Are you currently facing challenges in understanding the role of the Golgi apparatus in disease, uncovering novel drug targets, or gaining detailed insights into protein function and signaling pathways? Our Golgi apparatus proteomic analysis service helps you accelerate scientific discovery and overcome these challenges through advanced organelle isolation and state-of-the-art mass spectrometry platforms.
The Golgi apparatus is a highly dynamic organelle central to the protein secretory pathway. It processes, sorts, and packages proteins and lipids before they are secreted or delivered to other cellular compartments. Proteomic analysis of the Golgi provides a comprehensive view of its protein composition and dynamic nature, revealing insights into its roles in various cellular processes and diseases.
Fig.1 TING activates TBK1 at the Golgi.1
A comprehensive report outlining the methodologies used, data quality metrics, and key findings.
A complete list of all identified and quantified proteins in a user-friendly format, ready for your analysis.
Visual representations and reports showing the functional pathways and GO terms associated with the proteins identified.
The Golgi apparatus is often structurally and functionally altered in cancer cells, influencing protein secretion and cell signaling. Analyzing the proteome of the Golgi can help identify novel proteins involved in tumor growth, metastasis, and drug resistance, providing potential targets for new therapies.
Many neurodegenerative diseases, such as Alzheimer's and Parkinson's, are characterized by the accumulation of misfolded proteins. The Golgi apparatus is a key checkpoint for protein folding and quality control. Proteomic analysis can pinpoint how Golgi dysfunction contributes to the pathogenesis of these diseases.
The Golgi is the primary site of protein glycosylation. Studying its proteome can help researchers understand the mechanisms behind congenital disorders of glycosylation and other diseases related to abnormal glycosylation, leading to improved diagnostics and treatment strategies.
The Golgi responds dynamically to cellular stress. By profiling its proteome under different stress conditions, researchers can uncover the intricate signaling pathways that regulate its function and the cell's survival response.
Understanding the protein composition of the Golgi can reveal new molecular targets for small-molecule inhibitors or biologics. Proteomics provides the data needed to evaluate a drug's effect on Golgi function and its potential off-target effects.
With over 20 years of experience, our team of expert scientists possesses deep knowledge in proteomics and cell biology. We provide an unparalleled consultative partnership, from project design to data interpretation, ensuring you get the most out of your research.
Our two-step protocol for Golgi apparatus isolation, using differential centrifugation and sucrose density gradient centrifugation, guarantees a highly pure sample with minimal contamination. This translates to cleaner data and higher confidence in protein identification.
We use advanced mass spectrometry platforms to provide accurate and in-depth proteomic analysis. Our use of techniques like TMT allows for precise quantification and the analysis of low-abundance proteins.
We don't just deliver data. Our comprehensive bioinformatics analysis includes pathway and GO analysis, providing you with meaningful biological context and actionable insights that can accelerate your discoveries.
A: A whole-cell proteome provides a broad overview but can miss low-abundance proteins or organelle-specific changes. Our Golgi-specific analysis isolates the organelle of interest, reducing sample complexity and allowing for the deep profiling of Golgi-resident proteins and PTMs, which is crucial for understanding its specific function.
A: We can analyze a wide range of PTMs, with a strong focus on phosphorylation and glycosylation, as these are critical for Golgi function. We also offer services for ubiquitinomics and methylation analysis.
A: Yes, our methodology is robust and has been successfully applied to a variety of sample types, including cultured cells, frozen tissues from humans and animals, and even plant tissues. We recommend a consultation to discuss your specific sample type and ensure it is compatible with our workflow.
A: We employ a two-step isolation protocol using differential centrifugation and a density gradient to achieve high purity. This significantly reduces contamination from other organelles, ensuring the proteins we identify are genuinely Golgi-resident. The result is cleaner data with higher confidence in protein identification.
At Creative Biolabs, our commitment to scientific excellence and client-centric solutions ensures that your research is in expert hands. Contact our team to discuss your project!
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