Recombinant Human Neuregulin-2/NRG2 His-tag Protein, CF Summary
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 0.100-1.00 μg/mL. |
Source |
Chinese Hamster Ovary cell line, CHO-derived human Neuregulin-2/NRG2 protein Cys112-Lys404, with a C-terminal 6-His tag |
Accession # |
|
N-terminal Sequence |
Cys112 |
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 |
34 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 |
41-51 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 Neuregulin-2/NRG2 His-tag Protein, CF
Background
Neuregulins (NRGs) are a family of six related physiological
ligands all containing a receptor-binding epidermal growth factor (EGF)-like
domain that mediate their binding to cellular receptors. The EGF-like domain is
responsible for binding to the HER RTK family members (EGFR, HER2, HER3, and
HER4).
Human NRG2, also known as NTAK (neural-and
thymus-derived activator for ErbB kinases), is a ~92 kDa, 850 aa protein
composed of a 111 aa signal sequence, 294 aa extracellular domain, 21 aa
transmembrane domain, and a 424 aa cytoplasmic domain. Human NRG2 shares 95%
homology with mouse and rat NRG. NRG-2 encodes six to eight isoforms that
contain Ig-like domains near their N-termini. The NRG family are involved
in the development of the nervous and cardiovascular systems through the ErbB
signaling pathway (1). They also regulate multiple intercellular signal
transduction and a wide range of biological processes, such as differentiation,
migration, and myelination (2). The primary receptor for NRG-2 is HER4, but
binds directly to both ErbB3 and ErbB4, and transactivates ErbB1 and ErbB2 via
heterodimerization with ErbB3 or ErbB4 (3, 4). Interaction between NRGs and
their receptors plays an important role in the pathogenesis and treatment of
neurodegenerative diseases (5). NRGs can be used as targets for therapeutic or
clinical trials for their multiple roles in many neurological disorders, such
as ALS, brain trauma, spinal cord injury, peripheral neuropathy, and
schizophrenia (2). NRG-2 promotes neuronal survival when bound to ErbB3 on
neurons (6). NRG-2 can indirectly transactivate HER2 and trigger downstream
signaling pathways linked to carcinogenesis, tumor progression, and resistance
to cancer therapies (7). NRG-2 binds to HER3 and HER4 to mediate downstream
signaling linked to breast cancer initiation and progression (8, 9).
- Nagasaka, M. and S-H.I. Ou (2022) Trends Cancer 8:242.
- Ou, G-Y., et al. (2021) Front. Aging Neurosci. 13:662474.
- Carraway, K.L. et al. (1997) Nature 387:512.
- Higashiyama, S. et al. (1997) J. Biochem. 122:675.
- Bublil, E. M., and Y. Yarden (2007) Curr. Opin. Cell Biol. 19:124.
- Nakano N., et al. (2016) Neurosci. Lett. 622:88.
- Meyer, D., et al. (1997) Development 124:3575.
- Yang, L. et al. (2022) Am. J. Cancer Res. 12:2173.
- Centa, A. et al. (2018) Mol. Oncol. 12:1061.
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