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HS Code |
966602 |
| Productname | Fibronectin (Fn) |
| Type | Glycoprotein |
| Source | Human plasma or recombinant |
| Molecularweight | Approximately 440 kDa (dimer) |
| Structure | Dimeric with subunits linked by disulfide bonds |
| Function | Cell adhesion, migration, and wound healing |
| Purity | ≥95% (varies by supplier) |
| Storagetemperature | -20°C to -80°C |
| Solubility | Soluble in water or saline buffers |
| Formulation | Lyophilized powder or sterile solution |
| Isoelectricpoint | Approximately pH 5.5 |
| Applications | Cell culture coating, tissue engineering, ELISA |
| Organism | Human |
| Colorappearance | Off-white to pale yellow (lyophilized) |
| Casnumber | 86088-83-7 |
As an accredited Fibronectin (Fn) factory, we enforce strict quality protocols—every batch undergoes rigorous testing to ensure consistent efficacy and safety standards.
| Packing | Fibronectin (Fn) is supplied in a sterile, lyophilized powder form, packaged in a 1 mg vial with a tamper-evident seal. |
| Shipping | Fibronectin (Fn) is shipped as a lyophilized powder or frozen liquid, typically on dry ice or with cold packs to maintain stability. The packaging ensures protection from temperature fluctuations and contamination. Upon receipt, it should be stored at -20°C or lower until use, according to the manufacturer’s instructions. |
| Storage | Fibronectin (Fn) should be stored at -20°C or below in small aliquots to avoid repeated freeze-thaw cycles, which can degrade the protein. It is typically supplied as a lyophilized powder or solution. Protect from light and moisture, and thaw on ice before use. After reconstitution, store at 4°C for short-term use, keeping it sterile to prevent contamination. |
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Purity 95%: Fibronectin (Fn) with 95% purity is used in cell adhesion assays, where consistent and reproducible cell attachment is achieved. Molecular weight 450 kDa: Fibronectin (Fn) at 450 kDa is used in extracellular matrix coatings for tissue culture, where enhanced cell spreading and proliferation are observed. Endotoxin level <1 EU/mg: Fibronectin (Fn) with endotoxin level <1 EU/mg is used in stem cell culture, where it supports optimal cell viability and reduces inflammation. Sterile filtered: Fibronectin (Fn) sterile filtered is used in biomedical device surface preparation, where contamination risks are minimized for clinical applications. Solubility 1 mg/mL in PBS: Fibronectin (Fn) with solubility of 1 mg/mL in PBS is used in hydrogel formation, where it ensures uniform matrix integration and bioactivity. Storage stability -20°C: Fibronectin (Fn) with storage stability at -20°C is used in long-term biobank sample maintenance, where protein functionality is preserved over extended periods. Lyophilized form: Fibronectin (Fn) in lyophilized form is used in custom formulation for regenerative medicine, where easy reconstitution and transport are required. Human plasma-derived: Fibronectin (Fn) human plasma-derived is used in coating cultureware for primary human cell expansion, where physiological relevance and compatibility are maximized. Concentration 0.1 mg/mL: Fibronectin (Fn) at 0.1 mg/mL is used in neural differentiation protocols, where it supports selective neuronal attachment and outgrowth. Reduced glycosylation: Fibronectin (Fn) with reduced glycosylation is used in mechanistic cell signaling studies, where lower background interference is critical for accurate results. |
Competitive Fibronectin (Fn) prices that fit your budget—flexible terms and customized quotes for every order.
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Years of hands-on chemical production have taught us that purity and consistency in biomolecules demand attention to every detail at every step. Fibronectin (Fn), a high-molecular-weight glycoprotein found in the extracellular matrix and plasma, carries out crucial roles in cell adhesion, growth, migration, and differentiation. As manufacturers, we see the complexity of this protein up close—both its promise and its production challenges. Every batch we prepare goes through rigorous process controls starting from raw material selection, employing advanced chromatography techniques that separate out contaminants not just for regulatory demands but because we know subtle impurities throw off downstream experiments and industrial use. The lot-to-lot reliability that researchers and industry need drives how we structure our processes.
