Fibronectin Human

Fibronectin Human

Purified Human Fibronectin, derived from Human Plasma, with a Molecular Weight of 440kDa.

Shipped with Ice Packs
Cat. No.
BT29678
Source
Human Plasma.
Appearance

The product appears as a white, lyophilized (freeze-dried) powder after filtration.

Fibronectin Rat

Fibronectin Rat

Plasma fibronectin is a glycoprotein that exists in two primary forms: a soluble dimer in plasma and an insoluble dimer in the extracellular matrix (ECM). Elevated levels of plasma fibronectin are linked to severe coronary artery disease and venous thromboembolism (VTE), particularly in males, suggesting a potential connection between biomarkers, arterial atherothrombosis risk factors, and VTE. This protein is involved in numerous cellular processes, including tissue repair, embryogenesis, blood clotting, and cell migration/adhesion. It functions as a general cell adhesion molecule, facilitating the binding of cells to collagen or proteoglycan substrates. Fibronectin plays a critical role in organizing cellular interaction with the ECM by binding to various ECM components and membrane-bound fibronectin receptors on cell surfaces. The plasma form is produced by hepatocytes, while fibroblasts, chondrocytes, endothelial cells, macrophages, and some epithelial cells synthesize the ECM form. This molecule has a molecular weight of 220kDa.
Shipped with Ice Packs
Cat. No.
BT29727
Source
Rat Plasma.
Appearance
Sterile white powder, lyophilized (freeze-dried).

Fibronectin Recombinant

Fibronectin Human Recombinant

Recombinant Human Fibronectin, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 574 amino acids. It has a molecular weight of 62.6 kDa. The purification of recombinant human fibronectin is achieved using proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT29804
Source

Escherichia Coli. 

Appearance
The product appears as a sterile, white powder that has been lyophilized (freeze-dried).
Definition and Classification

Fibronectin is a high-molecular-weight glycoprotein of the extracellular matrix that binds to membrane-spanning receptor proteins called integrins. It also binds to other extracellular matrix proteins such as collagen, fibrin, and heparan sulfate proteoglycans . Fibronectin exists as a protein dimer, consisting of two nearly identical monomers linked by a pair of disulfide bonds . There are two main types of fibronectin in vertebrates: soluble plasma fibronectin, which is a major protein component of blood plasma, and insoluble cellular fibronectin, which is a major component of the extracellular matrix .

Biological Properties

Fibronectin plays a crucial role in cell adhesion, growth, migration, and differentiation . It is expressed in various tissues and is essential for processes such as wound healing and embryonic development . Plasma fibronectin is produced in the liver by hepatocytes, while cellular fibronectin is secreted by various cells, primarily fibroblasts . The expression patterns of fibronectin can vary, and its levels are often altered in response to tissue injury or disease .

Biological Functions

Fibronectin is involved in several key biological functions, including cell adhesion, growth, migration, and differentiation . It plays a significant role in wound healing and embryonic development . Additionally, fibronectin is involved in immune responses and pathogen recognition, as it can bind to various pathogens, including viruses, bacteria, fungi, and protozoa . This binding helps in the clearance of pathogens from the body and supports the immune system’s response to infections .

Modes of Action

Fibronectin interacts with other molecules and cells through specific domains that promote cell-to-cell adhesion, cell-to-basement-membrane attachment, and clot stabilization . It binds to integrin receptors on cell surfaces, which triggers downstream signaling cascades that regulate cell behavior . Fibronectin also plays a role in embryogenesis, nerve regeneration, fibroblast migration, and macrophage function . The shift from soluble to insoluble fibronectin fibrils occurs when cryptic fibronectin-binding sites are exposed along the length of a bound fibronectin molecule .

Regulatory Mechanisms

The expression and activity of fibronectin are regulated by various mechanisms, including transcriptional regulation and post-translational modifications . During extracellular matrix (ECM) assembly and turnover, cells upregulate the assembly of fibronectin into viscoelastic fibrils that can bind numerous growth factors and cytokines . These fibrils play a key role in assembling a provisional ECM during embryonic development and wound healing . Additionally, fibronectin expression can be influenced by factors such as tissue injury, inflammation, and disease .

Applications

Fibronectin has several applications in biomedical research, diagnostic tools, and therapeutic strategies . It is used in tissue engineering and regenerative medicine to promote cell adhesion and tissue repair . Fibronectin-enriched biomaterials are employed to enhance the biological responses at implant sites . In oncology, fibronectin serves as a prognostic and theranostic marker, aiding in cancer diagnosis and therapy . Its role in wound healing and tissue repair also makes it a valuable component in various medical treatments .

Role in the Life Cycle

Throughout the life cycle, fibronectin plays a vital role in development, aging, and disease . During embryonic development, fibronectin is essential for cell migration and tissue organization . In adulthood, it continues to support tissue repair and regeneration . Altered fibronectin expression and organization are associated with various pathologies, including cancer, arthritis, and fibrosis . As organisms age, changes in fibronectin levels and function can impact tissue integrity and contribute to age-related diseases .

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