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Neuregulin-1 (NRG1) type I-α is a trophic factor and member of the neuregulin-1 family of growth factors, which comprises greater than 30 isoforms grouped into types I through VI based on their N-terminal region, which is generated by alternative splicing of NRG1.1 It is composed of a type I N-terminal domain, an immunoglobulin-like (Ig-like) domain, a glycosylated domain, an EGF-like domain, a linker region that contains a proteolytic cleavage site to release the mature protein, a transmembrane domain, and a cytoplasmic tail.1,2 NRG1 type I-α is expressed in brain, liver, and cardiac microvascular endothelial cells and plays a role in neural development, nerve regeneration, and gluconeogenesis.3,4,5,1,6 NRG1 signaling is mediated by homodimers of HER4 and the heterodimers HER2-HER3, HER2-HER4, HER3-HER4, and EGFR-HER4.1 Low tumor levels of NRG1 type I-α are associated with decreased progression-free and overall survival in patients with breast cancer.7 Cayman’s Neuregulin-1 Type I-α EGF Domain (human, recombinant) protein can be used for binding assays. This protein is a disulfide-linked homodimer. The reduced monomer, composed of NRG1 type I-α (amino acids 177-241) fused to human IgG1 Fc at its N-terminus, consists of 326 amino acids and has a calculated molecular weight of 35.8 kDa. The monomer migrates at approximately 38 kDa by SDS-PAGE under reducing conditions.
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1. Neuregulin 1 in neural development, synaptic plasticity and schizophrenia. Nat. Rev. Neurosci. 9(6), 437-452 (2008).
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4. Type I neuregulin1α is a novel local mediator to suppress hepatic gluconeogenesis in mice. Sci. Rep. 7, 42959 (2017).
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6. Neuregulins 1-
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