InVivoMAb anti-human MUC16

Clone Catalog # Category
VK8 BE0391
USD 164 - USD 4280

About InVivoMAb anti-human MUC16

The VK8 monoclonal antibody reacts with human MUC16 also known as CA125. MUC16 is a large transmembrane glycoprotein primarily expressed on the surface of epithelial cells in various tissues. MUC16 is known for its clinical significance as a tumor marker for ovarian cancer. MUC16 has also been shown to play a role in cell adhesion, immune regulation, and protection of the ocular surface. Due to its complex structure and diverse functions, MUC16 is an area of ongoing research in both cancer biology and immunology.

InVivoMAb anti-human MUC16 Specifications

IsotypeMouse IgG1, κ
ImmunogenHuman ovarian cancer cell line OVCAR-3
Reported ApplicationsFlow cytometry Western blot
FormulationPBS, pH 7.0 Contains no stabilizers or preservatives
Endotoxin<2EU/mg (<0.002EU/μg) Determined by LAL gel clotting assay
Purity>95% Determined by SDS-PAGE
Sterility0.2 μm filtration
PurificationProtein G
Molecular Weight150 kDa
StorageThe antibody solution should be stored at the stock concentration at 4°C. Do not freeze.

Application References

InVivoMAb anti-human MUC16 (CLONE: VK8)

Felder M, Kapur A, Rakhmilevich AL, Qu X, Sondel PM, Gillies SD, Connor J, Patankar MS (2019). "MUC16 suppresses human and murine innate immune responses" Gynecol Oncol 152(3):618-628. PubMed

MUC16, the mucin that contains the CA125 epitopes, suppresses the cytolytic responses of human NK cells and inhibits the efficacy of therapeutic antibodies. Here, we provide further evidence of the regulatory role of MUC16 on human and murine NK cells and macrophages.

Gubbels JA, Belisle J, Onda M, Rancourt C, Migneault M, Ho M, Bera TK, Connor J, Sathyanarayana BK, Lee B, Pastan I, Patankar MS (2006). "Mesothelin-MUC16 binding is a high affinity, N-glycan dependent interaction that facilitates peritoneal metastasis of ovarian tumors" Mol Cancer 5(1):50. PubMed

The mucin MUC16 and the glycosylphosphatidylinositol anchored glycoprotein mesothelin likely facilitate the peritoneal metastasis of ovarian tumors. The biochemical basis and the kinetics of the binding between these two glycoproteins are not clearly understood. Here we have addressed this deficit and provide further evidence supporting the role of the MUC16-mesothelin interaction in facilitating cell-cell binding under conditions that mimic the peritoneal environment.