Phosphorylation-dependent Protein Subcellular LocalizationINQUIRY
Creative BioMart provides professional protein subcellular localization services to accelerate kinase/phosphatase biology research and pharmaceutical development. Our in-depth knowledge, state-of-the-art techniques, and extensive hands-on experience allow us to deliver high-quality and reliable results within a guaranteed time.
All cells are comprised of well-defined compartments with specific functions. The efficiency of many subcellular processes is increased by the fact that compartmentalization concentrates the required components to a confined space within the cell. Proteins are responsible for virtually every cellular process. Compartmentalization provides a specific environment for proteins to perform specific functions. Confinement to a specific compartment can also increase specificity. The most common subcellular localizations include the cytoplasmic membrane, the cell wall, the cytoplasma, and the extracellular environment. Abnormal localization of proteins can easily lead to disruption of cellular activities. Therefore, understanding the subcellular localization of proteins is necessary to study the functions of genes, protein interactions, and their mechanisms of action.
Phosphorylation is one of the main types of covalent modifications and is also recognized as the most frequent modification. Phosphorylation and dephosphorylation are important processes necessary for the regulation of subcellular localization. Subcellular localization is also involved in determining the signal output of signaling pathways mediated by kinases and phosphatases. Revealing the subcellular localization of kinases, phosphatases and other proteins involved in phosphorylation and dephosphorylation is a crucial step in kinase/phosphatase biology research and the development of therapies or biomarkers for phosphorylation-related disease
Figure 1. Subcellular localization of VIP1 variants. (Takeo K & Ito T, 2017)
- Understanding protein function and dissecting intracellular trafficking.
- Identifying abnormal subcellular localization of disease-associated proteins
- Revealing mechanisms of disease progression.
- Significantly improving target identification in the drug discovery process.
- Developing potential diagnostic targets and vaccine candidates.
Creative BioMart offers different strategies and scalable platforms for protein subcellular localization in different species, including mammalian, plant, insect, bacteria, fungi, yeast and algae, to meet the specific requirements of each project. Our scientific team has the ability to ensure reproducible results. Our services include, but are not limited to the following:
|Featured Services||Featured Platforms|
|Subcellular localization prediction||Online resources, software, and databases|
|In situ hybridization||Electron microscopy|
|Fluorescent imaging||Live-cell fluorescence microscopy|
|Fluorescence resonance energy transfer (FRET) imaging||Confocal laser scanning microscopy|
|Isotope tagging (LOPIT)||Mass spectrometry|
|Immunogold labeling||Immunogold electron microscopy|
|Subcellular colocalization analysis||High-throughput image analysis|
|Add-On Services||Types of Samples|
|Protein tagging||Cell cultures|
|Fusion protein expression||Tissue samples|
|Live-cell protein labeling||Living cells|
|Protein analysis||In vivo samples|
If you can't find what you are looking for in the options above, please fill out the online inquiry form and let us know more details.
Custom Project Workflow
Creative BioMart has a strong team of chemists, biologists, and pharmacologists working on your project to save your time and effort. If you require any further information, please feel free to contact us. We look forward to working together to meet your goals.
- Takeo K & Ito T. Subcellular localization of VIP 1 is regulated by phosphorylation and 14-3-3 proteins. FEBS letters, 2017, 591(13): 1972-1981.
- Simeunovic A, et al. Know where your clients are: subcellular localization and targets of calcium-dependent protein kinases. Journal of experimental botany, 2016, 67(13): 3855-3872.