Human Fibronectin III 10 N-GST

This recombinant FN fragment corresponds to amino acids 1416-1509 of type-III 10.

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.

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Catalog Number Product DataSheet Size AVAILABILITY Price Qty
EUR119
Human Fibronectin III 10 N-GST
250ug In stock
Regular Price:$151.00
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Specifications

Product Type: Protein
Name: Recombinant Human Fibronectin III 10; amino acids 1416-1509
Accession ID: Q9H6D8, Q5VTL7, Q8TC99, Q8BJN4
Source: Human protein expressed in E. coli DH5 alpha carrying the cloned gene in pGEX-2T
Molecular Weight: 36389.8 Da
Amino Acid Sequence: VSDVPRDLEVVAATPTSLLISWDAPAVTVRYYRITYGETGGNSPVQEFTVPGSKSTATISGLKPGVDYTITVYAVTGRGDSPASSKPISINYRT
Fusion Tag(s): GST, N-terminal
Purity: > 90% by SDS-PAGE
Buffer: Solution in PBS
Concentration: 2.4mg/mL
Storage: Store at -80C
Shipped: Dry ice

Provider
From the laboratory of Denise C. Hocking, PhD, University of Rochester Medical Center.
Comments
Schematic representation of a fibronectin subunit and recombinant fibronectin fusion protein.
References
  1. Hocking, D.C., Smith, R.K., and McKeown-Longo, P.J. (1996) A novel role for the integrin-binding III10 module in fibronectin matrix assembly. J. Cell Biol. 133:431-444.

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