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 Human NOV is a 36.2 kDa protein containing 331 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).
Amino Acid Sequence
Determined by a cell proliferation assay using BALB/c 3T3 cells. The expected ED50 for this effect is 1.0–2.0 µg/ml.
Endotoxin level is <0.1 ng/μg of protein (<1EU/μg).
Centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.1–1.0 mg/ml. Do not vortex. For extended storage, it is recommended to further dilute in a buffer containing a carrier protein, (example 0.1% BSA) and store in working aliquots at –20°C to –80°C.