Anti-Human FXYD5 Recombinant Antibody (M53) (CAT#: TAB-261MZ)

Juurikka, K., et al. "MMP8 increases tongue carcinoma cell-cell adhesion and diminishes migration via cleavage of anti-adhesive FXYD5." Oncogenesis 10.5 (2021): 44. https://doi.org/10.1038/s41389-021-00334-x

This research investigates the role of matrix metalloproteinase-8 (MMP8) in oral tongue squamous cell carcinoma (OTSCC), identifying a novel tumor-protective mechanism. The study demonstrates that MMP8 increases cell-cell adhesion and decreases cancer cell migration through the cleavage of FXYD domain-containing ion transport regulator 5 (FXYD5), an anti-adhesive glycoprotein. Using terminal amine isotopic labeling of substrates (TAILS) coupled with liquid chromatography and tandem mass spectrometry, researchers identified 36 potential substrates of MMP8, with FXYD5 being particularly significant. The cleavage of FXYD5 by MMP8 was confirmed through in vitro assays, and silencing FXYD5 increased cell-cell adhesion and diminished cell motility, similar to the effects of MMP8 overexpression.
Creative Biolabs provided a therapeutic antibody against FXYD5 (M53) that played a critical role in this research, enabling the investigators to target and study this anti-adhesive glycoprotein. As the study revealed FXYD5 as a marker of worse prognosis in OTSCC and other cancers, this antibody represents a promising therapeutic tool for further investigation. The researchers specifically highlighted the potential of the M53 antibody from Creative Biolabs as a candidate for future studies aimed at developing therapeutic approaches targeting FXYD5 in tongue cancer and potentially other cancer types where FXYD5 plays a similar role in promoting tumor progression.