GULP1/CED-6 Antibody

GULP1 (also PTB domain-containing engulfment adaptor protein 1 and Cell death protein 6 homolog/CED6) is a 36-40 kDa, cytosolic member of the ced-6 family of proteins. It is expressed by multiple cell types, including macrophages, neurons and sinusoidal endothelial cells, and is believed to play a key role in phaogcytosis, particularly involving apoptotic cells. Failure to remove apoptotic cells is suggested to contribute to chronic inflammatory conditions. GULP1 is involved with a MEGF10:GULF:stabilin-1:stabilin-2 internalization pathway. Possibly following endosome formation, it binds to transmembrane activated stabilins and/or LRP1 as a homodimer, and serves as an intermediate for signal transduction. GULP1 also binds to APP, facilitating its proteolysis and the generation of A beta. Human GULP1 is 304 amino acids (aa) in length. It contains one PTB domain (aa 17-154) that interacts with transmembrane receptors, a Leu-zipper (aa 163-193) that mediates dimerization, and a Pro-rich region (aa 238-271) that is likely involved with signal transduction. There are three splice variants. One shows a deletion of aa 31-133, a second contains a 34 aa substitution for aa 134-304, and a third contains a 10 aa substitution for aa 282-304. Over aa 1-92, human GULP1 shares 99% aa sequence identity with mouse GULP1.