Recombinant Human NRG1-beta 1/HRG1-beta 1 His Protein, CF Summary
Additional Information |
His-tag |
Details of Functionality |
Measured in a serum-free cell proliferation assay using MCF‑7 human breast cancer cells. Karey, K.P. et al. (1988) Cancer Research 48:4083. The ED50 for this effect is 0.250-2.50 ng/mL. |
Source |
Chinese Hamster Ovary cell line, CHO-derived human Neuregulin-1 beta 1/NRG1 beta 1 protein Ser20-Lys246, with a C-terminal 6-His tag |
Accession # |
|
N-terminal Sequence |
Ser20 |
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 |
|
Theoretical MW |
26 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 |
36-49 kDa, under 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 with Trehalose. |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 500 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 NRG1-beta 1/HRG1-beta 1 His Protein, CF
Background
The
Neuregulin family of structurally related glycoproteins comprises products from
four distinct but related genes, Nrg-1, Nrg-2, Nrg-3, and Nrg-4. Through
alternative splicing or the use of alternative promoters, Nrg-1 has been
shown to encode more than 14 soluble or transmembrane proteins. The
extracellular domain of the transmembrane NRG1 isoforms can be proteolytically
cleaved to release soluble growth factors. All NRG1 isoforms contain an EGF-like
domain ( alpha - or beta -splice variant that differ in their C-terminal region) that is
required for their direct binding to the ErbB3 or ErbB4 receptor tyrosine
kinases. In the 25 kDa NRG- beta 1 isoform, The EGF-like domain differentiates from
the canonical sequence from amino acids 213-234(QPGFTGARCTENVPMKVQNQEK →
PNEFTGDRCQNYVMASFYKHLGIEFM). Human NRG- beta 1 shares a 93.0% amino acid sequence identity to
the mouse and rat sequences. (Uniprot). The ErbB3 or
ErbB4 subsequently recruits and heterodimerizes with ErbB2, resulting in
tyrosine phosphorylation and NRG1 signaling. NRG1 isoforms can be classified
into three major subtypes. Type I (Neu Differentiation Factor, NDF; Heregulin,
HRG; Acetylcholine Receptor Inducing Activity, ARIA) and type II (Glial Growth
Factor, GGF) NRG1s have an immunoglobulin (Ig)-like domain N-terminal to the
EGF-like domain. Type I NRG1s differ from type II NRG1s by having a
glycosylation-rich domain between the Ig-like and the EGF-like domains. Type
III NRG1s (Sensory and Motor Neuron-Derived Factor) lacks the Ig-like domain
but has a cysteine rich domain (CRD) instead. NRG1 isoforms show distinct
spatial and temporal expression patterns. These proteins play important roles
during development of both the nervous system and the heart. While myocardiocytes express multiple isoforms of NRG,
NRG1 beta is a stronger activator of ErbB4 than NRG1 alpha (4,5). Activation of ERbB4 is
critical for development and differentiation of myocardiocytes(6). They have
been shown to regulate the selective expression of neurotransmitter receptors
in neurons and at the neuromuscular junction and promote the differentiation
and development of Schwann cells from neural crest stem cells. NRG1s have also
been shown to be involved in the establishment of the oligodendroglial lineage.
1. Buonanno, A., and G.D Fischbach (2001) Curr. Opin.
Neurobiol.
11:287.
2. Adlkofer, K. and C. Lai (2000) Glia
29:104.
3. Garratt, A.N. et al., (2000) BioEssays 22:987.
4. Yun Du et. al. (2012) J. Am. Chem. Soc. 134:6720.
5. Cote, G. et al. (2005). Exp. Cell Res. 311:135.
6. Pentassuglia, L. and Sawyer, D. (2009).
Experimental Cell Research. 315:627.
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