protein

NRG1 Heregulin-B2 Human Recombinant Protein

PROTQ02297

10 ug, 50 ug, 1 mg

NRG1 Heregulin-B2 Human Recombinant Protein

https://www.bosterbio.comnrg1-heregulin-b2-human-recombinant-protein-protq02297-boster.html

NRG1

10 ug, 50 ug, 1 mg

Mouse

Cell Culture

Introduction: Neuregulin is a signaling protein for ErbB2/ErbB4 receptor heterodimers on the cardiac muscle cells, playing an important role in heart structure and function through inducing ErbB2/ErbB4 receptor phosphorylation and cardiomyocyte differentiation. Research on molecular level discovered that neuregulin recombinant could make disturbed myocardial cell structure into order and strengthen the connection between myocardial cells by intercalated discs re-organization. Pharmacodynamic experiments in animals showed that neuregulin (NRG1) recombinant can reduce the degree of damage on myocardial cells caused by ischemia, hypoxia and viral infection.

Recombinant Human Neuregulin-1 beta 2 produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 61 amino acids and having a total molecular mass of 7.0kDa. NRG-1 is purified by proprietary chromatographic techniques.

E. Coli

Sterile Filtered White lyophilized (freeze-dried) powder.

SHLVKCAEKEKTFCVNGGECFMVKDLSNPSRYLCKCPNE
FTGDRCQNYVMASFYKAEELYQ.
Amino Acid Sequence:

Greater than 96.0% as determined by:. (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE.

Lyophilized NRG1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Heregulin should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.

Q02297

Pro-neuregulin-1, membrane-bound isoform

Pro-neuregulin-1, membrane-bound isoform;Pro-NRG1;Neuregulin-1;Acetylcholine receptor-inducing activity;ARIA;Breast cancer cell differentiation factor p45;Glial growth factor;Heregulin;HRG;Neu differentiation factor;Sensory and motor neuron-derived factor;NRG1;GGF, HGL, HRGA, NDF, SMDF;

Direct ligand for ERBB3 and ERBB4 tyrosine kinase receptors. Concomitantly recruits ERBB1 and ERBB2 coreceptors, resulting in ligand-stimulated tyrosine phosphorylation and activation of the ERBB receptors. The multiple isoforms perform diverse functions such as inducing growth and differentiation of epithelial, glial, neuronal, and skeletal muscle cells; inducing expression of acetylcholine receptor in synaptic vesicles during the formation of the neuromuscular junction; stimulating lobuloalveolar budding and milk production in the mammary gland and inducing differentiation of mammary tumor cells; stimulating Schwann cell proliferation; implication in the development of the myocardium such as trabeculation of the developing heart. Isoform 10 may play a role in motor and sensory neuron development.

Pro-neuregulin-1, membrane-bound isoform: Cell membrane; Single-pass type I membrane protein. Does not seem to be active.

Type I isoforms are the predominant forms expressed in the endocardium. Isoform alpha is expressed in breast, ovary, testis, prostate, heart, skeletal muscle, lung, placenta liver, kidney, salivary gland, small intestine and brain, but not in uterus, stomach, pancreas, and spleen. Isoform 3 is the predominant form in mesenchymal cells and in non-neuronal organs, whereas isoform 6 is the major neuronal form. Isoform 8 is expressed in spinal cord and brain. Isoform 9 is the major form in skeletal muscle cells; in the nervous system it is expressed in spinal cord and brain. Also detected in adult heart, placenta, lung, liver, kidney, and pancreas. Isoform 10 is expressed in nervous system: spinal cord motor neurons, dorsal root ganglion neurons, and brain. Predominant isoform expressed in sensory and motor neurons. Not detected in adult heart, placenta, lung, liver, skeletal muscle, kidney, and pancreas. Not expressed in fetal lung, liver and kidney. Type IV isoforms are brain-specific.