Recombinant Mouse Sortilin Protein, CF


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Product Details

Reactivity MuSpecies Glossary
Applications Binding Activity

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Recombinant Mouse Sortilin Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. Immobilized rmSortilin at 4 µg/mL (100 µL/well) can bind rh beta -NGF with a linear range of 3-200 ng/mL.
Mouse myeloma cell line, NS0-derived mouse Sortilin protein
Gly76-Asn753, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Protein/Peptide Type
Recombinant Proteins
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.


Theoretical MW
76.4 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
95-100 kDa, reducing conditions

Packaging, Storage & Formulations

Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Lyophilized from a 0.2 μm filtered solution in PBS.
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.


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

Alternate Names for Recombinant Mouse Sortilin Protein, CF

  • 100 kDa NT receptor
  • Glycoprotein 95
  • Gp95
  • Gp95LDLCQ6
  • Neurotensin receptor 3
  • NT3NTR3
  • Ntr3
  • SORT1
  • sortilin 1
  • Sortilin


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.

  1. Petersen, C.M. et al. (1997) J. Biol. Chem. 272:3599.
  2. Westergaard, U.B. et al. (2004) J. Biol. Chem. 279:50221. 
  3. Petersen, C.M. et al. (1998) EMBO J. 18:595. 
  4. Nielsen, M.S. et al. (2001) EMBO J. 20:2180. 
  5. Hermans-Borgmeyer, I. et al. (1999) Mol. Brain Res. 65:216.
  6. Mazella, J. et al. (1998) J. Biol. Chem. 273:26273.
  7. Nykjaer, A et al. (2004) Nature 427:843.
  8. Teng, H.K. et al. (2005) J. Neurosci. 25:5455.
  9. Chen, Z.-Y. et al. (2004) J. Neurosci. 25:6156.
  10. Shi, J and K.V. Kandror (2005) Dev. Cell 9:99.
  11. Nielsen, M.S. et al. (1999) J. Biol. Chem. 274:8832.

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Gene Symbol Sort1