Affinity Purification and Mass Spectrometry (AP-MS)
  • OVERVIEW

Affinity Purification and Mass Spectrometry (AP-MS)


Protein–protein interactions (PPIs) are physical contacts of high specificity establised between two or more protein molecules as a result of biochemical events steered by interactions that include electrostatic forces, hydrogen bonding and the hydrophobic effect. Many are physical contacts with molecular associations between chains that occur in a cell or in a living organism in a specific biomolecular context.

Proteins rarely act alone as their functions tend to be regulated. Many molecular processes within a cell are carried out by molecular machines that are built from numerous protein components organized by their PPIs. These physiological interactions make up the so-called interactomics of the organism, while aberrant PPIs are the basis of multiple aggregation-related diseases, such as Creutzfeldt–Jakob and Alzheimer's diseases.

The protein mixture in the sample obtained by IP, Co-IP, Pull-down and other technologies can be identified by LC-MS/MS technology, and the target protein and its interacting proteins can be identified at the same time, thereby constructing a protein interaction spectrum. This technique is suitable for both mass spectrometry analysis of in-gel enzymatic hydrolysis after SDS-PAGE separation of protein mixture, and mass spectrometry analysis of liquid enzymatic hydrolysis in protein mixture solution.


Highlights

Suitable for identification of protein mixture samples such as IP, Co-IP and Pull-down.

Can identify unknown interacting proteins.

High accuracy, high specificity, and short project cycle.


Applications

Protein interaction profiling identification.


Service Process

Receiving orders and samples

Affinity purification

LC-MS/MS data analysis

Interacting protein confirmation

Results delivered to customers


Sample Requirements

Samples to be analyzed

Sample Information Sheet: The source, content, status and other basic information of the sample should be filled in in detail.


Deliverables

An experimental report, including specific experimental procedures and proteome identification and quantitative results (bioinformatics analysis).


Bioinformatics Analysis Includes

Full-spectrum identification of proteins.

Differential analysis of protein expression.

Identify interacting proteins.

Predict the network interactions of proteins based on the STRING database and compare with experimental data.

Protein GO functional classification, COG functional annotation, and Pathway annotation.

Affinity Purification and Mass Spectrometry (AP-MS)


Protein–protein interactions (PPIs) are physical contacts of high specificity establised between two or more protein molecules as a result of biochemical events steered by interactions that include electrostatic forces, hydrogen bonding and the hydrophobic effect. Many are physical contacts with molecular associations between chains that occur in a cell or in a living organism in a specific biomolecular context.

Proteins rarely act alone as their functions tend to be regulated. Many molecular processes within a cell are carried out by molecular machines that are built from numerous protein components organized by their PPIs. These physiological interactions make up the so-called interactomics of the organism, while aberrant PPIs are the basis of multiple aggregation-related diseases, such as Creutzfeldt–Jakob and Alzheimer's diseases.

The protein mixture in the sample obtained by IP, Co-IP, Pull-down and other technologies can be identified by LC-MS/MS technology, and the target protein and its interacting proteins can be identified at the same time, thereby constructing a protein interaction spectrum. This technique is suitable for both mass spectrometry analysis of in-gel enzymatic hydrolysis after SDS-PAGE separation of protein mixture, and mass spectrometry analysis of liquid enzymatic hydrolysis in protein mixture solution.


Highlights

Suitable for identification of protein mixture samples such as IP, Co-IP and Pull-down.

Can identify unknown interacting proteins.

High accuracy, high specificity, and short project cycle.


Applications

Protein interaction profiling identification.


Service Process

Receiving orders and samples

Affinity purification

LC-MS/MS data analysis

Interacting protein confirmation

Results delivered to customers


Sample Requirements

Samples to be analyzed

Sample Information Sheet: The source, content, status and other basic information of the sample should be filled in in detail.


Deliverables

An experimental report, including specific experimental procedures and proteome identification and quantitative results (bioinformatics analysis).


Bioinformatics Analysis Includes

Full-spectrum identification of proteins.

Differential analysis of protein expression.

Identify interacting proteins.

Predict the network interactions of proteins based on the STRING database and compare with experimental data.

Protein GO functional classification, COG functional annotation, and Pathway annotation.

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