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ACROBiosystems/Human Neuregulin-4 / NRG4 Protein, His Tag/50ug/NR4
- SynonymNeuregulin-4,NRG4
- SourceHuman Neuregulin-4, His Tag (NR4-H52H3) is expressed from human 293 cells (HEK293). It contains AA Pro 2 - Phe 62 (Accession # Q8WWG1).Predicted N-terminus: Pro 2Request for sequence
- Molecular Characterization
This protein carries a polyhistidine tag at the C-terminus.
The protein has a calculated MW of 8.6 kDa. The protein migrates as 13 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.
- EndotoxinLess than 1.0 EU per μg by the LAL method.
- Purity
>90% as determined by SDS-PAGE.
- Formulation
Lyophilized from 0.22 μm filtered solution in 50 mM Tris, 100 mM NaCl, pH7.5. Normally trehalose is added as protectant before lyophilization.
Contact us for customized product form or formulation.
- Reconstitution
Please see Certificate of Analysis for specific instructions.
For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
- Storage
For long term storage, the product should be stored at lyophilized state at -20°C or lower.
Please avoid repeated freeze-thaw cycles.
This product is stable after storage at:
- -20°C to -70°C for 12 months in lyophilized state;
- -70°C for 3 months under sterile conditions after reconstitution.
Human Neuregulin-4, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 90%.
- BackgroundNeuregulin 4 also known as NRG4 is a member of the neuregulin protein family which in humans is encoded by the NRG4 gene. Loss of expression of NRG4 is frequently seen in advanced bladder cancer while increased NRG4 expression correlates to better survival. The neuregulins, including NRG4, activate type-1 growth factor receptors (EGFR) to initiating cell-to-cell signaling through tyrosine phosphorylation. Furthermore, NRG4 is a low affinity ligand for the ERBB4 tyrosine kinase receptor. Concomitantly recruits ERBB1 and ERBB2 coreceptors, resulting in ligand-stimulated tyrosine phosphorylation and activation of the ERBB receptors. NRG4 does not bind to the ERBB1, ERBB2 and ERBB3 receptors.
- References
- (1)Memon AA., et al., 2004, Br J Cancer. 91(12):2034-41.
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