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Recombinant human ErbB4 /HER4 Protein, His Tag, 100µg  

Recombinant human ErbB4 /HER4 Protein, His Tag, 100µg

Recombinant Human ErbB4 / HER4 Protein, Glu26-Pro 651, produced in human 293 cells (HEK293), His Tag

recombinant human protein HER4, ErbB4, Her-4, ErbB-4

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336,00 €

Receptor tyrosine-protein kinase erbB-4 (ErbB4), also known as Her4, is a single-pass type I transmembrane glycoprotein that is a member of the ErbB family of tyrosine kinase receptors. ErbB family members serve as receptors for the epidermal growth factor (EGF) family of growth factors. ErbB4 is expressed in normal skeletal muscle, heart, pituitary, brain and several breast carcinomas. ERBB4 contains multiple furin-like cysteine rich domains, a tyrosine kinase domain, a phosphotidylinositol-3 kinase binding site and a PDZ domain binding motif. The protein binds to and is activated by neuregulins-2 and -3, heparin-binding EGF-like growth factor and betacellulin. Ligand binding induces a variety of cellular responses including mitogenesis and differentiation. Multiple proteolytic events allow for the release of a cytoplasmic fragment and an extracellular fragment. ErbB4 appears to play important roles in neuronal development, development of the heart and cancer. ERBB4 has been shown to interact with: DLG4[1-2], NRG1, STAT5A,[3-4] and YAP1.[5] Mutations in this gene have been associated with cancer. Other single-nucleotide polymorphisms and a risk haplotype have been linked to schizophrenia.[6]

Recombinant Human ErbB4, His Tag (ER4-H5221) is expressed from human 293 cells (HEK293). It contains AA Gln 26 - Pro 651 (Accession # NP_005226.1).
Predicted N-terminus: Gln 26

Molecular Characterization
This protein carries a polyhistidine tag at the C-terminus.
The protein has a calculated MW of 70.7 kDa. The protein migrates as 95-110 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.

Less than 1.0 EU per μg of the rhErbB4 by the LAL method.

>95% as determined by SDS-PAGE.

Refer to data sheet

See Certificate of Analysis for details of reconstitution instruction and specific concentration.

Avoid repeated freeze-thaw cycles. No activity loss was observed after storage at:
In lyophilized state for 1 year (4°C-8°C); After reconstitution under sterile conditions for 1 month (4°C-8°C) or 3 months (-20°C to -70°C).

Please refer to product data sheet.


(1)Garcia R A., et al., 2000, (UNITED STATES) 97 (7): 3596–601.
(2)Huang, Y Z., et al., 2000, Neuron (UNITED STATES) 26 (2): 443–55.
(3)Williams Christopher C., et al., 2004, J. Cell Biol. (United States) 167 (3): 469–78.
(4)Schulze Waltraud X., et al., 2005, Mol. Syst. Biol. (England) 1 (1): 2005.0008.
(5)Omerovic Jasminka, et al., 2004, Exp. Cell Res. (United States) 294 (2): 469–79.
(6)Silberberg G., et al., 2006, Am J Med Genet B Neuropsychiatr Genet 141 (B2): 142–8.