| Code | CSB-RA998339A0HU |
| Size | US$210 |
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| Application | Recommended Dilution |
|---|---|
| WB | 1:500-1:2000 |
| IHC | 1:50-1:200 |
| IF | 1:50-1:200 |
| FC | 1:50-1:200 |
Alkaline phosphatase, tissue-nonspecific isozyme (ALPL) serves as a critical enzyme in mineralization processes and phosphate metabolism, playing essential roles in bone development, liver function, and kidney physiology. As a widely studied biomarker, ALPL expression patterns provide valuable insights into osteoblast differentiation, metabolic bone disorders, and various pathological conditions including certain cancers.
This recombinant monoclonal antibody, clone 16F4, offers researchers the reproducibility and consistency that only sequence-defined antibody production can provide. Generated against a synthetic peptide derived from human ALPL, the rabbit host system yields high-specificity IgG that delivers reliable results across experimental replicates, eliminating the lot-to-lot variability that can compromise longitudinal studies.
Extensive validation demonstrates this antibody's versatility across multiple experimental platforms. Western blot analysis confirms robust detection in human cell lines including LO2, HEK293, HeLa, and HepG2, as well as mouse kidney, rat kidney, and mouse liver tissue lysates, supporting cross-species reactivity with human, mouse, and rat samples. The observed band at 75 kDa, higher than the predicted 57 kDa molecular weight, reflects the extensive glycosylation characteristic of this membrane-anchored ectoenzyme. Immunohistochemistry validation in human endometrial carcinoma and adrenal gland tissues demonstrates clear tissue staining, while immunofluorescence studies in HepG2 cells and flow cytometry analysis in HeLa cells confirm utility for cellular localization and quantitative expression studies.
Whether investigating skeletal mineralization, characterizing stem cell differentiation toward osteogenic lineages, or exploring ALPL dysregulation in disease contexts, this antibody provides the experimental flexibility and cross-species reactivity essential for translational research workflows.
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