Measured by its ability to activate Wnt induced TCF reporter activity in HEK293 human embryonic kidney cells expressing human Frizzled-4 and human LRP-5. The ED50 for this effect is 40-200 ng/mL.
Source
E. coli-derived mouse Norrin protein Lys25-Ser131, with an N-terminal Met
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
12.3 kDa (monomer). 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.
Publications
Read Publications using 3497-NR/CF in the following applications:
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.
Buffer
Lyophilized from a 0.2 μm filtered solution in HCl.
Purity
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse Norrin Protein, CF
EVR2
exudative vitreoretinopathy 2 (X-linked)
FEVR
ND
NDP
Norrie disease (pseudoglioma)
Norrie disease protein
Norrin
X-linked exudative vitreoretinopathy 2 protein
Background
Norrin (also called Norrie Disease Protein or NDP) is a secreted regulatory protein that remains tightly associated with the extracellular matrix (1). At least 70 mutations of human Norrin have been identified in Norrie disease (X-linked retinal dysplasia) or in a minority of X-linked familial exudative vitreoretinopathy (FEVR). Both are disorders of retinal vascularization that cause blindness (2, 3). Norrin consists of disulfide-linked homodimers that oligomerize further via disulfide bridges to form higher order oligomers containing up to ten 12 kDa units. The cysteine-rich C-terminal domain of Norrin shows homology to von Willebrand factor, several extracellular mucin proteins, and members of the TGF-beta family. Molecular modeling studies predict that Norrin assumes the cysteine-knot structure typical of the TGF-beta family (4). Although Norrin is not related to Wnt family proteins, it functions like a Wnt protein in that it binds with high affinity to the receptor Frizzled-4, requires LDL receptor-related protein (LRP) as a co-receptor, and induces activation of the canonical Wnt signaling pathway (5). Norrin and Frizzled-4 are widely expressed, but at relatively low levels, in tissues displaying vascular phenotypes. Genetic disruption of either Norrin or Frizzled-4 results in blindness and progressive deafness due to vascular abnormalties (5-7). Female Norrin-/- mice are infertile due to abnormalities in decidual vasculature (8). Mature mouse Norrin shares 97-98% aa identity with human, canine and bovine Norrin.
Perez-Vilar, J. and R.L. Hill (1997) J. Biol. Chem. 272:33410.
Berger, W. et al. (1992) Nat. Genet. 1:199.
Berger, W. and H.H. Ropers, 2001, in “The Metabolic and Molecular Bases of Inherited Diseases”, C.R. Scriver, et al., eds., pp. 5977.
Meitinger, T. et al. (1993) Nat. Genet. 5:376.
Xu, Q. et al. (2004) Cell 116:883.
Hartzer, M.K. et al. (1999) Brain Res. Bull. 49:355.
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