Custom Protein Conjugation & Biotinylation

Conjugated Proteins, Consistent Activity

Conjugated proteins can be powerful tools to assess protein-protein interactions in a range of assay formats including immunoprecipitation, flow cytometry, immunoassays, and surface plasmon resonance. To be successful, it is crucial that conjugation does not affect protein structure or activity. We offer protein conjugation services on most R&D Systems proteins.

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Biotinylation

What to Expect

Protein Modifications
Available in vitro Protein Modifications:

  • Biotinylation
  • PEGylation
  • Fluorescent probe labeling
  • Non-standard chemical labels

Features and Benefits
Features and Benefits

  • Only source of labeled protein tested in the same bioassay as unlabeled proteins.
  • Full Quality Control testing including Purity, Activity, and Endotoxin.
  • Removal of free conjugates and determination of conjugate to protein levels.
  • Labeled via carbohydrates or amines to minimize interference of protein function.


VEGF

Bioactivity

Both Biotinylated Recombinant Human VEGF 165 (Catalog # BT293) and unlabeled Recombinant Human VEGF 165 (Catalog # 293-VE) stimulate HUVEC human umbilical vein endothelial cell proliferation. The ED50 for this effect is 1-6 ng/mL. The similarity in activity highlights that the biotinylated protein is fully functional.

TNF-a

Bioactivity

Both Biotinylated Recombinant Human TNF-alpha (Catalog # BT210) and unlabeled Recombinant Human TNF-alpha (Catalog # 210-TA) promotes cytotoxicity in L‑929 mouse fibroblast cells in the presence of the metabolic inhibitor actinomycin D. The ED50 for this effect is 25-100 pg/mL. The similarity in activity highlights that the biotinylated protein is fully functional.

IL-17A/F Heterodimer

Bioactivity

Both Biotinylated Recombinant Human IL-17A/F (Catalog # BT5837) and unlabeled Recombinant Human IL‑17A/F Heterodimer (Catalog # 5837-IL) induces IL-6 secretion by NIH‑3T3 mouse embryonic fibroblast cells. The ED50 for this effect is 0.4-2 ng/mL. The similarity in activity highlights that the biotinylated protein is fully functional.

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