| Application | Recommended Dilution |
|---|---|
| FC | 1:50-1:200 |
Vitamin D-binding protein, encoded by the GC gene, serves as the principal plasma carrier for vitamin D metabolites and plays essential roles in actin scavenging, macrophage activation, and inflammatory responses. Beyond its well-characterized function in vitamin D transport, this multifunctional glycoprotein has emerged as a significant biomarker in liver disease, sepsis, and various inflammatory conditions, making it a valuable target for researchers investigating metabolic regulation and immune function.
This recombinant rabbit monoclonal antibody, clone 7C3, offers the reproducibility and consistency that demanding research applications require. Generated against a synthetic peptide derived from human GC protein, the recombinant production method ensures sequence-defined specificity and eliminates the lot-to-lot variability that can compromise longitudinal studies. Affinity chromatography purification delivers a high-purity reagent suitable for quantitative applications.
Validation studies demonstrate robust performance in flow cytometry applications using HepG2 cells, a hepatocyte-derived line that naturally expresses GC protein given the liver's role as the primary source of circulating vitamin D-binding protein. The flow cytometry protocol employed fixation and permeabilization to detect intracellular protein, with clear separation between specific staining and isotype control, confirming reliable detection at dilutions ranging from 1:50 to 1:200. The antibody is also validated for ELISA, providing flexibility across different experimental workflows.
Supplied in a glycerol-containing buffer optimized for long-term stability at -20°C or -80°C, this unconjugated format allows researchers to select secondary detection systems appropriate for their specific instrumentation. This antibody supports investigations into vitamin D metabolism, acute phase responses, and the emerging connections between GC protein variants and disease susceptibility.
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