protein

Fibronectin Protein, Human

HY-P70593

5 μg;10 μg;50 μg

35;50;125 USD

Fibronectin Protein, Human

proteins

E. coli

5 μg;10 μg;50 μg

35;50;125 USD

Fibronectin is a glycoprotein located in the extracellular matrix that can bind to collagen, fibrin, heparin, DNA, and actin. Fibronectin is involved in cell adhesion, movement, conditioning, wound healing, and maintaining cell shape. Additionally, by binding to the LILRB4 receptor, Fibronectin can inhibit monocyte activation mediated by FCGR1A/CD64 , thereby exerting immune regulatory effects. Human Fibronectin is a recombinant protein dimer complex with a full length of 573 amino acids (P1270-S1546 & A1721-T2016), expressed in E. coli and is untagged [1] [2] [3] [4] [5] [6] [7] [8] [9] [10] [11] [12] .

Human

Fibronectin is a glycoprotein in the extracellular matrix that plays a role in cell adhesion, wound healing, embryonic development, and immune regulation. Wound healing involves the inflammatory phase, proliferative phase (granulation tissue formation), and remodeling phase. Excessive or abnormal deposition of Fibronectin after injury can lead to diseases such as fibrosis or atherosclerosis. Fibronectin plays a critical role in wound healing, involving initial repair, cell migration, tissue remodeling, and the final stages of healing [1] . (1) Inflammatory Phase: Fibronectin expression is upregulated in response to TGF-β stimulation and binds to integrins on platelets, promoting clot formation and initial cell adhesion. The activation of integrins enhances the accumulation of Fibronectin at the wound site and promotes platelet adhesion and the release of clotting factors [2] . (2) Proliferative Phase: Fibronectin binds to integrins (e.g., α5β1 integrin) and activates β-catenin, facilitating cell adhesion, migration, and proliferation [3] . (3) Remodeling Phase: The degradation and remodeling of Fibronectin depend on MMPs (matrix metalloproteinases) and TIMPs (tissue inhibitors of metalloproteinases) signaling pathways. MMPs degrade Fibronectin in the provisional ECM matrix, while TIMPs inhibit MMP activity to ensure proper ECM remodeling [4] . (4) Healing: Fibronectin binds to integrins (e.g., α5β1 integrin) to promote cell apoptosis and vascular reconstruction. TGF-β regulates Fibronectin expression to reduce excessive fibrosis and scarring [5] . Fibronectin also supports new vessel formation and repair during vascular wound healing, with increased Fibronectin promoting endothelial cell proliferation and capillary ingrowth [6] . Elevated Fibronectin expression may also be associated with tumor formation. The mRNA splicing of the ED-A segment of Fibronectin is dysregulated in human liver tumor tissues and is closely related to portal vein tumor thrombosis (PVTT) formation and intrahepatic tumor metastasis [7] . Fibronectin can bind with Anastellin to form Fibronectin polymers, known as Superfibronectin, which has enhanced adhesive properties. Superfibronectin can inhibit tumor growth, angiogenesis, and metastasis. Anastellin activates p38 MAPK and inhibits lysolipid signaling [8] . Fibronectin also inhibits monocyte activation and exerts immune regulatory effects. Fibronectin protein (Rat) (92.1% similarity to human Fibronectin protein) has been found to have effective anti-inflammatory effects in a chronic nephritis Wistar rat model [9] [10] .

NovoNectin; Fibronectin; FN; Cold-insoluble globulin; CIG; FN; Fibronectin 1

Greater than 95% as determined by reducing SDS-PAGE.

Lyophilized from a 0.2 μm filtered solution of 12.5 mM Sodium Citrate, 1.25% Sucrose, pH 5.5 or PBS, pH 6.8, 5% trehalose, 5% mannitol and 0.01% Tween 80.

Room temperature in continental US; may vary elsewhere.