Recombinant Human Nephronectin Protein, CF

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Immobilized Recombinant Human Nephronectin supports theadhesion of SVEC4‑10 mouse vascular endothelial cells. The ED50 for thiseffect is20-120 ng/mL.

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human Nephronectin Protein, CF Summary

Details of Functionality
Measured by the ability of the immobilized protein to support the adhesion of SVEC4‑10 mouse vascular endothelial cells. The ED50 for this effect is 20-120 ng/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived human Nephronectin protein
Glu20-Arg565, with Val144Ile, Ile234Val, Asp377Asn substitutions and a C-terminal 6-His tag
Accession #
N-terminal Sequence
Glu20
Protein/Peptide Type
Recombinant Proteins
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
61 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.
SDS-PAGE
72-95 kDa, reducing conditions
Publications
Read Publication using
9560-NP in the following applications:

Packaging, Storage & Formulations

Storage
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 Tris, NaCl, EDTA and CHAPS.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 200 μg/mL in water.

Notes

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

Alternate Names for Recombinant Human Nephronectin Protein, CF

  • EGFL6L
  • Nctn
  • Nephronectin
  • NPNT
  • POEM

Background

Nephronectin, also named POEM (preosteoblast EGF repeat protein with MAM domain) is a 70-90 kDa extracellular matrix protein that is a ligand for integrin alpha 8 beta 1 (1, 2). The 565 amino acid (aa) human Nephronectin contains a 19 aa signal sequence, a matrilin-type vWA domain, three calcium-binding EGF-like domains, a potential N-linked glycosylation site, a pro/ser/thr-rich mucin-like region, an RGD integrin binding motif, and a MAM domain (1, 3, 4). These features are often present in matrix proteins that, like Nephronectin, mediate cell adhesion and spreading (1, 2, 5). Six human Nephronectin isoforms were identified with alternative splicing. Mature human Nephronectin shows 88% aa identity with both mouse and rat Nephronectin. It is most highly expressed in developing endocrine organs such as parathyroid, thyroid, hypophysis and pineal organ, and around developing bone, teeth, and muscle (1, 2). Pre-osteoblast cells produce Nephronectin, but down-regulate it as they differentiate (1). It is also expressed in the Wolffian duct and ureteric bud basement membranes in the developing kidney, where it is colocalized, and forms an in-vivo complex with integrin alpha 8 beta 1 (2). Since deletion of integrin alpha 8 beta 1 results in renal agenesis, Nephronectin has been proposed to be a critical integrin alpha 8 beta 1 ligand during Nephrogenesis (2, 6).
  1. Morimura, N. et al. (2001) J. Biol. Chem. 276:42172.
  2. Brandenberger, R. et al. (2001) J. Cell Biol. 154:447.
  3. Sato, Y. et al. (2009) J. Biol. Chem. 284:14524.
  4. Patra, C. et al. (2012) Biomaterials. 33:4327.
  5. Yamanda, A. and R. Kamijo (2016) J. Dent. & Oral Disord. 2:1004.
  6. Miner, J. H. (2001) J. Cell Biol. 154:257.

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Publications for Nephronectin (9560-NP)(1)

We have publications tested in 1 confirmed species: Chicken.

We have publications tested in 1 application: Stimulation.


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