitate Perineural Invasion of Pancreatic Cancer via HGF/c-Met Pathway. Cell Transplantation, 28(9-10), 1289-1298.

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Culturing Human Pancreatic Cancer Cells

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The human PC cell lines (BxPC3 and Panc-1) were obtained from the Chinese Academy of Sciences Cell Bank of Type Culture Collection, and they were cultured in the corresponding medium (Invitrogen) which contains 10% fetal bovine serum (FBS), 100 μg/ml penicillin-streptomycin. The cells were incubated at 37°C in a humidified atmosphere containing 5% CO₂. Antibodies were purchased from the following sources: recombinant mature human Nodal (rhNodal) (R&D Systems) and its inhibitor SB431542 (Sigma-Aldrich); anti-MMP-9 (Bioworld); and anti-NGF, anti-BDNF, and anti-GDNF (Abcam).

Shen S., Wang Q., Wang X., Ding J., Chen F., Xiao Y., Qin T., Qian W., Li J., Ma Q, & Ma J. (2022). Nodal Enhances Perineural Invasion in Pancreatic Cancer by Promoting Tumor-Nerve Convergence. Journal of Healthcare Engineering, 2022, 9658890.

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Comprehensive Protein Analysis Protocol

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Protein preparation and western blot were performed as described previously [19 (link)]. The antibodies for immune blot analysis were as follows: mouse anti-Flag M2 (Sigma-Aldrich), rabbit anti-DACH1 (Proteintech), rabbit cyclinB1 (Bioworld Technology) and rabbit cdc2 (Bioworld Technology), rabbit anti-phospho-SMAD3 (Cell Signaling Technology, Inc, Shanghai, China), rabbit anti-phospho-SMAD2 (Millipore, Billerica, MA, USA), rabbit polyclonal anti-SMAD3, anti-SMAD2, anti-E-cadherin, anti-vimentin, anti-MMP-2, anti-MMP-9 (Bioworld Technology). The bands were visualized by enhanced chemiluminescence (Pierce Bioscience, Shanghai, China).

Yan W., Wu K., Herman J.G., Brock M.V., Zhou Y., Lu Y., Zhang Z., Yang Y, & Guo M. (2014). Epigenetic silencing of DACH1 induces the invasion and metastasis of gastric cancer by activating TGF-β signalling. Journal of Cellular and Molecular Medicine, 18(12), 2499-2511.

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Protein Expression Analysis of Hep-G2 Cells

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Cellular proteins were extracted from Hep-G2 cells (Con, NC, and sh-LOXL1-AS1) in lysis buffer (Beyotime). The cell proteins were separated by SDS-PAGE and transferred to poyvinylidene difluoride membranes (Millipore). The membranes were blocked and then probed with primary antibodies at 4°C overnight. The following primary antibodies were used in this study: anti- CyclinB1, anti-Cdc25A, anti-Cdc2, anti-MMP-2, anti-MMP-9, and anti-β-actin (all from Bioworld Technology). β-Actin (Beyotime) was employed as an internal control. After washing, the membranes were incubated with horseradish peroxidase-conjugated goat anti-rabbit or anti-mouse IgG (Beyotime) and were visualized with an enhanced chemiluminescence detection reagent from Pierce.

Liu J., Zhai C., Liu D, & Liu J. (2020). The Long Noncoding RNA LOXL1-AS1 Promotes the Proliferation, Migration, and Invasion in Hepatocellular Carcinoma. Analytical Cellular Pathology (Amsterdam), 2020, 4182092.

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Immunohistochemical Staining Protocol for Cell Proliferation Markers

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The procedure of IHC staining was performed as described previously. Anti–KIF3A (abcam, ab11259, dilution at 1:300), anti–phospho‐Rb, anti–E2F1, anti–Cyclin E1, anti–Cyclin D1, anti–P21, anti–ZEB1, anti–E‐cadherin, anti–vimentin, anti–MMP‐9 and anti–MMP‐2 (Bioworld Technology, all at dilution 1:200) were incubated overnight at 4°C. Each slide was photographed with a digital camera on an inverted Olympus IX81 microscope. The staining evaluation was made according to the semi–quantitative scoring system, as described previously. Briefly, the scores of positive tumor cell proportion (0, none; 1, <1/100; 2, 1/100 to 1/10; 3, 1/10 to 1/3; 4, 1/3 to 2/3; and 5,> 2/3) and staining intensity (0, none; 1, weak; 2, intermediate; and 3, strong) were added up to obtain a final total score, ranging from 0 to 8.

Wang W., Zhang R., Wang X., Wang N., Zhao J., Wei Z., Xiang F, & Wang C. (2020). Suppression of KIF3A inhibits triple negative breast cancer growth and metastasis by repressing Rb‐E2F signaling and epithelial‐mesenchymal transition. Cancer Science, 111(4), 1422-1434.

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Protein Extraction and Western Blotting

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Total protein was extracted in radioimmunoprecipitation assay (RIPA) buffer (Beyotime Institute of Biotechnology, Shanghai, China). Protein concentrations were quantified by bicinchoninic acid (BCA) assay (Beyotime Institute of Biotechnology). Western blotting was performed as previously described. 22 The following primary antibodies were used: anti-MMP-2 (1:500; Bioworld Technology, Atlanta, GA, USA), anti-MMP-9 (1:500; Bioworld Technology), anti-E-cadherin (1:300; Boster, Wuhan, China), anti-Vimentin (1:200; Boster), anti-phosphorylated AKT (1:500; Cell Signaling Technology, Beverly, MA, USA), anti-AKT (1:1000; Cell Signaling Technology) and anti β-actin (1:300; Zhongshan Golden Bridge, Beijing, China). Protein bands were quantified by densitometry using Quantity One 4.6.2 (Bio-Rad Laboratories, Hercules, CA, USA) and normalized to β-actin or total AKT.

Zhao Q., Xu L., Sun X., Zhang K., Shen H., Tian Y., Sun F, & Li Y. (2017). MFG-E8 overexpression promotes colorectal cancer progression via AKT/MMPs signalling. Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine, 39(6).

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Protein Expression Analysis in Melanoma

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Melanoma tissues or A375 cells were lysed in radioimmunoprecipitation assay lysis buffer (Beyotime Institute of Biotechnology, Haimen, China), and the protein concentrations of the cell lysates were determined using the Bicinchoninic Acid protein assay kit (Beyotime Institute of Biotechnology). Lysates (30 µg) were separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis and then transferred to polyvinylidene fluoride membranes. The membranes were blocked with 5% milk and then probed at 4°C overnight with the following primary antibodies: anti-SPAG9, anti-E-cadherin, and anti-vimentin (1:2500, Bioworld Technology, St. Louis Park, MN, USA); anti-MMP2, anti-MMP9, and anti-GAPDH (1:3500, Bioworld Technology); and anti-p38, anti-p-p38, anti-ERK, anti-p-ERK, anti-JNK, and anti-p-JNK (1:4500, Bioworld Technology). The membranes were then incubated with horseradish peroxidaselabeled goat anti-rabbit IgG (1:5000, Bioworld Technology) for 2 h, and immunoreactivity was assessed using enhanced chemiluminescence detection reagent (Beyotime Institute of Biotechnology) and ImageJ software.

Liu Y., Zhu X., You X., & Kang R. (2022). SPAG9 promotes the migration and invasion of melanoma cells by regulating the MAPK pathway. Tropical Journal of Pharmaceutical Research, 20(6), 1125-1130.

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