Description
Recombinant antibodies at Miltenyi Biotec
As an innovation-powered company with a commitment to quality and excellence, Miltenyi Biotec applies cutting-edge methods to discover and develop newer and better antibodies to satisfy both market demand and regulatory requirements.
The Miltenyi way of generating best-in-class antibodies and antibody conjugates
At Miltenyi Biotec, we opt for recombinant antibodies, which enable sequence verification and optimization for lot-to-lot consistency, making them superior to hybridoma-based antibodies.
Infusing our unique expertise
Recombinants are the result of combining genetic material from different immunized animals, and using display technologies to screen in-house antibody libraries for the best antibodies. Additional analyses on existing hybridoma-based antibodies can also give rise to sequences contributing to novel recombinants.
Maximizing value for your research
By further re-engineering these antibody sequences, we can precisely control their properties to achieve the following benefits:
reduce undesirable binding to Fc gamma receptors,
- eliminate destabilizing amino acid motifs,
- increase specific bonding affinity for stronger, more accurate targeting, and
- optimize fluorochrome conjugation for brighter and clearer signals.
In a final step, by synthesizing and cloning the resulting gene sequence, we achieve an expression vector that develops a cell line, which in turn produces a special recombinant antibody.
Better science with quality antibodies
Already in 2015, 100 of the world’s leading scientists collectively called for better standards and reproducibility in antibody production, proposing recombinant antibodies to circumvent variability (Baker, M. Reproducibility crisis: Blame it on the antibodies. Nature 521, 274–276 (2015). https://doi.org/10.1038/521274a). Moreover, by applying reverse engineering, which is encouraged by the EU Directive 2016/943 r, Miltenyi Biotec acts “[i]n the interest of innovation and fostering competition…” (§16).
Overview
Clone REA362 recognizes the human and mouse c-Cbl antigen phosphorylated at tyrosine 700 (pY700). The multifunctional adaptor Cbl acts as a negative regulator of intracellular signaling induced by engagement of cell-surface receptors. The RING finger domain of Cbl has E3 ubiquitin ligase activity that catalyses ubiquitilation and targeting of critical signaling molecules to lysosomal or proteosomal degradation. Moreover, Cbl regulates endocytosis of receptor tyrosine kinase and activity of other signaling proteins through a proteolysis-independent mechanism. c-Cbl unlike the other Cbl proteins contains only a short proline-rich region and no C-terminal leucine zipper-like region. The c-Cbl adapter protein is expressed in the cytoplasm in all tissues, with especially high levels of expression in hematopoietic cells.
Additional information: Clone REA362 displays negligible binding to Fc receptors.
