Fibronectin is an extracellular matrix glycoprotein present on most cell surfaces, in extracellular fluids and in plasma. A high molecular weight heterodimeric protein, it was originally discovered as a protein missing from the surfaces of virus-transformed cells, and it has been shown to be involved in various functions including cell adhesion, cell motility and wound healing. Alternative splicing and glycosylation give rise to several different forms of Fibronectin, some of which exhibit restricted tissue distribution or association with malignancies. It has been shown that Myofibroblast phenotype formation correlates with the occurrence of glycosylated Fibronectin and Fibronectin splice variants in Dupuytren's disease.
Background References
1. Patten J et al. Fibronectin in development and wound healing. Adv Drug Deliv Rev. 2021 Mar
2. Dalton CJ et al. Fibronectin: Molecular Structure, Fibrillar Structure and Mechanochemical Signaling. Cells. 2021 Sep
mIHC analysis of mouse muscle tissue (Formalin/PFA-fixed paraffin-embedded sections) with Rabbit anti-Fibronectin antibody (IRS144RB) at 1/100 dilution. The immunostaining was performed with the IRISKitCmTSA Kit (900808). Heat mediated antigen retrieval with Tris-EDTA buffer (pH 9.0) for 30 mins at 95℃. DAPI (blue) was used as a nuclear counter stain. Image acquisition was performed with Olympus VS200 Slide Scanner.
mIHC analysis of mouse heart tissue (Formalin/PFA-fixed paraffin-embedded sections) with Rabbit anti-Fibronectin antibody (IRS144RB) at 1/100 dilution. The immunostaining was performed with the IRISKitCmTSA Kit (900808). Heat mediated antigen retrieval with Tris-EDTA buffer (pH 9.0) for 30 mins at 95℃. DAPI (blue) was used as a nuclear counter stain. Image acquisition was performed with Olympus VS200 Slide Scanner.
Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"