We never lose sight of the fact that end users judge our work based on their own hard results, not the brochures. We developed our Fibronectin (Fn) model with the needs of biomedical research, medical device engineering, and regenerative medicine in mind. During formulation, we avoid animal-derived components as much as possible. Animal-origin factors introduce batch variability and regulatory headaches, which don’t help either side achieve good outcomes. Our human plasma-derived Fibronectin meets high purity—typically more than 95% by SDS-PAGE analysis—with endotoxin levels monitored below acceptable thresholds for cell culture and medical coating applications. Our recombinant variants, for applications needing specific peptide sequences or site-directed labeling, express in mammalian cell systems to retain glycosylation patterns similar to native human Fn—a difference that reveals itself in downstream cell attachment behavior and signaling pathway responses.
In the lab, researchers rely on consistency; clinical trial runs or scaffold fabrication lines cannot afford deviations. We freeze-dry or flash-freeze to retain full bioactivity. Surface-coating protocols we validate in-house give you reliable attachment for fibroblasts, keratinocytes, stem cells, and more. For medical devices, our Fn coatings provide bioactive, non-denaturing protein layers whose functional domains remain exposed for maximum integrin binding. This reduces unpredictable protein-surface interactions later down the manufacturing line, which often saves time and prevents costly setbacks during scale-up or regulatory review.
Having years of feedback from tissue engineers and cell biologists makes a difference in fine-tuning the product. Users working on stem cell expansion or directed differentiation have told us time and again that even small changes in Fibronectin source alter stemness and lineage commitment. Signaling cascades—through integrins like α5β1 and αvβ3—depend on precise exposure of the protein’s RGD motifs and the structural integrity of its modules. We measure that through not only ELISA but also functional cell-based assays, because a high-signal spot on a gel means little if it cannot support cell spreading, proliferation, or migration in practical use. Our batches support robust attachment at low coating concentrations (as little as 1–10 µg/mL), maintaining bioactivity with minimal lot variation. Each product release passes a cell adhesion test with at least two relevant cell types to ensure user-facing results match published data.
Tissue engineers working with decellularized matrices or hydrogel scaffolds require Fn with exceptional solubility and modular integrity. Poorly solubilized proteins precipitate or lose function, while truncated forms miss key biological activities. By controlling storage and shipping conditions, we deliver Fn that dissolves within minutes and maintains consistency in both low- and high-salt environments. Users building vascularized tissue, neural scaffolds, or skin replacements have reported that our Fn supports higher cell viability and migration. That feedback leads us to optimize further, ensuring the protein backbone and all functionally relevant modules remain intact through manufacture and packaging.
Producing Fibronectin for coating applications, we engineer the process so the protein’s critical binding domains remain active following immobilization. Surface chemistry can easily denature sensitive glycoproteins, so compatibility testing goes into every new batch. We track coating density and test substrate types commonly used in the industry—polystyrene, glass, titanium, and custom polymers—because inert laboratory conditions rarely capture the requirements of medical device assembly or diagnostic chip fabrication lines. Our coating procedures consistently yield robust attachment profiles, reducing the time technicians spend troubleshooting uneven cell attachment or non-specific binding. We see this as the difference between a raw ingredient and a true functional reagent.
In pre-filled medical device systems, Fn faces long storage times and sometimes harsh sterilization. Our stabilization protocols allow longer shelf life and minimize loss of structural integrity—all tested with real-time accelerated aging studies and repeated freeze-thaw cycles. We draw on our own experiences providing protein solutions to OEM device manufacturers, knowing their operational environment differs from standard research labs. Pure, stable protein means fewer rejected batches, less device-to-device variation, and quicker regulatory approvals.
