| Code | CSB-RA919940A0HU |
| Size | US$210 |
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| Application | Recommended Dilution |
|---|---|
| FC | 1:50-1:200 |
Fibronectin 1 (FN1) is a high-molecular-weight glycoprotein that plays a fundamental role in cell adhesion, migration, and extracellular matrix organization. This multifunctional protein serves as a critical mediator of cell-matrix interactions and undergoes proteolytic processing to generate bioactive fragments including anastellin, which has been implicated in anti-angiogenic and anti-tumorigenic activities. FN1's involvement in tissue remodeling, wound healing, and embryonic development makes it a compelling target for researchers investigating cancer progression, cardiovascular biology, and stem cell behavior.
This recombinant monoclonal antibody (clone 25A1) offers the reproducibility and consistency that demanding experimental workflows require. Because it is produced from a defined genetic sequence rather than traditional hybridoma methods, researchers can expect uniform performance across lots, eliminating the variability that can compromise longitudinal studies or multi-site collaborations. The rabbit IgG format provides excellent signal-to-noise characteristics, and affinity chromatography purification ensures high specificity for the target epitope derived from human FN1.
Validation by flow cytometry demonstrates clear detection capability, with testing in 3T3 cells showing distinct positive signal separation from isotype control when used at 1:50 dilution. The protocol employed fixation and permeabilization to access intracellular fibronectin pools, confirming utility for intracellular staining applications. The antibody is also validated for ELISA, providing flexibility across detection platforms.
For investigators exploring the intersection of extracellular matrix dynamics with cancer metastasis, cardiovascular remodeling, developmental processes, or signal transduction pathways, this antibody delivers the technical reliability needed to generate meaningful, reproducible data in human-focused studies.
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