Recombinant Human BOC Protein, CF Summary
Asp31-Asp852 & Leu417-Asp852, both with a C-terminal 6-His tag
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.
|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.
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).
- 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.
Citation for Recombinant Human BOC Protein, CF
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
1 Citation: Showing 1 - 1
Widespread potential for growth-factor-driven resistance to anticancer kinase inhibitors.
Authors: Wilson TR, Fridlyand J, Yan Y, Penuel E, Burton L, Chan E, Peng J, Lin E, Wang Y, Sosman J, Ribas A, Li J, Moffat J, Sutherlin DP, Koeppen H, Merchant M, Neve R, Settleman J
Sample Types: Whole Cells
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