Recombinant Human Collectrin Fc Chimera Protein, CF

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Collectrin, also known as TMEM27 and NX‑17, is a 35‑45 kDa transmembrane protein that shows structural similarity to the C‑terminal region of Angiotensin Converting Enzyme 2 (ACE‑2) but lacks peptidase activity (1, 2). Mature human Collectrin consists of a 127 amino acid (aa) extracellular domain (ECD), a 21 aa transmembrane segment, and a 60 aa cytoplasmic domain (3). Within the ECD, human Collectrin shares 87% and 89% aa sequence identity with mouse and rat Collectrin, respectively. Collectrin is expressed as a disulfide‑linked homodimer of variably glycosylated subunits (4‑6). It is highly expressed in the proximal convoluted tubules of renal collecting ducts and inhibits the proliferation of tubule epithelial cells (3, 6‑8). It associates with several amino acid transporters on the luminal surface of these cells, where it is required for the reabsorption of multiple amino acids (7‑9). Collectrin is also expressed in pancreatic islet beta cells and enhances glucose‑stimulated insulin secretion as well as insulin resistance (4, 5, 9, 10). In both the kidney and pancreas, cytoplasmic Collectrin interacts with multiple components of the SNARE complex and other vesicle trafficking proteins (5, 6). A 25 kDa glycosylated fragment of the ECD can be shed from both renal tubule cells and pancreatic beta cells (4, 10). In beta cells, shedding is mediated by BACE2, and the portion left in the membrane can be subsequently cleaved by gamma‑Secretase, releasing the intracellular domain into the cytosol (11). Inhibition of Collectrin shedding from beta cells results in increased beta cell mass and insulin secretion (11).

Array 7580-CL

• Collectrin/TMEM27 Antibodies
• Collectrin/TMEM27 ELISA Kits
• Collectrin/TMEM27 Lysate
• Collectrin/TMEM27 Protein
• Collectrin/TMEM27 Proteins and Enzyme