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Anti elavl1 antibody

Manufactured by Cell Signaling Technology
Sourced in China, United States

The Anti-ELAVL1 antibody is a laboratory tool used to detect and study the ELAVL1 (also known as HuR) protein. ELAVL1 is an RNA-binding protein involved in the regulation of gene expression. This antibody can be used in various techniques, such as western blotting, immunoprecipitation, and immunohistochemistry, to help researchers investigate the role of ELAVL1 in biological processes.

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3 protocols using anti elavl1 antibody

1

Immunoprecipitation of ELAVL1 complexes

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The transfected cells were treated with 20 μM MG132 (Sigma Aldrich) for 6 h, which was followed by cell lysis for immunoprecipitation. The cell lysates were incubated overnight with Protein-A/G MagBeads (Yeasen, Shanghai, China) and anti-ELAVL1 antibody (Cell Signaling Technology) or normal rabbit IgG (Cell Signaling Technology) at 4 °C. The protein complexes were retrieved, washed, and subjected to western blotting with an anti-ubiquitin antibody (Cell Signaling Technology) [23 (link)].
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2

ELAVL1 Expression in Hepatocellular Carcinoma

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A total of 77 pairs of tumor and adjacent non-tumor tissues were subjected to clinicopathological analyses. Written informed consent was obtained from all patients. Paraffin-embedded tumor tissues and the surrounding non-tumor tissues were examined via H&E staining and immunohistochemistry with anti-ELAVL1 antibody (Cell Signaling Technology). Based on the ELAVL1 expression in the nuclei of cells, tumor and non-tumor tissues were classified as follows: negative, partial expression (<50% of nuclei), and diffuse expression (≥50% of nuclei). HCCs with negative or partial ELAVL1 expression were classified as the ELAVL1low group, whereas HCCs with diffuse ELAVL1 expression were classified as the ELAVL1high group. All patients received postoperative radiological follow-up every 2–6 months. Radiological assessments were evaluated based on the response evaluation criteria in solid tumors [39 (link)]. This study was approved by the research ethics committees of the Graduate School of Medicine, Chiba University (approval number: 3300) and performed according to the Declaration of Helsinki.
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3

ELAVL1 and PI3Kδ Protein Analysis

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This work utilized RIPA buffer (Beyotime, Shanghai, China) for extracting total cellular proteins. BCA method (Keygen Biotech, Nanjing, China) was applied in determining protein content. After separating protein aliquots through SDS-PAGE, this study transferred on PVDF membranes (Millipore, MA, USA). Later, 5% defatted milk was later utilized to block membranes for a 1-h period. Blots were cultivated with anti ELAVL1 antibody (#12582, 1:1000, Cell Signaling Technology, Danvers, MA, USA) as well as PI3Kδ antibody (ab1678, 1:1000, Abcam, Cambridge, MA, USA) overnight under the temperature of 4˚C. Subsequently, this study adopted secondary antibody (Cell Signaling Technology) for additional 1-h incubation under ambient temperature. Signals were detected by enhanced chemiluminescence (Millipore). β-actin was used as internal reference.
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