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Hydroxylation is one of the important reversible post-translational modifications of proteins, and protein hydroxylation is an important detoxification reaction in cells, mainly facilitated by groups of enzymes called hydroxylases. Creative BioMart's extensive experience in post-translational modification of proteins based on computational and experimental methods enables us to provide protein hydroxylation service to accelerate your project.
Protein hydroxylation refers to the post-translational modification catalyzed by 2-oxoglutarate-dependent dioxygenases and is a key regulator of protein-protein interactions. Hydroxylation modifications can occur on various amino acids including, but not limited to, proline, lysine, asparagine, aspartic acid, and histidine. Hydroxyl groups can form hydrogen bonds with water molecules as well as other organic functional groups such as amines, amides, and carboxyl groups. Therefore, hydroxylated molecules become more soluble in water, which may affect the structure and function of organic molecules as well as biomolecules. Proline hydroxylation-mediated collagen modification has been extensively studied as a key cellular mechanism regulating oxygen-responsive pathways in tumor initiation and progression. However, its substrate diversity and function remain largely unknown. A better understanding of protein hydroxylation will help identify new therapeutic targets and their regulatory mechanisms, thereby facilitating the development of more effective therapeutic strategies for various human cancers.
Fig 1. Regulation of hypoxia-inducible factor alpha (HIF-alpha) via hydroxylation. (Zurlo G, et al., 2016)
The experimental identification of hydroxylated proteins with proline or lysine sites is often very difficult, time-consuming and expensive using mass spectrometry. In contrast, computer forecasting methods save time and cost. Creative BioMart has successfully performed reliable studies of protein hydroxylation using a variety of techniques to fully understand the hydroxylation status of proteins. In addition, our scientists are committed to developing more general computational methods to annotate the hydroxylation sites of newly discovered abundant proteins in the post-genomic era. Here, we can help you achieve the hydroxylation of various amino acids as novel hydroxylation targets to facilitate drug development, including NDRG3 prolyl, FOXO3a prolyl, Akt prolyl, EPOR prolyl, Filamin A prolyl , eEF2K prolyl, p53 prolyl, etc.
Combining pharmacological substrate capture strategies, advanced mass spectrometry techniques and computational bioinformatics enables the localization of numerous hydroxylation sites in proteins. The hypoxia response mechanism mediated by proline hydroxylation regulates multiple cellular pathways and signaling processes in cells and may play a broader role in regulating cellular physiology and protein function. We provide the following services for proline hydroxylation, including but not limited to:
Our mission is to provide global customers with the most comprehensive and professional customized protein hydroxylation service. If you have any special requirements about our services, please feel free to contact us. We are looking forward to working together with your attractive projects.
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