Abstract
The human neuregulin 1-beta1 (NRG1-beta1, amino acid residues 176-246) was chemically synthesized by Fmoc-based solid phase peptide synthesis (SPPS) followed by folding in a redox buffer. The biological activity of the synthesized NRG1-beta1 was confirmed by ligand-induced tyrosine phosphorylation on Chinese hamster ovary (CHO) cells expressing ErbB-4.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acids / chemistry*
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Epidermal Growth Factor / chemistry*
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Epidermal Growth Factor / physiology
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Fluorenes / chemistry*
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Humans
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Nerve Tissue Proteins / chemistry*
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Neuregulin-1
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Peptides / chemical synthesis*
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Polymers / chemical synthesis*
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Polymers / chemistry
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Protein Structure, Tertiary
Substances
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Amino Acids
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Fluorenes
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N(alpha)-fluorenylmethyloxycarbonylamino acids
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NRG1 protein, human
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Nerve Tissue Proteins
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Neuregulin-1
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Peptides
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Polymers
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Epidermal Growth Factor