| Code | CSB-RA090772A0HU |
| Size | US$210 |
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| Application | Recommended Dilution |
|---|---|
| WB | 1:500-1:2000 |
| IHC | 1:50-1:200 |
| FC | 1:50-1:200 |
PUM1 (Pumilio homolog 1) is an RNA-binding protein that plays a central role in post-transcriptional gene regulation, controlling mRNA stability and translation through sequence-specific interactions with target transcripts. As a key regulator of stem cell maintenance, neuronal function, and cell cycle progression, PUM1 has emerged as an important research target in developmental biology, neuroscience, and cancer studies where dysregulated RNA metabolism contributes to disease pathology.
This recombinant monoclonal antibody, generated against a synthetic peptide derived from human PUM1, offers the reproducibility and consistency that demanding experimental workflows require. Because the antibody sequence is defined and production occurs in a controlled recombinant system, researchers can expect reliable performance across experiments and between lots, eliminating the variability often encountered with traditional hybridoma-derived antibodies.
Validation studies demonstrate robust performance across multiple applications. In western blot analysis, the antibody detects PUM1 in HEK293 and COLO-205 whole cell lysates at dilutions of 1:500–1:2000, producing a band at approximately 140 kDa. The observed molecular weight exceeds the predicted 126 kDa, which is consistent with post-translational modifications such as glycosylation commonly observed with this protein. Immunohistochemistry studies confirm specific staining in paraffin-embedded human colorectal cancer tissue, while flow cytometry analysis in HeLa cells shows clear separation from isotype controls, demonstrating utility for intracellular protein detection in fixed and permeabilized samples.
This antibody serves researchers investigating RNA-protein interactions, translational control mechanisms, and PUM1's contributions to oncogenesis and neurological disorders, providing a dependable tool for characterizing this multifunctional regulatory protein across complementary experimental platforms.
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