Recombinant Human NOV(Discontinued)
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| Amount : | 20 µg |
| Purification : | Purity: >= 95% by SDS-PAGE gel and HPLC analyses. |
| Content : | This recombinant protein is supplied in lyophilized form. |
| AA sequence : | MQVAATQRCP PQCPGRCPAT PPTCAPGVRA VLDGCSCCLV CARQRGESCS DLEPCDESSG LYCDRSADPS NQTGICTAVE GDNCVFDGVI YRSGEKFQPS CKFQCTCRDG QIGCVPRCQL DVLLPEPNCP APRKVEVPGE CCEKWICGPD EEDSLGGLTL AAYRPEATLG VEVSDSSVNC IEQTTEWTAC SKSCGMGFST RVTNRNRQCE MLKQTRLCMV RPCEQEPEQP TDKKGKKCLR TKKSLKAIHL QFKNCTSLHT YKPRFCGVCS DGRCCTPHNT KTIQAEFQCS PGQIVKKPVM VIGTCTCHTN CPKNNEAFLQ ELELKTTRGK M |
Source:E.coli
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 tumorigenicity 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).
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 tumorigenicity 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).
Determined by a cell proliferation assay using BALB/c 3T3 cells. The expected ED50 for this effect is 1.0-2.0 µg/ml
For Research Use Only. Not for use in diagnostic/therapeutics procedures.
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