详细说明
- Purity>85%, 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.
- ActivityMeasured by its binding ability in a functional ELISA. Immobilized rhSHH at 4 µg/mL can bind rhBOC with an apparent K D <5 nM.
- SourceMouse myeloma cell line, NS0-derived Asp31-Asp852 & Leu417-Asp852, both with a C-terminal 6-His tag
- Accession #
- N-terminal Sequence
AnalysisAsp31 & Leu417
- Predicted Molecular Mass91.1 kDa
- SDS-PAGE135 kDa, reducing conditions
| 2036-BC | | |
| Formulation Lyophilized from a 0.2 μm filtered solution in PBS. | ||
| Reconstitution Reconstitute at 100 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.
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BOC (Brother of CDO [CAM-related/down-regulated by oncogenes]) is a member of the Immunoglobulin (Ig) superfamily, Ig/Fibronectin (FN) type III repeat family of cell surface proteins (1). Human BOC is a type I transmembrane (TM) protein. It is synthesized as a 1114 amino acid (aa) precursor that contains a 30 aa signal sequence, an 825 aa extracellular domain (ECD), a 21 aa TM segment and a 238 aa cytoplasmic region (1, 2). The ECD contains four Ig-like domains, followed by three FN type III repeats. The third (or juxtramembrane) FN type III repeat (aa 712 - 809) binds SHH (3). The intracellular region is not essential for BOC-containing receptor complex signaling (1). However, it appears both the ECD and intracellular regions of BOC are used to form functional subunit interactions in cis-oriented receptor complexes (1, 4). One 157 aa BOC alternate splice form is reported that shows a 32 aa substitution for aa 126 - 1114. The ECD of human BOC is 92% aa identical to mouse BOC ECD. BOC is found in the embryo associated with muscle precursors, limb mesenchyme, early chondrocytes and neurons (2, 5, 6). It appears to promote muscle differentiation and axon guidance (2, 6). BOC contributes to two multi-subunit receptor complexes. On myocytes, a BOC-associated complex includes CDO, neogenin, netrin, and at least two cadherin homodimers formed by either M- or N-cadherin (2). A second complex on neurons, somewhat ill-defined, potentially includes BOC, CDO and Gas1. Here, BOC and/or CDO interact with SHH, with subsequent “transfer” or presentation of SHH to PTCH1 (6, 7).
- References:
- Kang, J.-S. et al. (2002) EMBO J. 21:114.
- Krauss, R.S. et al. (2005) J. Cell Sci. 118:2355.
- Yao, S. et al. (2006) Cell 125:343.
- Kang, J.-S. et al. (2003) Proc. Natl. Acad. Sci. USA 100:3989.
- Mulieri, P.J. et al. (2002) Dev. Dyn. 223:379.
- Okada, A. et al. (2006) Nature 444:369.
- Allen, B.L. et al. (2007) Genes Dev. 21:1244.
- Long Name:Brother of CDO
- Entrez Gene IDs:91653 (Human); 117606 (Mouse)
- Alternate Names:Boc homolog (mouse); BOC; brother of CDO; Protein BOC
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