| Application | Recommended Dilution |
|---|---|
| WB | 1:500-1:2000 |
F2RL1, commonly known as Proteinase-activated receptor 2 (PAR-2), is a G-protein coupled receptor that plays a central role in inflammatory signaling, pain perception, and tissue remodeling. Unlike classical receptors activated by soluble ligands, PAR-2 undergoes proteolytic cleavage by serine proteases including trypsin and mast cell tryptase, exposing a tethered ligand that triggers receptor activation. This unique activation mechanism positions PAR-2 as a critical mediator linking protease activity to cellular responses in contexts ranging from gastrointestinal inflammation to tumor microenvironment dynamics.
This recombinant rabbit monoclonal antibody, clone 3E12, offers the consistency and reproducibility that demanding research applications require. Generated against a synthetic peptide derived from human F2RL1, the recombinant production method ensures sequence-defined specificity and eliminates the lot-to-lot variability that can compromise longitudinal studies or multi-site collaborations.
Western blot validation demonstrates reliable detection across multiple human cell lines, including A431, HepG2, HEK293, and MCF-7 whole cell lysates at dilutions of 1:500 to 1:2000. The observed molecular weight of approximately 55 kDa exceeds the predicted 44 kDa, a difference attributable to the extensive N-linked glycosylation characteristic of this receptor, which is essential for proper membrane trafficking and function. This antibody is also validated for ELISA applications, providing flexibility for researchers employing multiple detection strategies.
Whether investigating PAR-2 signaling in inflammatory disease models, examining receptor expression in cancer cell biology, or exploring protease-receptor interactions in epithelial systems, this antibody delivers the performance and consistency needed for meaningful experimental outcomes.
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