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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 (rhErbB4) Glu26-Pro 651, produced in human 293 cells (HEK293), His Tag

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

More details

ER4-H5221-100

Availability: within 7 days

336,00 €

Background
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]

Source
Recombinant Human ErbB4 / HER4 Protein (rhErbB4) Glu26-Pro 651 (Accession # NP_005226.1)was produced in human 293 cells (HEK293)

Molecular Characterization
rhErbB4, fused with 6×his tag at the C-terminus and has a calculated MW of 70.6 kDa expressed. The predicted N-terminal is Glu26. Protein migrates as 95-110 kDa in reduced SDS-PAGE due to glycosylation.

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

Purity
>95% as determined by SDS-PAGE.

Formulation
Refer to data sheet

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

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

Bioactivity
Measured by its ability to inhibit the biological activity of Neuregulin-1-β1 on MCF-7 human breast cancer cells. In the presence of 10 ng/mL of Recombinant Human NRG1-β1/HRG1-β1 Extracellular Domain. The ED50 for this effect is typically 0.2-2.5 μg/mL.

References

(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.