| Code | CSB-RA909932A0HU |
| Size | US$210 |
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| Application | Recommended Dilution |
|---|---|
| WB | 1:500-1:5000 |
| IHC | 1:50-1:200 |
FDFT1, also known as squalene synthase, catalyzes the first committed step in cholesterol biosynthesis by converting two molecules of farnesyl pyrophosphate into squalene. This enzymatic checkpoint positions FDFT1 as a critical regulator of sterol metabolism, making it a compelling target for researchers investigating metabolic disorders, cardiovascular disease, and cancer biology, where altered cholesterol synthesis often supports rapid cell proliferation.
This recombinant monoclonal antibody, generated in rabbit against a synthetic peptide derived from human FDFT1, offers the reproducibility and consistency that demanding experimental workflows require. Because the antibody sequence is defined and production is cell-based, you can expect uniform performance across lots, eliminating the variability that can complicate long-term studies or multi-site collaborations.
Validation data demonstrates reliable detection across multiple platforms. In Western blot applications, the antibody identifies FDFT1 in THP-1 and K562 whole cell lysates at dilutions ranging from 1:500 to 1:5000, producing a clear band at approximately 50 kDa. The slight difference from the predicted molecular weights likely reflects post-translational modifications or the detection of a predominant isoform. For immunohistochemistry, the antibody has been validated in paraffin-embedded human testis and human lung cancer tissue at 1:50 to 1:200 dilutions using citrate buffer antigen retrieval, showing specific staining patterns suitable for tissue-based studies.
Whether you are exploring cholesterol pathway dysregulation in tumor microenvironments, investigating metabolic reprogramming in hematological cell models, or examining FDFT1 expression in cardiovascular or neurological contexts, this antibody provides a dependable tool for both protein quantification and spatial localization studies.
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