Recombinant Human/Bovine/Porcine NRG-1, Animal-Free Protein

NRG-1 activity is determined using the Promega serum response element luciferase reporter assay (*) in transfected MCF-7 cells. Cells are treated in triplicate with a serial dilution of NRG-1 for 4 hours. Firefly luciferase activity is measured and normalized to the control Renilla luciferase activity. EC50 = 0.28 ng/ml (37.9 pM).*Promega pGL4.33[luc2P/SRE/Hygro] #E1340

NRG-1 migrates as a single band at 7.5 kDa in non-reducing (NR) conditions and upon reduction (R). No contaminating protein bands are visible.Purified recombinant protein (3 µg) was resolved using 18% w/v SDS-PAGE in reduced (+ beta -mercaptothanol, R) and non-reduced (NR) conditions and stained with Coomassie Brilliant Blue R250.

• Reactivity: Hu, Po, Bv
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human/Bovine/Porcine NRG-1, Animal-Free Protein Summary

• Details of Functionality: No significant difference between EC₅₀ of reference and test lots
• Source: E. coli-derived Neuregulin-1/NRG1 protein
• Accession #: Q02297.3
• Protein/Peptide Type: Animal-Free Recombinant Proteins
• Purity: Single species with expected mass
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 7.5 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: Monomeric NRG-1 protein only

Packaging, Storage & Formulations

• Storage: Store lyophilized protein between -20 and -80 °C until the date of expiry. Avoid freeze-thaw cycles.
• Buffer: Lyophilized from acetonitrile/TFA
• Purity: Single species with expected mass
• Reconstitution Instructions: Resuspend in water at >100 µg/ml, prepare single use aliquots, add carrier protein if desired.

Notes

The above product was manufactured, tested and released by R&D System's contract manufacturer, Qkine Ltd, at 1 Murdoch House, Cambridge, UK, CB5 8HW. The product is for research use only and not for the diagnostic or theraputic use.

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

Alternate Names for Recombinant Human/Bovine/Porcine NRG-1, Animal-Free Protein

• ARIA
• GGF2
• GGFglial growth factor
• Heregulin-1
• HGL
• HGLneu differentiation factor
• HRG
• HRG1
• HRG1-alpha
• HRG1-beta 1
• HRGAneuregulin 1 type IV beta 1a
• MST131
• MSTP131
• NDFheregulin, alpha (45kD, ERBB2 p185-activator)
• neuregulin 1 type IV beta 3
• neuregulin 1
• Neuregulin1
• Neuregulin-1
• NRG1
• pro-neuregulin-1, membrane-bound isoform
• pro-NRG1
• sensory and motor neuron derived factor
• SMDF

Background

Neuregulin-1 (NRG1) belongs to a family of structurally related glycoproteins encoded by four distinct but related genes, Nrg1, Nrg2, Nrg3, and Nrg4. Through alternative splicing or the use of alternative promoters, Nrg1 encodes more than 14 soluble or transmembrane proteins. Type I NRG1 isoforms include Neu Differentiation Factor, Heregulin, and ARIA. These consist of an N-terminal domain, an Ig-like domain, a linker with a Ser/Thr rich region, an EGF-like domain, a transmembrane segment, and a cytoplasmic domain. Type II isoforms such as Glial Growth Factor have a larger N-terminal domain and lack the Ser/Thr rich linker. Type III isoforms such as Sensory and Motor neuron-Derived Factor lack the Ig-like domain but contain a cysteine rich domain (CRD) and a second transmembrane segment (1 - 5). The alpha and beta splice variants of NRG1 differ in their extracellular juxtamembrane regions (3, 6). This recombinant protein corresponds to the extracellular domain (ECD) of the type I alpha isoforms (Accession # Q7RTV8). NRG1 isoforms exhibit distinct expression patterns and functions (7). The EGF-like domain, which is common to all NRG1 isoforms, is required for Neuregulin binding to ErbB3 or ErbB4 receptors (3). ErbB3 or ErbB4 subsequently heterodimerize with ErbB2, resulting in tyrosine phosphorylation and NRG1 induced signaling (1, 2). Soluble growth factors can be released by TACE/ADAM17, BACE, or ADAM19 mediated shedding of the ECD of transmembrane NRG1 (8 - 10). The cytoplasmic region can be cleaved by gamma -secretase, generating a repressor that inhibits the transcription of proapoptotic genes (11). NRG1 regulates multiple nervous system functions including axon guidance, synapse formation and plasticity, glial cell development, and axon myelination (1, 2). In the heart, NRG1 regulates organ morphogenesis and contractility and also plays a cardioprotective role following tissue injury (12). Multiple polymorphisms and aberrant expression of NRG1 isoforms are associated with the development of schizophrenia and many cancers (1, 2, 13).

1. Mei, L. and W.-C. Xiong (2008) Nat. Rev. Neurosci. 9:437.
2. Talmage, D.A. (2008) Novartis Found. Symp. 289:74.
3. Holmes, W.E. et al. (1992) Science 256:1205.
4. Marchionni, M.A. et al. (1993) Nature 362:312.
5. Ho, W.-H. et al. (1995) J. Biol. Chem. 270:14523.
6. Wen, D. et al. (1994) Mol. Cell. Biol. 14:1909.
7. Meyer, D. et al. (1997) Development 124:3575.
8. Hu, X. et al. (2006) Nat. Neurosci. 9:1520.
9. Willem, M. et al. (2006) Science 314:664.
10. Yokozeki, T. et al. (2007) Genes Cells 12:329.
11. Bao, J. et al. (2003) J. Cell Biol. 161:1133.
12. Lemmens, K. et al. (2007) Circulation 116:954.
13. Breleux, M. (2007) Cell. Mol. Life Sci. 64:2358.

Bioinformatics

• Uniprot:
  • Q02297.3()