Human Neuregulin 3 (NRG3) Protein

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Description
Human Neuregulin 3 (NRG3) Protein is a Recombinant Human protein expressed in E. coli.
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Product specifications
Category | Proteins and Peptides |
Immunogen Target | Neuregulin 3 (NRG3) |
Host | E. coli |
Origin | Human |
Conjugation | Unconjugated |
Observed MW | Concentration: Prior to lyophilization: 200 µg/ml Sequence Fragment: Please enquire. Tag: N-terminal His tag |
Expression | Recombinant |
Purity | > 90% |
Size 1 | 1 mg |
Size 2 | 5 mg |
Form | Lyophilized To keep the original salt concentration, we recommend reconstituting to the original concentration prior to lyophilization (see Concentration) in ddH2O. If a lower concentration is required, dilute in PBS, pH 7.4. If a higher concentration is required, the product can be reconstituted directly in PBS, pH 7.4, though please note that this will change the overall salt concentration. The stock concentration should be between 0.1-1.0 mg/ml. Do not vortex. |
Tested Applications | WB, SDS-PAGE |
Buffer | Prior to lyophilization: PBS, pH 7.4, containing 0.01% Sarcosyl, 1 mM DTT, 5% Trehalose and Proclin-300. |
Availability | Shipped within 1-2 months. |
Storage | Store at 2-8 °C for up to one month. Store at -80 °C for up to one year. Avoid repeated freeze/thaw cycles. |
Dry Ice | No |
Alias | HRG3,pro-NRG3,Pro-neuregulin-3 membrane-bound isoform |
Background | Protein NRG3 |
Status | RUO |
Note | This product is for research use only. Not for human consumption, cosmetic, therapeutic or diagnostic use. |
Descripción
Neuregulin 3 (NRG3) is a specialized member of the neuregulin family, characterized by its expression in the central nervous system during key stages of brain development and throughout adulthood. It plays critical roles in cortical formation, neuronal migration, and the establishment of synaptic signaling networks. Acting through ErbB4 receptors, NRG3 is involved in shaping neural circuits that influence cognitive and behavioral functions. Variations in the NRG3 gene have been associated with psychiatric disorders such as schizophrenia and autism spectrum disorders. Its emerging importance in brain development and function makes it a valuable target for investigating neurological and psychiatric conditions, as well as for the development of innovative therapies.
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NRG3, which belongs to the neuregulin family, is a direct ligand for the ERBB4 tyrosine kinase receptor. Binding results in ligand-stimulated tyrosine phosphorylation and activation of the receptor. NRG3 does not bind to the EGF receptor, ERBB2 or ERBB3 receptors. The protein exists as an type I membrane protein and as a proteolytically released soluble growth factor form. The membrane-bound form does not appear to be active. NRG3 is highly expressed in most regions of the brain with the exception of corpus callosum, and is expressed at lower level in testis. It is not detected in heart, placenta, lung, liver, skeletal muscle, kidney, pancreas, spleen, thymus, prostate, ovary, small intestine, colon and peripheral blood leukocytes. The NRG3 cytoplasmic domain may be involved in the regulation of trafficking and proteolytic processing. Regulation of the proteolytic processing may involve initial intracellular domain dimerization.
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Neuregulin 3 (NRG3) Antibody
NRG3, which belongs to the neuregulin family, is a direct ligand for the ERBB4 tyrosine kinase receptor. Binding results in ligand-stimulated tyrosine phosphorylation and activation of the receptor. NRG3 does not bind to the EGF receptor, ERBB2 or ERBB3 receptors. The protein exists as an type I membrane protein and as a proteolytically released soluble growth factor form. The membrane-bound form does not appear to be active. NRG3 is highly expressed in most regions of the brain with the exception of corpus callosum, and is expressed at lower level in testis. It is not detected in heart, placenta, lung, liver, skeletal muscle, kidney, pancreas, spleen, thymus, prostate, ovary, small intestine, colon and peripheral blood leukocytes. The NRG3 cytoplasmic domain may be involved in the regulation of trafficking and proteolytic processing. Regulation of the proteolytic processing may involve initial intracellular domain dimerization.
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