Phosphoprotein Biotinylation Detection

Protein phosphorylation is the process of transferring the phosphate group of ATP to the amino acid residue of the substrate protein under the action of protein kinase, which is the most basic and important mechanism for regulating and pore protein activity and function. Protein phosphorylation is a ubiquitous post-translational modification that participates in important physiological roles, and detection of phosphoproteins is an important research tool for proteomics research. For example, phosphotyrosine-specific antibodies are often used to detect and enrich phosphoproteins. Currently, a variety of strategies for phosphopeptide labeling have been developed, including immobilized metal affinity chromatography, covalent phosphate modification, and bioorthogonal affinity purification. Phosphate stains can be used for efficient detection of phosphoproteins, and enzymatic methods can be used for labeling and detection of phosphoproteins. Kinase-mediated biotinylation enables efficient detection of phosphoproteins in cell lysates or phosphopeptides following tryptic proteolysis, demonstrating its utility in proteomics studies. Alfa Chemistry provides efficient biotinylation detection services for phosphorylated proteins, and can customize efficient biotinylation strategies to meet customer needs.

The Services

Alfa Chemistry's biotechnology is composed of experienced experts and has the ability to provide customers with efficient phosphorylated protein biotinylation detection services. Related services we can provide include but are not limited to:

• Professional data analysis
• Efficient phosphoprotein biotinylation assay
• Specialized phosphoprotein biotinylation strategies
• Protein phosphorylation site detection
• Purification and activity analysis of protein phosphokinase

Current research

In order to facilitate the detection of phosphoproteins, researchers have developed assays for efficient detection of phosphoproteins. The kinase is coupled to an ATP-biotin conjugate for efficient biotinylation. Kinase-mediated biotinylation can effectively detect the level of hydrolyzed phosphoproteins, and has wide applicability in proteomics.

Features and advantages of protein phosphorylation detection platform

• Optional sample-adapted testing procedures
• Project-responsive detection of phosphoprotein biotinylation
• Broad range of biotinylation detection strategies
• Versatile detection means
• Professional protein phosphorylation detection platform

Protein phosphorylation

Protein phosphorylation is the process of transferring the phosphate group of ATP to amino acid residues (serine, threonine, tyrosine) of the substrate protein catalyzed by protein kinases. Protein phosphorylation is a common regulatory method in organisms, an important mechanism to regulate and control protein activity and function, and plays an important role in the process of cell signal transduction. Protein phosphokinase is an enzyme that catalyzes the transfer of a phosphate group from a phosphate donor to an acceptor protein, usually the γ-phosphate of ATP as the donor.

Purification of protein phosphokinase

Purification of protein kinases can be divided into micro purification and mass purification. The former is usually applied to cells cultured under special conditions, while the latter is generally applied to special tissues and organs. The factors that need to be paid attention to in the purification of protein phosphokinase include the selection of purification method, inhibitors and inactivators, sample volume and cryopreservation.

Alfa Chemistry provides efficient phosphoprotein biotinylation detection services, provides a wide range of biotinylation strategies, and insists on meeting customer needs. If you are interested in our services, please contact us immediately.

References:

1. Keith. D. G.; et al. Phosphoprotein Biotinylation Detection. J. Am. Chem. Soc. 2007, 129(1): 10-11.

※ It should be noted that our service is only used for research, not for clinical use.