| Application | Recommended Dilution |
|---|---|
| WB | 1:1000-1:5000 |
| IHC | 1:20-1:200 |
| IF | 1:20-1:200 |
| FC | 1:20-1:200 |
Glyceraldehyde-3-phosphate dehydrogenase, commonly known as GAPDH, serves as one of the most widely used loading controls in protein research due to its consistent, high-level expression across virtually all cell types. Beyond its classical role in glycolysis, GAPDH participates in diverse cellular processes including apoptosis, DNA repair, and membrane trafficking, making it relevant to studies spanning metabolism, cancer biology, neuroscience, and signal transduction.
This recombinant monoclonal antibody, clone 9B1, offers the reproducibility that demanding quantitative experiments require. Because recombinant antibodies are produced from defined genetic sequences rather than traditional hybridoma methods, researchers can expect consistent performance across lots, eliminating the variability that can compromise longitudinal studies or multi-site collaborations. The rabbit IgG format provides strong signal amplification while maintaining specificity against human GAPDH.
Validation across multiple experimental platforms demonstrates this antibody's versatility in the laboratory. Western blot analysis confirms reliable detection of the expected 36 kDa band in HepG2 hepatocellular carcinoma cells, U87 glioblastoma cells, and Jurkat lymphocytes, with recommended dilutions ranging from 1:500 to 1:2000. For tissue-based studies, immunohistochemistry has been validated in paraffin-embedded human placenta sections using standard citrate buffer antigen retrieval. Immunofluorescence microscopy in HepG2 cells reveals cytoplasmic localization patterns consistent with GAPDH's known distribution, while flow cytometry analysis in HeLa cells enables quantitative single-cell assessments.
The affinity-purified antibody arrives in a glycerol-based buffer optimized for long-term storage at -20°C or -80°C. Whether normalizing protein loading, validating sample integrity, or investigating GAPDH's emerging non-glycolytic functions, this antibody provides the consistency researchers need for publication-quality results.
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