Human Fibronectin III 11C C-His
This recombinant fragment is modeled after the C-terminal two-thirds of the type-III 11 (amino acids L1532-T1599), which acts as a negative control for type-III 1C FN. Treatment of purified FN in solution with the type-III 11-C does not result in higher molecular weight 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 fragment is modeled after the C-terminal two-thirds of the type-III 11 (amino acids L1532-T1599), which acts as a negative control for type-III 1C FN. Treatment of purified FN in solution with the type-III 11-C does not result in higher molecular weight 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 11, amino acids L1532-T1599 |
| Accession ID: | Q9H6D8, Q5VTL7, Q8TC99, Q8BJN4 |
| Source: | Human protein expressed in E. coliDH5 alpha carrying the cloned gene in pQE12 |
| Molecular Weight: | 8733 Da |
| Amino Acid Sequence: | MRGSLPSSSPVTGYRVTTTPKNGPGPTKTKTAGPDQTEMTIEGLQPTVEYVVSVYAQNPSGESQPLVQTAVTGSRSHHHHHH |
| Fusion Tag(s): | 6-His, C-terminal |
| Purity: | > 95% by SDS-PAGE |
| Buffer: | Solution in PBS |
| Concentration: | 1.1mg/mL |
| Storage: | Store at -80C |
| Shipped: | Dry ice |
Serves as inactive control for Recombinant Human Fibronectin III 1C.
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| Schematic representation of a fibronectin subunit and recombinant fibronectin fusion protein. |
- Morla, A., Zhang, Z., and Ruoslahti, E. (1994) Superfibronectin is a functionally distinct form of fibronectin. Nature 367:193-196.
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