In situ Spatial Proteomcis Service

Q: How many markers can I detect at once?

In situ spatial untargeted proteomics Service is an antibody-free, unbiased approach, meaning it does not rely on predefined targets. The number of proteins detected depends on several factors, including the sample type, spatial resolution, and analyzed tissue area.

Mapping Proteins Across Tissue Architecture

In situ Spatial Proteomcis Service is an innovative, antibody-free technique that enables researchers to map protein expression patterns within tissue samples while preserving their spatial context. By combining mass spectrometry with advanced imaging, this method provides unbiased, comprehensive insights into protein localization, interactions, and modifications across tissue architecture. As an antibody-independent approach, it avoids the limitations of targeted assays and opens new avenues for biomarker discovery, tissue characterization, and therapeutic development.

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Our service
Workflow
Applications
Why choose
FAQs
Sample preparation
Case Study
Reference

Our Service

We offer a technology-agnostic ecosystem, allowing us to select the precise instrument that matches your resolution, sensitivity, and throughput requirements

Mass Spectrometry Imaging (Label-Free Discovery)

For unbiased detection of lipids, metabolites, and drugs.

Technologies: MALDI-MSI and DESI-MSI.
Key Features: Enables label-free direct detection of peptides, proteins, and small molecules. While currently lower in throughput than antibody methods, this is the premier choice for discovering unknown targets and mapping drug distribution without prior knowledge of the target.

Workflow

workflow of spatial proteomics analysis

Applications

Cancer Research: Identify tumor-specific biomarkers and map protein expression in different regions of tumors.
Neuroscience: Study the spatial distribution of proteins in the brain, contributing to insights into neurodegenerative diseases and brain function.
Drug Discovery: Investigate the interactions of therapeutic targets within tissue architecture.
Tissue Engineering: Understand protein localization in engineered tissues for better design and optimization of tissue-based therapies.
Immunology: Examine the spatial distribution of immune cells and proteins in response to infection or disease.

Why choose

Precision & Accuracy: Using cutting-edge MS technologies, we offer unparalleled sensitivity in protein detection and quantification.
High Resolution: Our platform allows analysis at cellular and sub-cellular resolution, providing deep insights into protein localization.
Expert Support: Our team of experts provides comprehensive support throughout the process, from experimental design to data interpretation.

FAQs

How many markers can I detect at once?

In situ spatial untargeted proteomcis Service is an antibody-free, unbiased approach, meaning it does not rely on predefined targets. The number of proteins detected depends on several factors, including the sample type, spatial resolution, and analyzed tissue area.

How does this compare to spatial transcriptomics?

Spatial transcriptomics measures RNA (the blueprint), while spatial proteomics measures protein (the functional machinery). Proteomics often correlates better with actual phenotype and drug targets.

Learn about other Q&A.

Sample Requirements

For optimal results, we require your tissue samples to be prepared as follows:

Sample Types: We accept FFPE (Formalin-Fixed Paraffin-Embedded) blocks/slides and Fresh Frozen tissue.
Tissue Thickness: Standard cuts of 5-10 µm are recommended.
Slide Type: Positively charged slides (e.g., Superfrost Plus) are required to prevent tissue detachment.
Fixation: For FFPE, fixation time should be standardized (typically 24–48 hours) to preserve antigenicity.

Important: Important: Please consult our technical team for detailed sample preparation instructions prior to submitting your samples.

Spatial Untargeted Proteomics Case Study

graphical abstract of spatial proteomics case study

Title: Spatial proteomics revealed a CX3CL1-dependent crosstalk between the urothelium and relocated macrophages through IL-6 during an acute bacterial infection in the urinary bladder

Journal: Mucosal Immunology

Published: 2020

Urinary tract infections (UTIs) represent one of the most prevalent bacterial infections globally, predominantly caused by uropathogenic Escherichia coli (UPEC). While the urothelium functions as the primary physical barrier, UPEC can breach this defense, triggering inflammation and tissue damage. Although macrophages are recognized as pivotal defenders against UPEC, the spatial dynamics of their recruitment into the infected urothelium—and the molecular signals orchestrating this process—remained poorly characterized. This study employed spatial proteomics to decode the spatiotemporal dialogue between infected epithelial cells and immune cells during acute bladder infection.

