Active Recombinant Cynomolgus ERBB2 protein, hFc-tagged

• Cat.No.: ERBB2-1216C
• Product Overview: Recombinant Cynomolgus ERBB2 protein()(Met1-Thr652), fused with hFc tag, was expressed in HEK293.

Specification

• Species: Cynomolgus
• Source: HEK293
• Tag: Fc
• Protein Length: Met1-Thr652
• Form: Lyophilized from sterile PBS, pH 7.4.Please contact us for any concerns or special requirements. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hard copy of CoA.
• Bio-activity: 1. Immobilized Her2/ERBB2 Protein, Cynomolgus, Recombinant (ECD, hFc Tag)(Cat:90295-C02H) at 2 μg/ml (100 μl/well) can bind Anti-Erbb2 Antibody (Trastuzumab)(Cat:68046-H002), the EC50 is 15-70 ng/mL.2. Measured by its ability to block anti-ErbB2 mediated inhibition of BT474 human breast ductal carcinoma cell proliferation. The ED50 for this effect is 0.3-1.8 μg/mL in the presence of 0.6 µg/mL Anti-ErbB2/Her2 Monoclonal Antibody.
• Molecular Mass: The recombinant cynomolgus ERBB2 consists 871 amino acids and predicts a molecular mass of 96.4 kDa.
• Endotoxin: < 1.0 EU per μg protein as determined by the LAL method.
• Purity: > 85 % as determined by SDS-PAGE.
• Storage: Samples are stable for up to twelve months from date of receipt at -20°C to -80°C
  Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
• Reconstitution: It is recommended that sterile water be added to the vial to prepare a stock solution of 0.2 ug/ul. Centrifuge the vial at 4°C before opening to recover the entire contents.

Q&As

Do you have a recommended protocol for immobilizing any avi-tagged recombinant proteins on a streptavidin coated plate?

1.Prepare the streptavidin-coated plate by washing it with PBS (phosphate-buffered saline) or another suitable buffer to remove any impurities. 2.Dilute the Avi-tagged protein in the desired buffer at the desired concentration. It is important to use a buffer that is compatible with the protein and does not interfere with its activity or stability. 3.Add the diluted protein to the streptavidin-coated plate and incubate it for a suitable amount of time at room temperature or 4°C. The exact conditions will depend on the specific protein and the desired level of immobilization. 4.Wash the plate with a suitable buffer to remove any unbound protein. 5.Block the remaining binding sites on the plate with a suitable blocking agent such as BSA (bovine serum albumin) or casein. 6.Wash the plate again to remove any unbound blocking agent. 7.Use the immobilized protein for further experiments such as ELISA, Western blotting, or other assays.