Human Fibronectin III 1H,8RGD N-GST
This recombinant FN fragment corresponds to amino acids I597-T673 of type-III 1H, joined to A1235-T1325 of type-III 8 by a GS linker, with amino acids E1312-E1315 replaced by GRGDSPAS. Surfaces passively coated with FN III 1H,8RGD support cell adhesion and migration, induce collagen matrix contraction, and display enhanced proliferative activity over either integrin-binding fibronectin fragments or full-length FN.
Fibronectins (FN) are a family of high molecular weight, multidomain glycoproteins composed of two structurally similar subunits which are joined at the carboxyl terminus by disulfide bonds. The primary structure of FN is organized into three types of repeating homologous units, termed types I, II, and III. These modules in turn are organized into functional domains which have been shown to contain multiple binding sites, including those for sulfated glycosaminoglycans, gelatin, fibrin, and cell surface integrin receptors. Twelve type I modules are found grouped at the amino- and carboxyl-terminal regions, and two type II modules are located within the gelatin-binding region. Fifteen to seventeen type III modules are contained within the middle of the molecule and comprise 60% of fibronectin’s sequence.
From the laboratory of Denise C. Hocking, PhD, University of Rochester Medical Center.
Part of The Investigator's Annexe program.
This recombinant FN fragment corresponds to amino acids I597-T673 of type-III 1H, joined to A1235-T1325 of type-III 8 by a GS linker, with amino acids E1312-E1315 replaced by GRGDSPAS. Surfaces passively coated with FN III 1H,8RGD support cell adhesion and migration, induce collagen matrix contraction, and display enhanced proliferative activity over either integrin-binding fibronectin fragments or full-length FN.
Fibronectins (FN) are a family of high molecular weight, multidomain glycoproteins composed of two structurally similar subunits which are joined at the carboxyl terminus by disulfide bonds. The primary structure of FN is organized into three types of repeating homologous units, termed types I, II, and III. These modules in turn are organized into functional domains which have been shown to contain multiple binding sites, including those for sulfated glycosaminoglycans, gelatin, fibrin, and cell surface integrin receptors. Twelve type I modules are found grouped at the amino- and carboxyl-terminal regions, and two type II modules are located within the gelatin-binding region. Fifteen to seventeen type III modules are contained within the middle of the molecule and comprise 60% of fibronectin’s sequence.
From the laboratory of Denise C. Hocking, PhD, University of Rochester Medical Center.
Part of The Investigator's Annexe program.
| Product Type: | Protein |
| Name: | Recombinant Human Fibronectin III 1H,8RGD; amino acids I597-T673, joined to A1235-T1325 by a GS linker (*GS*), with amino acids E1312-E1315 replaced by GRGDSPAS (*GRGDSPAS*) |
| Accession ID: | Q9H6D8, Q5VTL7, Q8TC99, Q8BJN4 |
| Source: | Human protein expressed in E. coli DH5 alpha carrying the cloned gene in pGEX-2T |
| Molecular Weight: | 45490.1 Da |
| Amino Acid Sequence: | IQWNAPQPSHISKYILRWRPKNSVGRWKEATIPGHLNSYTIKGLKPGVVYEGQLISIQQYGHQEVTRFDFTTTSTST*GS*AVPPPTDLRFTNIGPDTMRVTWAPPPSIDLTNFLVRYSPVKNEEDVAELSISPSDNAVVLTNLLPGTEYVVSVSSVY*GRGDSPAS*STPLRGRQKT |
| Fusion Tag(s): | GST, N-terminal |
| Purity: | > 90% by SDS-PAGE |
| Buffer: | Solution in PBS |
| Concentration: | 1.9mg/mL |
| Storage: | Store at -80C |
| Shipped: | Dry ice |
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| Recombinant Human Fibronectin III 1H,8RGD (Left) Schematic representation of a fibronectin subunit and recombinant fibronectin fusion protein. FNIII1H is the heparin-binding, C-terminal fragment of FNIII1. In (Right), aliquots (5 ug) of recombinant protein was electrophoresed on a 10% SDS-polyacrylamide gel and stained with Coomassie Blue. Molecular mass markers are shown on left. Adapted from: Roy, .C., Wilke-Mounts, S. and Hocking, D.C. (2011) Chimeric fibronectin matrix mimetic as a functional growth- and migration-promoting adhesive substrate. Biomaterials 32(8): 2077-2087 |
- Roy, C., Wilke-Mounts, S. and Hocking, D.C. (2011) Chimeric fibronectin matrix mimetic as a functional growth- and migration-promoting adhesive substrate. Biomaterials 32(8): 2077-2087
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