Recombinant Mouse NOV protein

Background

NOV is a member of the CCN family of secreted cysteine rich regulatory proteins. The full length NOV protein contains four structural domains that confer distinct, and sometimes opposing, biological activities. Elevated expression of NOV is associated with certain tumors, including Wilm’s tumor and most nephroblastomas. However, in other tumor types and certain cancer cell lines, increased tumorgenicity and proliferation is correlated with decreased NOV expression. Additionally, NOV induces cell adhesion and cell migration by signaling through specific cell surface integrins and by binding to heparin sulfate proteoglycans and to fibulin 1C. NOV has also been reported to exert proangiogenic activities. Recombinant Mouse NOV is a 36.4 kDa protein containing 333 amino acid residues. It is composed of four distinct structural domains (modules) - the IGF binding protein (IGFBP) domain, the von Willebrand Factor C (VWFC) domain, the Thrombospondin type-I (TSP type-1) domain, and a C-terminal cysteine knot-like domain (CTCK).

Expression system

Escherichia coli.

Purity

> 95 % by SDS-PAGE and HPLC analyses.

Molecular weight

Approximately 36.4 kDa, a single non-glycosylated polypeptide chain containing 333 amino acids.

Endotoxin

Less than 0.1 EU/μg of rMuNOV as determined by LAL method.

Form

Sterile Filtered White lyophilized (freeze-dried) powder. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM Tris-HCl, pH 8.6, 150 mM NaCl.

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