Human ErbB3 / Her3 Protein, Strep Tag

INTRODUCTION

QC & Assay Protocol

Citation & Background

Synonym
ERBB3,HER3,LCCS2,MDA-BF-1,MGC88033,c-erbB3,erbB3-S,p180-ErbB3,p45-sErbB3,p85-sErbB3
Source
Human ErbB3, Strep Tag (ER3-H5288) is expressed from human 293 cells (HEK293). It contains AA Ser 20 - Thr 643 (Accession # NP_001973.2).
Predicted N-terminus: Ser 20
Request for sequence
Molecular Characterization
This protein carries a twin strep tag at the C-terminus.
The protein has a calculated MW of 71.7 kDa. The protein migrates as 100-110 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.
Endotoxin
Less than 1.0 EU per μg by the LAL method.
Purity
>95% as determined by SDS-PAGE.

Formulation
Lyophilized from 0.22 μm filtered solution in PBS, pH7.4. 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.
No activity loss is observed after storage at:
1. 4-8^°C for 12 months in lyophilized state;
2. -70^°C for 3 months under sterile conditions after reconstitution.

SDS-PAGE

Human ErbB3, Strep Tag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 95%.

Background
ErbB3,also known as Her3 (human epidermal growth factor receptor 3), is a member of the epidermal growth factor receptor (EGFR) family of receptor tyrosine kinases. This membrane-bound glycoprotein has a neuregulin binding domain but has not an active kinase domain. It therefore can bind the ligand but cannot mediate the intracellular signal transduction through protein phosphorylation. However, it does form heterodimers with ErbB2 or other EGFR members responsible for tyrosine phosphorylation to give a receptor complex and initiate the related pathway, which lead to cell proliferation or differentiation. Overexpression of this protein has been reported in numerous cancers, including prostate, bladder, and breast tumors. This protein has different isoforms derived from alternative splicing variants, and among which, the secreted isoform lacking the intermembrane region modulates the activity of membrane-bound form.
References
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