| First Author | Qian J | Year | 1996 |
| Journal | Biochem Biophys Res Commun | Volume | 225 |
| Issue | 2 | Pages | 406-12 |
| PubMed ID | 8753776 | Mgi Jnum | J:34943 |
| Mgi Id | MGI:82398 | Doi | 10.1006/bbrc.1996.1187 |
| Citation | Qian J, et al. (1996) Cloning of the cDNA for rabbit L-selectin and expression of recombinant protein with a kinase target site to facilitate radiolabeling. Biochem Biophys Res Commun 225(2):406-12 |
| abstractText | The cDNA encoding rabbit L-Selectin has been cloned from a cDNA library, utilizing a PCR-derived probe. It encodes a peptide of 377 amino acids, including a signal peptide of 38 amino acids. Sequence analysis demonstrated extensive homology with L-Selectin's from other species. Recombinant rabbit L-Selectin protein was expressed in eukaryotic cells in a chimeric construct incorporating the entire extracellular portion of the protein coding region, a phosphokinase target site to allow high activity radiolabeling with 32P, and the constant region of the heavy chain of human IgG1 to facilitate purification and detection. Amino-terminal peptide sequencing of recombinant L-Selectin confirmed that the signal peptide had been removed at the expected site. |
