Recombinant Mouse NELL1 Protein, CF Summary
Product Specifications
Arg17-Asn810, with a C-terminal 6-His tag
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
7109-NL
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
| Reconstitution | Reconstitute at 200 μg/mL in 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.
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Reconstitution Calculator
Background: NELL1
NELL1 (neural EGF‑like like protein 1) is an approximately 140 kDa modular glycoprotein that plays an important role in bone physiology (1). NELL1 contains an N‑terminal Laminin G‑like domain and three vWF‑C domains interspersed with five tandem EGF‑like domains (2). Mature mouse NELL1 shares 98% and 93% aa identity with rat and human NELL1, respectively. NELL1 can be retained in the cytosol where it interacts with ARP3 (apoptosis‑related protein 3) and becomes phosphorylated by PKC (3, 4). NELL1 is secreted as an approximately 400 kDa noncovalent homotrimer of heavily glycosylated subunits (5). It is expressed in bone and in select B cell lines (6, 7). NELL1 promotes the osteogenic differentiation of adipose‑derived stromal/stem cells and inhibits adipogenic differentiation (8). It does not promote osteoblastic differentiation from myoblasts, but it does enhance the activity of BMP‑2 in that function (9). NELL1 interacts directly with osteoblasts via Integrin alpha 3 beta 1 (10, 11) and promotes osteoblast differentiation and mineralization (3, 12, 13). It synergizes with BMP‑2 to increase phosphate uptake through the transporters Pit1 and Pit2 in pre‑osteoblasts (14). In vivo, NELL1 expression in the cranium is localized at sites of suture closure (6). Its overexpression induces multiple abnormalities in cranial development including premature suture closure (craniosyntosis) and overlapping sutures (12, 13). Experimental engrafting demonstrates the ability of NELL1 to promote new bone formation and the healing of calvarial defects (13, 15).
- Zhang, X. et al. (2010) J. Dent. Res. 89:865.
- Desai, J. et al. (2006) Hum. Mol. Genet. 15:1329.
- Zou, X. et al. (2011) FEBS Lett. 585:2410.
- Kuroda, S. and K. Tanizawa (1999) Biochem. Biophys. Res. Commun. 265:752.
- Kuroda, S. et al. (1999) Biochem. Biophys. Res. Commun. 265:79.
- Ting, K. et al. (1999) J. Bone Miner. Res. 14:80.
- Luce, M.J. and P.D. Burrows (1999) Gene 231:121.
- James, A.W. et al. (2012) Stem Cells Dev. 21:2170.
- Cowan, C.M. et al. (2007) J. Bone Miner. Res. 22:918.
- Hasebe, A. et al. (2012) FEBS Lett. 586:2500.
- Shen, J. et al. (2012) J. Cell. Biochem. 113:3620.
- Zhang, X. et al. (2002) J. Clin. Invest. 110:861.
- Aghaloo, T. et al. (2006) Am. J. Pathol. 169:903.
- Cowan, C.M. et al. (2012) Biochem. Biophys. Res. Commun. 422:351.
- Xue, J. et al. (2011) Bone 48:485.
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