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Can all proteins pulled down be identified by mass spectrometry?

Not all proteins pulled down in a pull-down assay can be identified by mass spectrometry. The success of identification depends on several factors:

1. Protein abundance:

High-abundance proteins are easier to identify, whereas low-abundance proteins may be difficult to detect.

2. Sample preparation:

Proteins may be lost during sample processing, especially those that are prone to degradation or adhere to the walls of the tube.

3. Mass spectrometry sensitivity:

The sensitivity of the mass spectrometer determines the minimum abundance of proteins that can be detected.

If a low-abundance protein is captured in a pull-down experiment and some of it is lost during sample processing, it may still be difficult to detect with even high-sensitivity mass spectrometry equipment, especially in complex samples like cell lysates.

BiotechPack, A Biopharmaceutical Characterization and Multi-Omics Mass Spectrometry (MS) Services Provider

Related Services:

GST pull-down protein interaction analysis

Protein interaction analysis

Mass spectrometry analysis of protein interactions

Pull-down target protein mass spectrometry identification

SILAC and co-immunoprecipitation coupled mass spectrometry for protein interaction analysis

Cross-linking method for protein interaction analysis

Far-Western Blot analysis

Label transfer method for protein interaction analysis

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