Introduction

Biotree designs and produces specialized magnetic beads (Patented bead D1) to enrich low abundance protein in plasma/serum samples. Developed from Nanomaterial Surface Modification technology, our beads can detect on Astral Zoom as many as 5000 different proteins in plasma/serum samples.

Technical Advantages

◉ High Depth & Broad Coverage:

• Utilizes Bio-Tech's proprietary Magnetic Beads D1 to enrich low-to-medium abundance proteins, exhibiting superior affinity for low-abundance targets.

• Capable of identifying over 5,000 proteins in a single run from human plasma samples.

◉ High Throughput & Rapid Turnaround:

• Features a fully automated sample preparation workflow, reducing the processing time from enrichment to peptide generation to just 7 hours.

• Supports high-capacity processing with 96 samples handled simultaneously in a single batch.

◉ Superior Stability & Enhanced Functional Protein Detection:

• Achieves a consistent detection rate of up to 80% across different batches of the proprietary Magnetic Beads D1.

• Ensures stable and reliable detection of critical functional proteins, such as Tumor Necrosis Factor (TNF) and other key biomarkers.

Sample Requirement

LC-MS Platform

Orbitrap Astral Zoom，Thermo

Applications

◉ Early Disease Diagnosis & Biomarker Discovery: Screen for specific blood protein biomarkers associated with cancer, cardiovascular diseases, and neurodegenerative disorders. This enables early screening, precise diagnostic subtyping, and monitoring of disease progression, significantly enhancing both diagnostic sensitivity and specificity.

◉ Elucidation of Disease Pathological Mechanisms: Compare blood proteome differences between healthy individuals and patients to analyze changes in protein expression, post-translational modifications (e.g., glycosylation), and protein-protein interactions. This reveals the molecular mechanisms driving disease onset and development.

◉ Drug Development & Therapeutic Efficacy Assessment: Identify key regulatory proteins as potential drug targets. Monitor proteomic changes before and after treatment to quantify therapeutic efficacy and optimize dosing regimens. Additionally, detect abnormal expression of toxicity-related proteins to provide early warnings of adverse drug reactions.

◉ Precision Medicine & Disease Subtype Classification: Perform molecular subtyping of diseases (such as tumors) based on blood proteome signatures. By integrating individual protein expression profiles, this approach facilitates the customization of personalized treatment plans and health management strategies.

◉ Health Warning Systems & Aging Research: Establish a baseline blood proteome for healthy populations to predict potential health risks (e.g., metabolic disorders, immune abnormalities) through fluctuations in protein expression. Furthermore, investigate dynamic proteomic changes across different age groups to uncover the molecular regulatory networks associated with aging.

Example Publication

Proteomic Analysis Based on Blood Protein Corona-DIA 1X Technology

Title: Lysozyme modulates inflammatory responses to exacerbate the severity of rheumatoid arthritis

Journal: International ImmunopharmacologyImpact Factor: 4.7

Research Summary: This study investigates the role and underlying mechanisms of Lysozyme (LYZ) in Rheumatoid Arthritis (RA). By integrating Blood Protein Corona-DIA 1X proteomics with single-cell sequencing of synovial fluid, the researchers discovered that LYZ is highly expressed in the plasma of early-stage RA patients and in macrophages within the synovial fluid.

Key findings include:

◉ In Vivo Validation: In a Collagen Antibody-Induced Arthritis (CAIA) model using LYZ1 conditional knockout mice, the absence of LYZ1 significantly alleviated arthritis symptoms, joint damage, and inflammatory responses.

◉ In Vitro Mechanisms: Silencing LYZ in MH7A cells inhibited cell proliferation, promoted apoptosis, and improved inflammatory phenotypes.

◉ Pathway Analysis: RNA sequencing of Fibroblast-Like Synoviocytes (FLSs) revealed that LYZ likely exerts its effects by regulating the TNF signaling pathway and RA-associated genes (e.g., CXCL12, IL-6).

Conclusion:

The study confirms that LYZ exacerbates RA progression by modulating inflammation-related pathways. These findings highlight LYZ's potential as both a biomarker for early RA diagnosis and a promising therapeutic target.