Human SREC‑I/SCARF1 Biotinylated Antibody

The scavenger receptor (SR) family comprises a group of functionally defined membrane receptors that share a common ability to bind and internalize modified forms of low density lipoproteins (LDL) such as acetylated LDL (AcLDL) and oxidized LDL (OxLDL) (1‑3). Family members are classified alphabetically. They play important roles in lipid metabolism, in host defence and in the regulation of acquired immunity (2, 4). Scavenger receptor expressed by endothelial cells-I (SREC-I) and SREC-II are two proteins that belong to the F type scavenger receptor group (SR-F1 and SR-F2). The full length cDNA of human SREC-I encodes an 830 amino acid (aa) type I transmembrane protein which contains a 19 aa signal peptide, a 402 aa extracellular region, a 21 aa transmembrane segment, and a 388 aa long cytoplasmic domain. The extracellular region contains ten EGF-like repeats (five of which fit the exact consensus sequence for an EGF-like domain) while the cytoplasmic domain is rich in serine and proline in the N-terminal half, and glycine in the C-terminal segment (5, 6). In addition to the full length form, four SREC-I isoforms exist. Two show insertions of a stop codon in EGF-like domain #8, resulting in mature soluble forms of 323 aa and 318 aa, respectively. A third isoform deletes part of domain #8 plus domains #9 and #10; it continues in-frame to generate a mature transmembrane protein of 725 aa. The last isoform shows only cytoplasmic splicing, with 72 aa substituted for the last 332 aa of the full length form. All three transmembrane forms bind acetylated LDL (6). Native SREC-I is approximately 150 kDa in size, and expressed by endothelial cells, macrophages and fetal neurons (7, 8). In the extracellular region human SREC-I is 76% aa identical to mouse SREC-I. The extracellular regions of human SREC-I and II are 53% aa identical.