The study applied an integrated spatial proteomics workflow combining MALDI-MSI and LC-MS/MS to profile protein distributions in UPEC-infected murine bladder tissues. The custom-developed SPRING algorithm enabled spatial mapping of cellular interactions directly from tissue sections, while SCHNELL facilitated precise macrophage quantification. Key observations were validated through multimodal imaging and functional in vivo experiments using CX3CR1-deficient mice and targeted IL-6 inhibition.

Figure 1 provides integrated spatial proteomic evidence that UPEC infection drives macrophage recruitment and activation specifically within the bladder urothelium. Proteomic profiling revealed significant upregulation of macrophage-associated proteins—particularly Myo9b and Tim3—in the infected urothelial layer, with Myo9b showing the strongest spatial correlation to the macrophage marker F4/80. Enrichment of chemotaxis and migration pathways further supports active macrophage relocation to the infection site, collectively demonstrating a targeted host immune response at the proteome level.

MSI of macrophage migration and activation Figure 1. Mass spectrometry imaging indicates macrophage migration and activation within the infected urothelium.

This study conclusively demonstrates that spatial proteomics can decode tissue-resolved host-pathogen interactions, identifying the IL-6/CX3CL1 axis as a critical pathway for macrophage recruitment and dual protective functions during bladder infection. These insights establish a foundation for novel UTI therapeutics and diagnostics while affirming spatial proteomics as an indispensable tool for unraveling cellular crosstalk in complex disease microenvironments.

Reference

Bottek J, Soun C, Lill JK, et al. Spatial proteomics revealed a CX3CL1-dependent crosstalk between the urothelium and relocated macrophages through IL-6 during an acute bacterial infection in the urinary bladder. Mucosal Immunol. 2020;13(4):702-714. doi:10.1038/s41385-020-0269-7

* For Research Use Only. Not for use in diagnostic procedures.

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From Our Clients

"I recently used their proteomics service for a project analyzing protein interactions in yeast models. The team was very responsive and helped clarify the methodology they employed, which made me feel confident in the results. The data quality was solid, with clear identification of several key proteins involved in our study. Their thorough analysis enabled me to pinpoint specific interactions that I hadn't considered before, which significantly improved the direction of my research. I appreciate their professionalism and support throughout the process."

Sarah Thompson, University of California, Berkeley

"Our lab collaborated with them on a project studying cancer biomarkers. The proteomics analysis provided was detailed and focused, specifically highlighting the differential expression of proteins between healthy and tumor samples. Their clear explanations of the data helped my team understand the biological implications. I also appreciated their willingness to revise the reports based on our feedback, ensuring that we had everything we needed for our publication. This collaborative spirit was invaluable."

Emily Rodriguez, Stanford University

"Our lab worked with them on a project studying the effects of diet on gut microbiota using proteomics. They used a label-free quantification method to analyze proteins in fecal samples before and after dietary intervention. The results showed significant changes in protein expression linked to microbial activity. This was pivotal for our hypothesis about diet-microbiota interactions. The clarity of their data presentation made it easy for our team to integrate these findings into our ongoing research."

Dr. Lisa Wong, University of Toronto

"My experience with Creative Proteomics during the mass spectrometry analysis was excellent. We sent in human saliva and mouse brain tissue samples, which they expertly analyzed using both LC-MS and GC-MS techniques. The results were invaluable, revealing key metabolites in the saliva and identifying biomarkers linked to brain function in the brain tissue."

Dr. Emily Carter, Senior Research Scientist

"The overall service from Creative Proteomics was outstanding. They made the entire process seamless and efficient, allowing us to focus on our research. We worked with leaf and root samples from various Arabidopsis genotypes for targeted metabolomics analysis. Their thorough profiling of primary and secondary metabolites gave us important insights into how the plants respond metabolically to environmental stress."

Dr. Laura Henderson, Plant Physiologist

"We had a pleasant collaboration with Creative Proteomics on mass spectrometry analysis of lipids. They conducted a detailed analysis of lipid species, providing us with important insights into lipid metabolism and its relationship with metabolic syndrome disease states."

Dr. Sarah Mitchell, Research Scientist

Online Inquiry

Please submit a detailed description of your project. We will provide you with a customized project plan to meet your research requests. You can also send emails directly to for inquiries.

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