Protein Purity Analysis in E. coli Using Chromatography Techniqu

The purity analysis of Escherichia coli proteins is a crucial step in biotechnology and molecular biology research, especially in the fields of protein engineering, drug development, and proteomics. This technique mainly uses two chromatographic methods, molecular sieves (gel filtration) and reverse phase chromatography (RP-HPLC), to separate and purify proteins from E. coli, ensuring the acquisition of high-purity protein samples for subsequent structural and functional analysis.

 

Technical Principle

Molecular sieve chromatography, also known as gel permeation chromatography (GPC), is a technique that separates proteins based on molecular size. In this process, the sample goes through a chromatographic column filled with gel particles of different pore sizes. Large molecular proteins, unable to enter the small pores of the gel particles, are eluted from the column first, while small molecular proteins or impurities, due to their entry into the pores, have an extended flow time in the column, thus achieving separation.

 

Reverse phase high-performance liquid chromatography (RP-HPLC) is a technique that separates proteins based on the hydrophilic and hydrophobic interactions between the protein and the column packing. In reverse phase chromatography, the column packing is hydrophilic, while the sample is hydrophobic under the action of an organic solvent. Proteins are retained in the column to different extents according to their hydrophobicity, and eluted by changing the concentration of the organic solvent, thus achieving the separation and purification of proteins.

 

MtoZ Biolabs is equipped with both molecular sieve and reverse phase liquid chromatography techniques for protein/peptide purification analysis, which can be used for the separation and determination of various protein samples, meeting the needs of various protein sample purity analysis.

 

Service Advantages

1. High Purity

Combination of molecular sieve and reverse phase chromatography can effectively remove impurities and homologues from protein samples, obtaining high purity proteins.

 

2. High Selectivity

By adjusting chromatographic conditions, such as column temperature, composition of mobile phase, and flow rate, high selectivity separation and purification can be achieved for specific proteins.

 

3. High Sensitivity

Especially in reverse phase chromatography analysis, by using different types of detectors, such as ultraviolet light detectors, fluorescence detectors, etc., high sensitivity detection of trace proteins can be achieved.

 

4. Wide Range of Applications

This technique is not only suitable for the purity analysis of E. coli proteins, but also suitable for the purity analysis and identification of other microbial, animal, plant, and human proteins.

 

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