Anti cd147

Manufactured by Santa Cruz Biotechnology

Sourced in United States

Anti-CD147 is a monoclonal antibody that specifically binds to the CD147 protein. CD147 is a cell surface glycoprotein involved in various cellular processes. The anti-CD147 antibody can be used as a tool for the detection and study of CD147 expression in research applications.

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CD147 (5 citations) Antibody anti-CD147 (3 citations) Mouse anti-CD147 (3 citations)

7 protocols using anti cd147

Immunoblot Analysis of Protein Extracts

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Proteins were extracted, sonicated, centrifuged at 13,000 rpm for 45 min at 4oC, and supernatants used for immunoblot analysis, as previously described (5 (link),6 ). Actin was always used as an internal loading control. Primary antibodies used were as follows: anti GSAP full length (1:200) and GSAP-16kDa (1:150) (Thermo Scientific, Waltham, MA); anti-TMP21 (1:200), anti-CD-147 (1:200), anti-caspase-3, anti-caspase-7 (1:200) (Santa Cruz Biotech., Dallas, TX), anti-APP (1:200), anti CTF-α and CTF-β (1:200) (Millipore, Billerica, MA, USA); anti-β-actin (1:200). IRDye infrared secondary antibodies were from LI-COR Bioscience.

Chu J., Li J.G., Joshi Y.B., Giannopoulos P.F., Hoffman N.E., Madesh M, & Praticò D. (2014). Gamma secretase activating protein is a substrate for caspase-3: implications for Alzheimer’s disease. Biological psychiatry, 77(8), 720-728.

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Western Blot Analysis of CD147

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Cell samples were lysed with RIPA buffer (Beyotime, China). Equal amounts (10 μg) of total protein were loaded, and then subsequently immunoblotted with the primary antibodies, including anti-CD147 and tubulin monoclonal antibodies (Santa Cruz, CA, USA). Proteins were detected using the Amersham enhanced chemiluminescence system (Pierce, Rockford, IL, USA) according to the manufacturer’s instructions.

Luo L.J., Zhang L.P., Duan C.Y., Wang B., He N.N., Abulimiti P, & Lin Y. (2017). The inhibition role of miR-22 in hepatocellular carcinoma cell migration and invasion via targeting CD147. Cancer Cell International, 17, 17.

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Immunoblot Analysis of Protein Extracts

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Proteins were extracted, sonicated, centrifuged at 13,000 rpm for 45 min at 4 ^oC, and supernatants used for immunoblot analysis, as previously described17 (link)18 . Actin was always used as an internal loading control. Primary antibodies used were as follows: anti GSAP full length (1:200) and GSAP-16 kDa (1:150) (Thermo Scientific); anti-5LO (1:500) (BD Bioscience); anti-12-15LO (1:200) (Santa Cruz Biotech., Dallas, TX); anti-TMP21 (1:200), anti-CD147(1:200), anti-caspase-3 (1:200) (Santa Cruz Biotech., Dallas, TX); anti-β-actin (1:200) (Santa Cruz Biotech., Dallas, TX). IRDye infrared secondary antibodies were from LI-COR Bioscience (Lincoln, NE).

Chu J., Li J.G., Hoffman N.E., Stough A.M., Madesh M, & Praticò D. (2015). Regulation of gamma-secretase activating protein by the 5Lipoxygenase: in vitro and in vivo evidence. Scientific Reports, 5, 11086.

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Quantifying CD147 Expression in Human Sperm

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Isolated human sperm were resuspended in lysis buffer (RIPA buffer: 50 mM Tris-HCl [pH 8.0], 150 mM NaCl, 1% NP-40, 0.5% sodium deoxycholate, 0.1% SDS) and lysed with ultrasonication. Sperm lysates (30 μg) were subjected to sodium dodecyl sulfate-polyacrylamide gel electrophoresis (4%–15%, v/w), and resolved proteins were transferred to nitrocellulose membranes. After the membranes were blocked with 5% nonfat milk for 1 h, they were immunoblotted with anti-CD147 (1:500, Santa Cruz sc-9725) or anti-GAPDH (1:2,000, Santa Cruz sc-47724) overnight at 4°C. The membranes were washed three times with TBST and incubated with anti-mouse IgG-peroxidase (Bio-Rad) for 1 h at room temperature. Signals were detected with enhanced chemiluminescence (Amersham, Piscataway, NJ, USA). The intensities of the bands were quantified by densitometry with an Alpha Imager HP.

