fn1

Fibronectin is a high molecular glycoprotein present in the blood, connective tissue and at cell surface. It is synthesized by many types of differentiated cells and is believed to be involved in the attachment of cells to the surrounding extracellular matrix. Fibronectin has affinity to the other main components of extracellular matrix, collagen and glycosaminoglycans. Fibronectin Protein, Human, Recombinant (aa 1266-1356, hFc) is expressed in HEK293 mammalian cells with C-hFc tag. The predicted molecular weight is 36.47 kDa and the accession number is P02751-13.

Fibronectin is a high molecular glycoprotein present in the blood, connective tissue and at cell surface. It is synthesized by many types of differentiated cells and is believed to be involved in the attachment of cells to the surrounding extracellular matrix. Fibronectin has affinity to the other main components of extracellular matrix, collagen and glycosaminoglycans. Fibronectin Protein, Human, Recombinant (aa 32-345, His) is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 35.93 kDa and the accession number is P02751-1.

Fibronectin is a high molecular glycoprotein present in the blood, connective tissue and at cell surface. It is synthesized by many types of differentiated cells and is believed to be involved in the attachment of cells to the surrounding extracellular matrix. Fibronectin has affinity to the other main components of extracellular matrix, collagen and glycosaminoglycans. Fibronectin Protein, Human, Recombinant (aa 32-602, His) is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 65.47 kDa and the accession number is P02751-1.

Fibronectin is a high molecular glycoprotein present in the blood, connective tissue and at cell surface. It is synthesized by many types of differentiated cells and is believed to be involved in the attachment of cells to the surrounding extracellular matrix. Fibronectin has affinity to the other main components of extracellular matrix, collagen and glycosaminoglycans. Fibronectin Protein, Human, Recombinant (aa 1266-1356, His) is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 10.81 kDa and the accession number is P02751-13.

Fibronectin is a high-molecular weight glycoprotein of the extracellular matrix that binds to membrane-spanning receptor proteins called integrins. Similar to integrins, fibronectin binds extracellular matrix components such as collagen, fibrin, and heparan sulfate proteoglycans. Fibronectin plays a major role in cell adhesion, growth, migration, and differentiation, and it is important for processes such as wound healing and embryonic development. Altered fibronectin expression, degradation, and organization has been associated with a number of pathologies, including cancer and fibrosis. Anastellin binds fibronectin and induces fibril formation. This fibronectin polymer, named superfibronectin, exhibits enhanced adhesive properties. Both anastellin and superfibronectin inhibit tumor growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and inhibits lysophospholipid signaling.

Fibronectin Protein, Human, Recombinant (His) is expressed in E. coli expression system with His-tag tag. The predicted molecular weight is 23.6 kDa and the accession number is P02751.

SLFN11 Protein, Human, Recombinant (His) is expressed in E. coli expression system with N-10xHis tag. The predicted molecular weight is 69.6 kDa and the accession number is Q7Z7L1.

SLFN12 Protein, Human, Recombinant (His) is expressed in in vitro E. coli expression system.

Fibronectin1(FN1) is a secreted protein and contains 12 fibronectin type-I domains,fibronectin type-II domains and 16 fibronectin type-III domains.Recombinant human fibronectin fragment, is a protein of ~63 kDa containing a central cell-binding domain, a high affinity heparin-binding domain II,and CS1 site within the alternatively spliced III CS region of human fibronectin. Cells bind to a VLA-4 ligand, a CS-I site, and a VLA-5 ligand, a cell attachment domain, and virus vectors binds to a heparin binding domain II, which co-locates the cell and the virus vector on NovoNectin. This process enhances the density of both cells and vectors, and facilitates the gene transduction in the result.