Purification of Her-2 extracellular domain and identification of its cleavage site
| Autor: | Amy L Lasut, Mark J Rupar, Michael Ramaker, Chao-Xing Yuan, Phillip C Liu, Gregory F Hollis, Ray Meade, Richard Wynn, Nicola T. Neff |
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| Rok vydání: | 2003 |
| Předmět: |
Receptor
ErbB-2 Amino Acid Motifs Molecular Sequence Data Cleavage (embryo) Chromatography Affinity Receptor tyrosine kinase Sequence Analysis Protein Cell Line Tumor Extracellular Humans Amino Acid Sequence Receptor chemistry.chemical_classification Binding Sites biology Immunochemistry Molecular biology Embryonic stem cell Peptide Fragments Protein Structure Tertiary Amino acid Biochemistry chemistry SKBR3 Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization ROR1 biology.protein Biotechnology |
| Zdroj: | Protein Expression and Purification. 29:217-222 |
| ISSN: | 1046-5928 |
| Popis: | The EGF family of receptors belongs to the tyrosine kinase receptor (TKR) family and plays an important role during embryonic and postnatal development and also in the progression of tumors. Her-2/neu/c-erbB-2, a member of the epidermal growth factor receptor family, can be cleaved into a soluble extra cellular domain (ECD) and a membrane-bound stub fragment. Her-2 ECD from a breast cancer cell line SKBR3 was immunopurified and analyzed with matrix-assisted laser desorption ionization (MALDI) and carboxyl terminal amino acid sequencing. A sequence within the juxtamembrane region (only 11 amino acid residues) P AEQR↓AS P was identified most likely as a primary site of cleavage, P A↓EQRAS P as a minor site, that generate the ECD. The sites of cleavage are within the signature motif P/GX5–7P/G highly conserved in the EGF receptor family. |
| Databáze: | OpenAIRE |
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