Recombinant Human Ninjurin-1 Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Format
Carrier-Free

Order Details

Recombinant Human Ninjurin-1 Protein, CF Summary

Details of Functionality
Bioassay data are not available.
Source
E. coli-derived human Ninjurin-1 protein
Asp2-Val81
with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Asp2 & Ser3
Protein/Peptide Type
Innovator Recombinant Proteins
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
9 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
10 kDa, reducing conditions

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 PBS and NaCl.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 250 μg/mL in PBS.

Notes

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

Alternate Names for Recombinant Human Ninjurin-1 Protein, CF

  • Nerve injury-induced protein 1
  • nerve injury-induced protein-1
  • NIN1
  • NINJ1
  • ninjurin 1
  • NINJURIN
  • Ninjurin1
  • Ninjurin-1

Background

Ninjurin-1 (nerve injury-induced protein 1) is a 20-22 kDa member of the Ninjurin family of transmembrane (TM) proteins (1, 2). It is expressed by Schwann cells, neurons and hepatocytes and participates in intercellular homophilic binding during nerve regeneration. Human Ninjurin-1 is 152 amino acids in length. It has an unusual membrane orientation. There is an 80 amino acid (aa) N-terminal extracellular domain (ECD) (aa 1-80), followed by a TM segment, a cytoplasmic region, a second TM segment and a C-terminal ECD (aa 142-152). Homophilic binding is divalent-cation dependent and occurs between Pro26 and Asn37 (2). Over aa 1-80, human Ninjurin-1 shares 84% aa sequence identity with mouse Ninjurin-1. Human Ninjurin-1 shares only 50% aa sequence identity with human Ninjurin-2. Expression of NINJ‑1 increased under inflammation conditions, and itself can also exert proinflammatory effects such as stimulating leukocyte migration, and activating TLR4 signaling pathway (3). Inhibiting hemophilic interaction of NINJ1 in circulating tumor cells greatly inhibit the mobility of the cancer cells (4).
  1. Araki, T. and Milbrandt J. (1996) Neuron 17:353.
  2. Araki, T. and Milbrandt J. (1997) J. Biol Chem 272:21373.
  3. Jennewein, C. et. al. (2015) Am J Respir Cell Mol Biol 53:656.
  4. Park, J. et. al. (2017) Anticancer Res 37:1687.

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