MyD88 expression level in treated H9C2 cells and myocardial tissue was determined by western blotting. Briefly, cells or left ventricular myocardium were collected and homogenized in ice-cold RIPA buffer containing 0.1% phenylmethylsulfonyl fluoride. The homogenates were centrifuged at 12,000× rpm for 15 min at 4 °C. Supernatants were collected and protein concentration was quantified using a BCA assay kit (Pierce, Rockford, IL, USA). Equal amounts of cell extracts or heart homogenates were separated by 12% SDS-PAGE and electroblotted onto PVDF membranes. After blocking with 5% skimmed milk for 2 h at room temperature, membranes were incubated with rabbit anti-MyD88 antibody (1:800) (Cell Signaling Technology, Danvers, Massachusetts, USA) overnight at 4 °C, followed by HRP-conjugated goat anti-rabbit IgG (1:4000) (Merck Millipore, Basilica, Massachusetts, USA) for 1 h at 37 °C. Immunoreactive protein bands were visualized using a Tanon 5200 Chemiluminescence Imaging System (Tanon, Shanghai, China).
Rabbit anti myd88 antibody
Manufactured by Cell Signaling Technology
Sourced in United States
The Rabbit anti-MyD88 antibody is a primary antibody that specifically recognizes the MyD88 protein. MyD88 is an important adaptor protein involved in signal transduction pathways related to the innate immune response. This antibody can be used to detect and study the expression and localization of MyD88 in various biological samples.
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Lab products found in correlation
4 protocols using rabbit anti myd88 antibody
1
MyD88 Expression in H9C2 and Myocardium
2
Western Blot Analysis of MyD88 Expression
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MyD88 expression level in treated H9C2 cells and myocardial tissue was determined by Western blotting. Brie y, cells or left ventricular myocardium were collected and homogenized in ice-cold RIPA buffer containing 0.1% phenylmethylsulfonyl uoride. The homogenates werecentrifuged at 12,000 rpm for 15 min at 4℃. Supernatants were collected and protein concentration was quanti ed using BCA assay kit (Pierce, Rockford, IL, United States). Equal amounts of cell extracts or heart homogenates were separated by 12% SDS-PAGE and electroblotted onto PVDF membranes. After blocking with 5% non-fat milk for 2 h at room temperature, the membranes were incubated with rabbit anti-MyD88 antibody (1:800) (Cell Signaling Technology, Danvers, Massachusetts, USA) overnight at 4°C, followed by HRP-conjugated goat anti-rabbit IgG (1:4,000) (Merck Millipore, Basilica, Massachusetts, USA) for 1 h at 37°C. Immunoreactive protein bands were visualized using a Tanon 5,200 Chemiluminescence imaging system (Tanon, Shanghai, China).
3
Western Blot Analysis of MyD88 Expression
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
MyD88 expression level in treated H9C2 cells and myocardial tissue was determined by Western blotting. Brie y, cells or left ventricular myocardium were collected and homogenized in ice-cold RIPA buffer containing 0.1% phenylmethylsulfonyl uoride. The homogenates werecentrifuged at 12,000 rpm for 15 min at 4℃. Supernatants were collected and protein concentration was quanti ed using BCA assay kit (Pierce, Rockford, IL, United States). Equal amounts of cell extracts or heart homogenates were separated by 12% SDS-PAGE and electroblotted onto PVDF membranes. After blocking with 5% non-fat milk for 2 h at room temperature, the membranes were incubated with rabbit anti-MyD88 antibody (1:800) (Cell Signaling Technology, Danvers, Massachusetts, USA) overnight at 4°C, followed by HRP-conjugated goat anti-rabbit IgG (1:4,000) (Merck Millipore, Basilica, Massachusetts, USA) for 1 h at 37°C. Immunoreactive protein bands were visualized using a Tanon 5,200 Chemiluminescence imaging system (Tanon, Shanghai, China).
4
Quantifying MyD88 Expression in H9C2 Cells
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MyD88 expression level in treated H9C2 cells and myocardial tissue was determined by Western blotting. Briefly, cells or left ventricular myocardium were collected and homogenized in ice-cold RIPA buffer containing 0.1% phenylmethylsulfonyl fluoride. The homogenates werecentrifuged at 12,000 rpm for 15 min at 4 . Supernatants were collected and protein concentration was quantified using BCA assay kit (Pierce, Rockford, IL, United States). Equal amounts of cell extracts or heart homogenates were separated by 12% SDS-PAGE and electroblotted onto PVDF membranes. After blocking with 5% non-fat milk for 2 h at room temperature, the membranes were incubated with rabbit anti-MyD88 antibody (1:800) (Cell Signaling Technology, Danvers, Massachusetts, USA) overnight at 4°C, followed by HRP-conjugated goat anti-rabbit IgG (1:4,000) (Merck Millipore, Basilica, Massachusetts, USA) for 1 h at 37°C. Immunoreactive protein bands were visualized using a Tanon 5,200 Chemiluminescence imaging system (Tanon, Shanghai, China).
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