WSE-7057 EzRun BlueNative

Purpose and Application

• Blue-Native PAGE running buffer for SDS-free Tris-Glycine polyacrylamide gels

Features

• Suitable for SDS-free Tris-Glycine polyacrylamide gel

• Simply add CBB solution (BlueNative Buffer Additive) to buffer diluted with distilled water before electrophoresi

• Enables electrophoresis of protein complexes intact

• Stable at room temperature for 1 year

Data

Comparison with Conventional Bis-Tris Gel Methods

While Blue-Native PAGE is typically performed using Bis-Tris or Imidazole gels, these reagents are costly, making experiments expensive.
EzRun BlueNative is an electrophoresis buffer that enables Blue-Native PAGE with Tris-Glycine polyacrylamide gels, which are commonly used for SDS-PAGE.
It allows you to obtain electrophoresis patterns comparable to those achieved with conventional Bis-Tris gels, while significantly reducing experimental costs.

Protocol

The figure above shows the separation of chloroplast extracts by Blue-Native PAGE (A) using a 3–14% u-PAGEL H gel (first dimension), followed by second-dimension separation with HR-Clear-Native PAGE (B) and SDS-PAGE (C).BN-PAGE preserves protein complexes without dissociation. When analyzed by HR-CN-PAGE, however, a single BN-PAGE band was resolved into two or more bands (B), showing that the complex dissociates even under mild detergent conditions. In SDS-PAGE, strong detergents and reducing agents completely dissociated the complexes, revealing that one BN-PAGE band actually contained many proteins (C).In contrast, SDS-PAGE involves strong detergents and reducing agents under heat treatment, leading to complete dissociation of protein complexes. Indeed, in the SDS-PAGE second dimension (C), a single band observed in the first-dimension BN-PAGE was revealed to be composed of many different proteins.Moreover, additional third- or fourth-dimensional electrophoresis can be applied for deeper analysis of specific proteins. u-PAGEL H is an optimized ready-to-use polyacrylamide gel, ideally suited for analyzing high-molecular-weight protein complexes.

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