詳細(xì)說明
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Activity
Measured by its ability to mediate Balb/3T3 mouse embryonic fibroblast cell adhesion. Ball, D.K. et al. (2003) Reproduction 125:271. rhNOV, immobilized at 10 μg/mL, 100 μL/well, will mediate >30% Balbc/3T3 cell adhesion (3 x 10 4 cells/well added).
Source
Mouse myeloma cell line, NS0-derived Thr32-Met357, with a C-terminal 10-His tag
Accession #
N-terminal Sequence
AnalysisThr32
Predicted Molecular Mass
37.1 kDa
SDS-PAGE
55 kDa, reducing conditions
1640-NV |
| |
Formulation Lyophilized from a 0.2 μm filtered solution in PBS. | ||
Reconstitution Reconstitute at 250 μg/mL in sterile PBS. | ||
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. | ||
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Background: NOV/CCN3
NOV, also called CCN3, is one of six CCN (CYR61/CTGF/NOV) secreted proteins which share a common multimodular organization (1 - 4). NOV/CCN3 contains an N-terminal IGFBP domain that appears to be non-functional and a vWF type C and thrombospondin type I domain which mediate oligomerization and matrix interactions, respectively (1, 2). The C-terminal cysteine knot domain interacts with several partners, including the matrix protein fibulin 1C (5), Notch-1 (6), and CCN2, with which it may heterodimerize (2). NOV/CCN3 also interacts with the gap junction protein Connexin43 and mediates suppression of proliferation (7). It also binds the calcium binding protein S100A4 and promotes calcium channel activation (8). The 357 amino acid (aa), 44 kDa human NOV/CCN3 shares 80% aa identity with mouse, rat and dog NOV/CCN3, and 78% aa identity with cow NOV/CCN3. NOV/CCN3 also shows 38 - 50% aa identity with other family members including WISP proteins, except for WISP-2/CCN5 which lacks the cysteine knot (1). NOV/CCN3 is widely expressed developmentally, especially in muscle, endothelium, nervous system, adrenal cortex and chondrocytes (1 - 4). In transformed cells, a 32 kDa N-terminally truncated form lacks the signal sequence is localized to the nucleus. Truncation allows a C-terminal nuclear localization sequence to be active (9). Nuclear NOV/CCN3 acts as a transcriptional repressor but promotes proliferation, presumably by interfering with growth control (9). Full length NOV/CCN3 is a secreted matricellular protein which inhibits cell growth. Interaction of NOV/CCN3 with integrins alpha v beta 3 and alpha 5 beta 1 mediates endothelial cell adhesion, chemotaxis, and promotes angiogenesis (10, 11). Over-expression of NOV/CCN3 downregulates myogenic genes such as MyoD (12).
References:
Perbal, B. (2004) Lancet 363:62.
Perbal, B. (2006) Cell Commun. Signal. 4:3.
Martinerie, C. et al. (1994) Oncogene 9:2729.
Snaith, M. R. et al. (1996) Genomics 38:425.
Perbal, B. et al. (1999) Proc. Natl. Acad. Sci. USA 96:869.
Sakamoto, K. et al. (2002) J. Biol. Chem. 277:29399.
Fu, C. T. et al. (2004) J. Biol. Chem. 279:36943.
Li, C. L. et al. (2002) Mol. Pathol. 55:250.
Planque, N. et al. (2006) J. Cell. Biochem. 99:105.
Lin, C. G. et al. (2003) J. Biol. Chem. 278:24200.
Lin, C. G. et al. (2003) J. Biol. Chem. 280:8229.
Calhabeu, F. et al. (2006) Exp. Cell. Res. 312:1876.
Long Name:
Nephroblastoma Overexpressed Gene
Entrez Gene IDs:
4856 (Human); 18133 (Mouse)
Alternate Names:
CCN family member 3; CCN3; CCN3IGF-binding protein 9; IBP-9; IGFBP-9; IGFBP9novH; Insulin-like growth factor-binding protein 9; nephroblastoma overexpressed gene; Nephroblastoma-overexpressed gene protein homolog; NOV; NOVH; protein NOV homolog