Recombinant Mouse Sortilin Protein, CF
Recombinant Mouse Sortilin Protein, CF Summary
Gly76-Asn753, with a C-terminal 6-His tag
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 100 μg/mL in sterile 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.
Sortilin (neurotensin receptor 3, glycoprotein 95) is a 95 kDa Type I transmembrane monomeric glycoprotein that is one of five known members of the mammalian vacuolar protein sorting 10p domain (Vps10p-D) family of sorting receptors (1, 2). Mouse preprosortilin is processed by signal sequence cleavage followed by propeptide cleavage at a furin recognition site. The cationic propeptide exhibits pH-dependent high affinity binding that blocks the Sortilin ligand binding site both pre- and post-cleavage (3). The extracellular/luminal sequence comprises the Vps10p domain, including 10 conserved cysteines (10CC) essential for ligand binding (2). The cytoplasmic domain sorting motifs confer all trafficking during synthesis, targeting to lysosomes, endocytosis and Golgi-endosome transport; as little as 10% may be found on the cell surface (4). Mature mouse Sortilin shares 98% amino acid (aa) identity with rat, and 91% aa identity with human and canine sortilin. During murine development, sortilin is mainly expressed in the nervous system (5), where it is a receptor for neuropeptides including neurotensin, nerve growth factor (NGF) and brain-derived neurotrophic factor (BDNF) (6 - 9). ProNGF (or the NGF propeptide alone) binds sortilin with a much higher affinity (KD ~5-8 nM) than does mature NGF (KD ~90 nM). The complex of sortilin, pro-NGF and the receptor p75ntr results in endocytosis of proNGF and induction of apoptosis (7). Similar results have been obtained with proBDNF and BDNF (8 - 9). Sortilin is expressed in other tissues including testis, skeletal muscle and fat (1, 10). It is essential and sufficient for biogenesis of Glut4 storage vesicles necessary for insulin responsiveness in adipocytes (10). Sortilin also binds lipoprotein lipase (11), apoE (2) and RAP (1, 11). Binding is competitive, indicating that although unrelated, targets likely bind the same site.
- Petersen, C.M. et al. (1997) J. Biol. Chem. 272:3599.
- Westergaard, U.B. et al. (2004) J. Biol. Chem. 279:50221.
- Petersen, C.M. et al. (1998) EMBO J. 18:595.
- Nielsen, M.S. et al. (2001) EMBO J. 20:2180.
- Hermans-Borgmeyer, I. et al. (1999) Mol. Brain Res. 65:216.
- Mazella, J. et al. (1998) J. Biol. Chem. 273:26273.
- Nykjaer, A et al. (2004) Nature 427:843.
- Teng, H.K. et al. (2005) J. Neurosci. 25:5455.
- Chen, Z.-Y. et al. (2004) J. Neurosci. 25:6156.
- Shi, J and K.V. Kandror (2005) Dev. Cell 9:99.
- Nielsen, M.S. et al. (1999) J. Biol. Chem. 274:8832.
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