Anti-Mouse CD96 – Purified in vivo PLATINUM™ Functional Grade

This monoclonal antibody is aseptically packaged and formulated in 0.01 M phosphate buffered saline (150 mM NaCl) PBS pH 7.2 - 7.4 with no carrier protein, potassium, calcium or preservatives added. Due to inherent biochemical properties of antibodies, certain products may be prone to precipitation over time. Precipitation may be removed by aseptic centrifugation and/or filtration.

Functional grade preclinical antibodies are manufactured in an animal free facility using in vitro cell culture techniques and are purified by a multi-step process including the use of protein A or G to assure extremely low levels of endotoxins, leachable protein A or aggregates.

To protect mouse colonies from infection by pathogens and to assure that experimental preclinical data is not affected by such pathogens, all of Leinco’s Purified Functional PLATINUM™ antibodies are tested and guaranteed to be negative for all pathogens in the IDEXX IMPACT I Mouse Profile.

Functional grade preclinical antibodies may be stored sterile as received at 2-8°C for up to one month. For longer term storage, aseptically aliquot in working volumes without diluting and store at -80°C. Avoid Repeated Freeze Thaw Cycles.

Next Day 2-8°C

Clone 3.3 recognizes an epitope on mouse CD96.

CD96 is a single pass type I transmembrane glycoprotein in the immunoglobulin superfamily that is heavily N-glycosylated¹. Murine (m) CD96 is present at the surface of most lymphocytes, including NK, CD4⁺ T, CD8⁺ T, NKT, and γδ T cells, but not B lymphocytes, neutrophils, macrophages, or dendritic cells². mCD96 interacts with mCD155 and nectin-1 (CD111)¹. A V-like domain mediates binding of mCD96 to mCD155 via interaction between amino acids of the FG loop of one binding partner with residues in the C’C’’-loop of the other. CD96 is a member of an interaction network that includes adhesion, activation, and inhibition activities.

CD96 contains three Ig-like domains that are separated from the transmembrane domain by a long proline, serine, and threonine rich stalk that undergoes extensive O-linked glycomodification¹. The stalk may play a role in orientation or presentation of the Ig-like domains. mAb 3.3 binds to the first Ig domain and competes with CD155 for binding³.

Human CD96 has a mild boosting effect on 2B4- and NKp30-mediated killing, but a direct role in the activation of NK cell-mediated cytotoxicity in vitro has not been observed 1. In contrast, mCD96 suppresses NK cells in vivo². Blocking studies show that mCD96 competes with CD226 for CD155 binding and limits NK cell function by direct inhibition². Additionally, blocking mCD96 in vivo with mAb 3.3 protects against metastasis in three different tumor models. The antimetastatic effect of mAb 3.3 is independent of antibody-dependent cell-mediated cytotoxicity and activating Fc receptors^3,4 and is enhanced by anti-PD-1 and anti-CTLA-4 mAbs⁴. Suppression of metastasis by mAb 3.3 is dependent on NK cells, CD226 (DNAM-1), and IFN-γ⁴. Additionally, mAb 3.3 loses its antimetastatic function in CD155- and IL-12p35-deficient mice³.