Recombinant Human Collectrin Fc Chimera Protein, CF
Recombinant Human Collectrin Fc Chimera Protein, CF Summary
Accession # Q9HBJ8
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS.|
|Reconstitution||Reconstitute at 500 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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).
- Lambert, D.W. et al. (2010) Cell. Mol. Life Sci. 67:89.
- Zhang, Y. and J. Wada (2007) Biochem. Biophys. Res. Commun. 363:1.
- Zhang, H. et al. (2001) J. Biol. Chem. 276:17132.
- Akpinar, P. et al. (2005) Cell Metab. 2:385.
- Fukui, K. et al. (2005) Cell Metab. 2:373.
- Zhang, Y. et al. (2007) PLoS ONE 5:e414.
- Danilczyk, U. et al. (2006) Nature 444:1088.
- Malakauskas, S.M. et al. (2007) Am. J. Physiol. Renal Physiol. 292:F533.
- Malakauskas, S.M. et al. (2009) Mol. Endocrinol. 23:881.
- Altirriba, J. et al. (2010) Diabetologia 53:1406.
- Esterhazy, D. et al. (2011) Cell Metab. 14:365.
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