H0786
Heregulin-β, EGF Domain human
≥80% (SDS-PAGE), recombinant, expressed in E. coli, buffered aqueous glycerol solution
Synonym(s):
HRG-β
Sign Into View Organizational & Contract Pricing
Select a Size
100 μG
€819.00
All Photos(1)
Select a Size
Change View
100 μG
€819.00
About This Item
Recommended Products
biological source
human
Quality Level
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
Gene Information
human ... NRG1(3084)
General description
Truncated human sequence (amino acids 178-241) corresponding to the EGF domain and purified as a GST-fusion protein, cleaved with thrombin.
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.
Physical form
Solution in phosphate buffered saline containing 30% glycerol.
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.
Storage Class Code
10 - Combustible liquids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Choose from one of the most recent versions:
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
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
Active Filters
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service
