>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
<0.10 EU per 1 μg of the protein by the LAL method.
Measured by its binding ability in a functional ELISA. When
is immobilized at 2 μg/mL, 100 μL/well, the concentration of
Recombinant Human Nephrin that produces 50% of the optimal binding
response is 0.3-1.5 μg/mL.
Mouse myeloma cell line, NS0-derived human Nephrin protein Gln23-Thr1029, with a C-terminal 6-His tag
When Recombinant Human Podocin/NPHS2 (Catalog # 9287-PO) is coatedonto a microplate at 2 μg/mL, Recombinant Human Nephrin (Catalog # 9399-NN) bindswith an ED50 of 0.3-1.5 µg/mL.
is a 180 kDa type I transmembrane glycoprotein that belongs to the
immunoglobulin superfamily (1). Mature human Nephrin consists of a 1033 amino
acid (aa) extracellular domain (ECD) with eight Ig-like C2-set domains and one
fibronectin type III domain, a 21 aa transmembrane segment, and a 165 aa
cytoplasmic tail (2, 16). Within the ECD, human Nephrin shares 83% aa sequence
identity with both mouse and rat Nephrin (3). Usage of the alternate exon 1B
results in a distinct N-terminal sequence that lacks a clearly defined signal
peptide cleavage site (4). Nephrin is expressed primarily on podocytes in the
renal glomerulus and to a lesser extent in the brain and pancreas (3, 5). The
1B isoform is not expressed in the kidney (4). Nephrin localizes to
intercellular junctions between podocyte foot processes where it functions as a
homophilic adhesion molecule (2, 6). Nephrin is required for formation and
maintenance of the slit diaphragm between these processes (7). It associates
with Neph1, podicin, P-cadherin, and multiple scaffolding proteins which couple
it to the actin cytoskeleton (8-12). Nephrin expression is required for the
anti-apoptotic effect of VEGF on podocytes as well as for the ability of
podocytes to up-regulate Glut1 and Glut4 glucose transporters in response to
insulin (13, 14). Nephrin down-regulation contributes to diabetic nephropathy,
and nephrin mutations underlie the lethal congenital nephritic syndrome NPHS1
Ruotsalainen, V. et al. 1999, Proc. Natl. Acad. Sci. USA 96: 7962.
Holzman, L.B. et al. 1999, Kidney Int. 56:1481.
Putaala, H. et al. 2000, J. Am. Soc. Nephrol. 11:991.
Beltcheva, O. et al. 2003, J. Am. Soc. Nephrol. 14:352.
Putaala, H. et al. 2001, Hum. Mol. Genet. 10:1.
Khoshnoodi, J. et al. 2003, Am. J. Pathol. 163:2337.
Ruotsalainen, V. et al. 2000, Am. J. Pathol. 157:1905.
Barletta, G.M. et al. 2003, J. Biol. Chem. 278:19266.
Huber, T.B. et al. 2001, J. Biol. Chem. 276:41543.
Lehtonen, S. et al. 2004, Am. J. Pathol. 165:923.
Lehtonen, S. et al. 2005, Proc. Natl. Acad. Sci. 102:9814.
Verma, R. et al. 2006, J. Clin. Invest. 116:1346.
Foster, R.R. et al. 2005, Am. J. Physiol. Renal Physiol. 288:F48.
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