Customers often underestimate the value of full traceability until faced with a compliance audit or unexpected cell culture issues. We maintain batch records down to each raw plasma supply, purification run, and QC test. During routine audits, regulators appreciate direct access to our in-house analytics: peptide mapping, isoelectric focusing, glycan analysis, and end-user assay data. This level of transparency results in faster project starts for regulated research and clinical device makers. Traceability, for us, doesn’t just mean paperwork—it means users can connect their lab results or device performance directly to a specific production lot, resolving questions and avoiding costly troubleshooting. Over the last several years, we found this depth of data increasingly vital as more researchers push their work toward clinical translation and face complex regulatory paths with their own product reviewers.
Our experience with customer projects highlights the distinction between Fibronectin and other extracellular matrix proteins such as Collagen, Laminin, and Vitronectin. While Collagen provides structural support, Fibronectin dominates the initiation of cell adhesion and migration, especially for fibroblasts and endothelial cells. Laminin excels in basement membrane assembly, but without functional Fibronectin, early cell spreading and matrix remodeling tend to lag, especially in three-dimensional cultures. Vitronectin finds its place in serum-free and defined media applications, but it lacks the multidomain support structure that researchers require for tissue engineering or complex organoid development. Our batches have been benchmarked side-by-side in diverse cell models. In almost every comparison, users find that specific cell types exhibit higher engagement and signal activation on Fibronectin, supporting faster spreading, increased proliferation, or more reliable differentiation cues. These are not abstract claims—they’re based on feedback from laboratories repeatedly choosing Fn over competitors for high-value or time-sensitive projects.
Scaling protein production introduces new challenges; what works in a pilot batch doesn’t always translate to hundreds of liters. Our years of scale-up experience show the importance of consistent agitation, temperature control, and strict process validation. We refine chromatographic separation stages to eliminate fragment formation and maintain full-length, functioning Fibronectin molecules. Frequent in-process testing—such as absorbance, mass spectrometry, and functional bioassays—catches problems early, reducing downstream risk for device or scaffold makers relying on tight delivery schedules. By having protein chemistry and process engineering under one roof, adjustments happen quickly and efficiently.
Clients expanding from academic projects to industrial commercialization often struggle with batch-to-batch differences. They come to us for documented, reproducible protein quality. As direct manufacturers, we invite customer audits and support technology transfer consultations, helping troubleshoot cell culture, surface modification, or device integration protocols on site, often co-developing standard operating practices to ensure the highest performance in end-user hands. This collaboration sets benchmarks across the supply chain that few third-party distributors attempt to achieve.
Many diagnostic platforms now use immobilized proteins for high-specificity capture. We’ve adapted our Fibronectin production lines to supply buffer-match, endotoxin-limited product for high-sensitivity biosensor chips and microarray systems. Here, the protein's binding reliability directly impacts device sensitivity and repeatability. Users developing microfluidic chips or point-of-care devices count on our Fn to remain stable, active, and free of cross-reactive contaminants. In therapeutic production—such as engineered skin or wound healing matrices—our product supports robust migration and proliferation of key cell types, cutting timelines from concept to clinical exploration. Our relationships with device manufacturers and research hospitals have shown that advanced applications depend less on the “brand” of Fibronectin and more on direct results, traceable paperwork, and proven compatibility with regulatory frameworks. We back each lot with the full analytical and functional dataset, helping innovators clear every hurdle from research to commercialization.
Global advancements in biomanufacturing and regenerative medicine will keep raising the bar for raw material quality and consistency. We produce Fibronectin with a direct understanding of cell biology, surface chemistry, and device engineering. Our years of refining purification, stabilization, and functional validation reflect our belief that real-world results come from manufacturing expertise, not marketing claims. While many see proteins as commodities, daily experience tells us the leap from chemical production to reliable bioreagent only happens through systematic attention, real feedback, and continuous validation. We bring this philosophy to every batch, every audit, and every customer relationship, supporting both research pioneers and established device makers pushing the boundaries of what is possible in cell biology and regenerative medicine.