Tris-Glycine Precast Gel(8-16%,15 wells,1.5mm,Glass)
8-16%, 15 holes, 1.5mm, glass plate
- Product Code: 111522
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Density: | Storage Condition: | 2-8℃ |
Product Description:
Tris-Glycine precast gels are widely used in protein electrophoresis for separating proteins based on their molecular weight. The 8-16% gradient concentration allows for the resolution of a broad range of protein sizes, making it suitable for analyzing complex protein mixtures. These gels are commonly applied in research labs for tasks such as protein characterization, purity assessment, and immunoblotting (Western blotting). The 15-well format provides high throughput, enabling simultaneous analysis of multiple samples, while the 1.5mm thickness ensures sufficient sample loading capacity and clear resolution. The glass plate construction enhances durability and handling during the electrophoresis process. These gels are particularly useful in molecular biology, biochemistry, and proteomics studies, where precise protein separation is critical.
Sizes / Availability / Pricing:
Size (g) | Availability | Price | Quantity |
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10.000 | 10-20 days | ฿4,104.00 |
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Tris-Glycine Precast Gel(8-16%,15 wells,1.5mm,Glass)
Tris-Glycine precast gels are widely used in protein electrophoresis for separating proteins based on their molecular weight. The 8-16% gradient concentration allows for the resolution of a broad range of protein sizes, making it suitable for analyzing complex protein mixtures. These gels are commonly applied in research labs for tasks such as protein characterization, purity assessment, and immunoblotting (Western blotting). The 15-well format provides high throughput, enabling simultaneous analysis of multiple samples, while the 1.5mm thickness ensures sufficient sample loading capacity and clear resolution. The glass plate construction enhances durability and handling during the electrophoresis process. These gels are particularly useful in molecular biology, biochemistry, and proteomics studies, where precise protein separation is critical.
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