Recombinant Human Her2/ErbB2 Protein is expressed from HEK293 with hFc tag at the C-Terminus.It contains Thr23-Thr652.
Pureté
> 95 % as determined by Tris-Bis PAGE,> 95 % as determined by HPLC
Stérilité
0.22 μm filtered
niveau d'endotoxine
Less than 1EU per μg by the LAL method.
Biological Activity Comment
Immobilized Human Her2 at 1μg/ml (100μl/well) on the plate. Dose response curve for Biotinylated Anti-Her2 Antibody , hFc Tag with the EC50 of 0.15μg/ml determined by ELISA. See testing image for detail.
ErbB2/Her2
Origine: Humain
Hôte: HEK-293 Cells
Recombinant
The purity of the protein is greater than 95 % as determined by SDS-PAGE and Coomassie blue staining.
ErbB2/Her2
Origine: Humain
Hôte: HEK-293 Cells
Recombinant
>95 % as determined by SDS-PAGE.
Active
Restrictions
For Research Use only
Format
Lyophilized
Reconstitution
Centrifuge the tube before opening. Reconstituting to a concentration more than 100 μg/mL is recommended. Dissolve the lyophilized protein in distilled water.
Buffer
Lyophilized from 0.22μm filtered solution in PBS ( pH 7.4). Normally 8 % trehalose is added as protectant before lyophilization.
Stock
-20 °C,-80 °C
Stockage commentaire
-20 to -80°C for 12 months as supplied from date of receipt., -80°C for 3-6 months after reconstitution., 2-8°C for 2-7 days after reconstitution., Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
ErbB2, also called Neu and Her2 (human epidermal growth factor receptor 2), is a type I membrane 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.Upon ERBB2 activation, the MEMO1-RHOA-DIAPH1 signaling pathway elicits the phosphorylation and thus the inhibition of GSK3B at cell membrane. This prevents the phosphorylation of APC and CLASP2, allowing its association with the cell membrane.
Poids moléculaire
96.1 kDa. Due to glycosylation, the protein migrates to 100-120 kDa based on Tris-Bis PAGE result.