Product Name
Heregulin-β, EGF Domain human, ≥80% (SDS-PAGE), recombinant, expressed in E. coli, buffered aqueous glycerol solution
biological source
human
recombinant
expressed in E. coli
assay
≥80% (SDS-PAGE)
form
buffered aqueous glycerol solution
mol wt
185 kDa
packaging
pkg of 100 μg
storage condition
avoid repeated freeze/thaw cycles
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
Quality Level
Gene Information
human ... NRG1(3084)
Analysis Note
Stimulates tyrosine phosphorylation of the ErbB-3/HER-3 receptor.
The biological activity is measured by its ability to activate the c-ErbB3/HER-3 receptor in treated MCF-7 cells.
Biochem/physiol Actions
Growth factor ligand for ErbB3 and ErbB4 receptor tyrosine kinases.
Growth factor ligand for ErbB3 and ErbB4 receptor tyrosine kinases. The binding of HRG results in receptor dimerization and receptor trans-autophosphorylation. The phosphorylated receptors recruit cellular signaling proteins, initiating signaling pathways.
General description
Truncated human sequence (amino acids 178-241) corresponding to the EGF domain and purified as a GST-fusion protein, cleaved with thrombin.
Physical form
Solution in phosphate buffered saline containing 30% glycerol.
Storage Class
10 - Combustible liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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Marcia R Campbell et al.
Cell reports, 38(5), 110291-110291 (2022-02-03)
Effective inactivation of the HER2-HER3 tumor driver has remained elusive because of the challenging attributes of the pseudokinase HER3. We report a structure-function study of constitutive HER2-HER3 signaling to identify opportunities for targeting. The allosteric activation of the HER2 kinase
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