Protein separation

Separation of proteins from sample mixture

HPLC and SDS PAGE are two of the most common protein separation techniques utilized to distinguish proteins and peptides by their physiochemical properties. Protein separation can stand alone and provide you with information about specific proteins. However, you can also combine with other analyses to ...

HPLC and SDS PAGE are two of the most common protein separation techniques utilized to distinguish proteins and peptides by their physiochemical properties. Protein separation can stand alone and provide you with information about specific proteins. However, you can also combine with other analyses to purify the sample beforehand. For instance when a HPLC system is coupled to a mass spectrometer.

Alphalyse offers a comprehensive range of services for both analysis types. For instance, we can set up any customer method within our lab and optimize the HPLC methods for specific purposes.

UV-HPLC analysis

It can also be helpful to combine the HPLC analysis with mass spectrometry, to obtain additional information about chromatographic peaks and stained spots on gels. All our protein separation services rely on our more than 15 years of experience working with these analyses.

SDS PAGE gel bands

SDS gel bands is often a vital part of analyses such as protein ID by mass spectrometry or N-terminal sequencing by Edman degradation. If you prefer staining and cutting gels for protein identification yourself, we recommend you check our protocols. Please send a request for combinations of protein separation and protein analysis by mass spectrometry or Edman sequencing.

You can read more about the protein separation services below.

You may also want to combine with our other analyses: N-terminal Edman sequencing, protein identification, process-related impurity analysis or post-translational modifications.

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How much protein should I load onto a gel for protein ID by mass spec?

The protein load on each gel should be approximately 50-300 microgram for complex samples with many proteins, and 5-50 microgram for pure protein samples.

Should I use 1D SDS PAGE or 2D PAGE for protein separation?

2D PAGE is the classical approach to separate and visualize many proteins from complex proteomics samples. However, for large and hydrophobic proteins it is better to use 1D SDS PAGE.

How can I increase protein concentration before loading onto 1D SDS PAGE?

You can use TCA precipitation, ice cold ethanol/acetone precipitation or a classical acetone precipitation.

How do I cut the protein band/spot from an SDS PAGE gel?

Cut the gel on a clean glass plate, while wearing gloves at all times. Use a new clean scalpel blade for cutting out the desired protein band/spot. Place the gel piece in a clean Eppendorf tube. It is now ready for protein identification analysis.

Who is this for?

We primarily help customers within the pharmaceutical industry, and biotechs working on drug development, e.g.

Project managers

Working with process development and characterization projects.

Analytical experts

Protein scientists that work with elisa, masss spectrometry, or CMC.

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