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 REA1195 recognizes the human CD112 antigen, a Single-pass type I membrane protein which is also known as Nectin-2, Herpesvirus entry mediator B (HveB) or Poliovirus receptor-related protein 2 (PRR2). Nectins are Ca2+-independent cell adhesion molecules that consist of 4 members: CD111 (Nectin-1), CD112 (Nectin-2), CD113 (Nectin-3), and Nectin-4. CD112 is one of the plasma membrane components of adherens junctions and is widely expressed in human tissues, including hematopoietic cells. It is also over-expressed in various cancers, e.g. breast and ovarian cancers. It has been reported to regulate cell adhesion between epithelial cells through the formation of trans-dimers between adjacent cells. CD112-mediated cell adhesion induces the formation of E-cadherin-based adherens junctions followed by the formation of claudin-based tight junctions. In addition to its function as a cell adhesion molecule, previous studies have suggested that CD112 acts as an organizer of Sertoli cell-spermatid junctions in the testis and of synapse formation by neurons and as an entry receptor for viruses. CD112 is also known to be one of the ligands of CD226 (DNAM-1) and TIGIT.
Additional information: Clone REA1195 displays negligible binding to Fc receptors.
