Active Recombinant Rhesus ERBB2 protein, His-tagged

• Cat.No.: ERBB2-4113R
• Product Overview: Recombinant Rhesus ERBB2 protein(XP_001090430.1)(Met1-Thr652), fused with His tag, was expressed in HEK293.

Specification

• Species: Rhesus macaque
• Source: HEK293
• Tag: His
• Protein Length: Met1-Thr652
• Form: Lyophilized from sterile PBS, pH 7.4Please contact us for any concerns or special requirements. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.
• Bio-activity: Measured by its binding ability in a functional ELISA. Immobilized Rhesus Her2/ERBB2 His at 2 μg/ml (100 μl/well) can bind Herceptin, the EC50 of Herceptin is 10-50 ng/mL.
• Molecular Mass: The recombinant Rhesus ErbB2 consists of 640 amino acids and predicts a molecular mass of 70.7 kDa. As a result of glycosylation, rhesus ErbB2 migrates as an approximately 105 kDa band in SDS-PAGE under reducing conditions.
• Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method
• Purity: > 95 % as determined by SDS-PAGE. > 90 % as determined by SEC-HPLC.
• 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.