Anti-MEGF9 Antibody Picoband® Fluoro488 Conjugated

MEGF9 (Multiple EGF?like domains protein 9; also EGF?like protein 5) is a 63 kDa (predicted) novel transmembrane glycoprotein that shares some homology to beta ?chains of laminin. It is expressed by hepatocytes, cerebellar Purkinje cells, Schwann cells, keratinocytes and intestinal epithelium. MEGF9 is suggested to participate in cell motility, and its absence correlates with tumor cell migration. Mature human MEGF9 is 572 amino acids (aa) in length. It is a single span type I transmembrane protein that contains a 484 aa extracellular region (aa 31?514) plus a 68 aa C?terminal cytoplasmic domain. The extracellular region possesses a lengthy Pro?rich region (aa 55?200), followed by five EGF?like domains (aa 204?451) . MEGF9 may run at approximately 160 kDa in SDS?PAGE, suggesting either heavy glycosylation or dimerization. Over aa 36?514, human MEGF9 shares 76% aa sequence identity with mouse MEGF9.

Required for DNA double-strand breaks (DSBs) formation in unsynapsed regions during meiotic recombination. Probably acts by forming a complex with MEI4 and REC114, which activates DSBs formation in unsynapsed regions, an essential step to ensure completion of synapsis. Not required for HORMAD1 functions in pairing-independent synaptonemal complex formation, ATR recruitment to unsynapsed axes, meiotic silencing of unsynapsed chromatin (MSUC) or meiotic surveillance.

1. Nakayama, M., Nakajima, D., Nagase, T., Nomura, N., Seki, N., Ohara, O. Identification of high-molecular-weight proteins with multiple EGF-like motifs by motif-trap screening. Genomics 51: 27-34, 1998.