Chen H., Shi X., Li X., Diao R., Ma Q., Jin J., Qiu Z., Li C., Yu M.K., Wang C., Li X., Li F., Chan D.Y., Zhao A.Z., Cai Z., Sun F, & Fok K.L. (2021). CD147 deficiency is associated with impairedsperm motility/acrosome reaction and offersa therapeutic target for asthenozoospermia. Molecular Therapy. Nucleic Acids, 26, 1374-1386.

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Acetate-induced Protein Expression

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Cells were seeded in 6-well plates and exposed to acetate for 48 hours: 45 mM, 70 mM for HCT-15 and 75 mM, 110 mM for RKO cells (IC₃₀ and IC₅₀ acetate doses for both cell lines) previously determined by us [5 (link)]. As negative control, cells were incubated with fresh medium. Cell lysis, total protein and Western blotting were carried out as previously described [5 (link)].
The primary antibodies used were: anti-MCT1 (1:500), anti-MCT2 (1:200), anti-MCT4 (1:500), anti-SMCT1 (1:250), anti-CD147 (1:500), and anti-actin (1:5000), from Santa Cruz Biotechnology; anti-GLUT 1 (1:200) (Abcam). Chemiluminescence was detected using the ECL detection system (Amersham) and the imager Chemi-Doc XRS system (Bio-Rad).

Ferro S., Azevedo-Silva J., Casal M., Côrte-Real M., Baltazar F, & Preto A. (2016). Characterization of acetate transport in colorectal cancer cells and potential therapeutic implications. Oncotarget, 7(43), 70639-70653.

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Protein Extraction and Western Blot Analysis

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Total proteins were extracted from the gastric cancer tissues and cells using the standard methods 9 (link). Proteins were quantified using a BCA Protein Assay Kit (Pierce, Rockford, IL, USA). Then samples were separated by 10% SDS-PAGE and transferred to PVDF membranes. The primary antibodies were anti-β3GnT8 (1:1000), anti-CD147 (1:500; Santa Cruz, CA, USA), anti-annexin A2 (ANXA2) (1:1000; Santa Cruz), and anti-GAPDH (1:1000; Santa Cruz). The specificity of β3GnT8 antibody has been verified in our previous study 7 (link). Bands on the membranes were visualized using an ECL detection kit obtained from Beyotime Institute of Biotechnology (Jiangsu, China).

Shen L., Dong X., Yu M., Luo Z, & Wu S. (2017). β3GnT8 Promotes Gastric Cancer Invasion by Regulating the Glycosylation of CD147. Journal of Cancer, 8(2), 314-322.

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CD147 Protein Expression Analysis

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The cells were harvested and lysed with ice-cold lysis buffer (Beyotime Biotechnology Inc., Haimen, China) for 30 min on ice. The lysate protein (50 mg) was separated by 10% sodium dodecyl sulfate polyacrylamide gel electrophoresis, and transblotted onto polyvinylidene difluoride membranes (Millipore, Billerica, MA, USA). The membrane was blocked with 5% non-fat dry milk and subsequently probed with an anti-CD147 1:500; Santa Cruz Biotechnology, Santa Cruz, CA, USA) or anti-b-actin (Santa Cruz Biotechnology) antibody at 4°C overnight. The cells were then incubated with horseradish peroxidase-conjugated secondary antibodies (1:2000; Santa Cruz Biotechnology) for 1 h at room temperature. The protein bands were detected using the ECL detection system (Beyotime Biotechnology Inc.). All experiments were performed in triplicate.

Li H.Y., Liu Y.C., Bai Y.H., Sun M., Wang L., Zhang X.B, & Cai B. (2016). SNP at miR-483-5p-binding site in the 3'-untranslated region of the BSG gene is associated with susceptibility to esophageal cancer in a Chinese population. Genetics and molecular research : GMR, 15(2).

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