|Detection of Human GPR115 by Western Blot. Western blot shows lysates of HeLa human cervical epithelial carcinoma cell line. PVDF membrane was probed with 1 µg/mL of Goat Anti-Human GPR115 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF5437) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF019). A specific band was detected for GPR115 at approximately 100-110 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 8.|
GPR115 is a member of the LN-7TM family of adhesion-type 7-transmembrane (TM) G-protein coupled receptors (GPCR) that show a long extracellular N-terminus (1, 2). The 695 amino acid (aa) human GPR115 sequence predicts a 21 aa signal sequence, a 385 aa N‑terminal extracellular domain (ECD), seven TM regions separated by 6‑24 aa intracellular and extracellular regions, and a 40 aa cytoplasmic tail. Like other LN-7TM members, the ECD contains a highly glycosylated mucin‑like stalk that is predicted to function in adhesion. This is followed by a cysteine-rich GPCR proteolytic cleavage site (GPS) (1). GPS domains, which have been described in other 7TM proteins including ETL, GPR126, HE6, and Latrophilin-1, are cleavage sites for processing proteins into two subunits (3‑7). Within the N‑terminal region that ends with the predicted cleavage site (aa 22‑347), human GPR115 shares 58% aa sequence identity with the corresponding region of mouse and rat GPR115. GPR115 was identified from expressed sequence tags (ESTs) found in pregnant uterus, breast, and the genitourinary tract (1).
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