Recombinant Mouse NgR/RTN4R Protein (His Tag) | PKSM041117

Recombinant Mouse NgR/RTN4R Protein (His Tag) | PKSM041117 | Gentaur US, UK & Europe Disrtribition

Synonyms: Reticulon-4 Receptor; Nogo Receptor; NgR; Nogo-66 Receptor; RTN4R; NOGOR

Active Protein: N/A

Activity: Recombinant Mouse Nogo-66 Receptor/Reticulon 4 Receptor is produced by our Mammalian expression system and the target gene encoding Cys27-Ser447 is expressed with a 6His tag at the C-terminus.

Protein Construction: Recombinant Mouse Nogo-66 Receptor/Reticulon 4 Receptor is produced by our Mammalian expression system and the target gene encoding Cys27-Ser447 is expressed with a 6His tag at the C-terminus.

Fusion Tag: C-6His

Species: Mouse

Expressed Host: Human Cells

Shipping: This product is provided as lyophilized powder which is shipped with ice packs.

Purity: > 95 % as determined by reducing SDS-PAGE.

Endotoxin: < 1.0 EU per μg as determined by the LAL method.

Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

Molecular Mass: 46.6 kDa

Formulation: Lyophilized from a 0.2 μm filtered solution of PBS, pH7.4.

Reconstitution: Please refer to the printed manual for detailed information.

Background: Nogo Receptor (NgR) is a glycosylphosphoinositol (GPI)-anchored protein that belongs to the Nogo recptor family. Human NgR is predominantly expressed in neurons and their axons in the central nervous systems. As a receptor for myelin-derived proteins Nogo, myelin-associated glycoprotein (MAG) and myelin oligodendrocyte glycoprotein (OMG), NgR mediates axonal growth inhibition and may play a role in regulating axonal regeneration and plasticity in the adult central nervous system. NgR may be proposed as a potential drug target for treatment of various neurological conditions. Additionally, NgR may play a role in regulating the function of gap junctions.

Research Area: N/A