Neculai D. et al. (2013) Structure of LIMP-2 provides functional insights with implications for SR-BI and CD36. Nature. 504: 172-176.
LIMPII (Lysosomal Integral Membrane Protein II), also known as LPG85 (85 kDa lysosomal membrane sialoglycoprotein) and as CD36 antigen-like 2 (CD36L2), is a major lysosomal membrane protein. LIMP-II is a type-III protein that traverses the membrane twice, with an N-terminal transmembrane anchor as a result of an uncleaved signal peptide and a second membrane spanning region near the C-terminus, followed by a 20 amino acid cytoplasmic tail. LIMPII is currently known to be a member of a superfamily of scavenger receptor proteins (class B), which also includes scavenger receptor (SR)-B1 and SR-B3. These three proteins share their structure, which comprises two transmembrane domains, a relatively large extracellular domain, and both the amino and carboxyl termini located within the cytoplasm. LIMPII as the mannose-6-phosphate- independent trafficking receptor for beta-glucocerebrosidase.
1μg (R: reducing condition, N: non-reducing condition).