| Code | CSB-RA986192A0HU |
| Size | US$210 |
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| Application | Recommended Dilution |
|---|---|
| WB | 1:500-1:2000 |
| IF | 1:50-1:200 |
| FC | 1:50-1:200 |
AGR2, or Anterior Gradient 2, is a protein disulfide isomerase family member that plays a critical role in protein folding and secretion within the endoplasmic reticulum. This protein has garnered significant research attention due to its elevated expression in various adenocarcinomas and its involvement in cancer cell survival, metastasis, and therapeutic resistance. Understanding AGR2 biology is particularly relevant for researchers investigating tumor progression, ER stress responses, and potential diagnostic or therapeutic targets in oncology.
This recombinant monoclonal antibody against human AGR2 offers the consistency and reliability that demanding experimental workflows require. Produced using recombinant technology with a defined sequence, clone 9H3 eliminates the lot-to-lot variability that can compromise longitudinal studies and reproducibility. The rabbit IgG format, purified by affinity chromatography, ensures high specificity for your target.
Validation across multiple platforms demonstrates this antibody's experimental versatility. Western blot analysis successfully detects AGR2 in COLO205 colorectal carcinoma, MCF-7 breast cancer, and A549 lung adenocarcinoma cell lysates at dilutions ranging from 1:500 to 1:2000.The observed ~17 kDa band is likely due to the cleavage of the signal peptide, potential proteolytic processing, or inherent SDS-PAGE migration discrepancies causing a downward shift from the predicted 20 kDa. Immunofluorescence staining in THP-1 cells reveals clear cellular localization, while flow cytometry analysis in A549 cells shows distinct positive population shifts compared to isotype controls.
Whether you are characterizing AGR2 expression patterns across cancer cell lines, investigating its role in ER homeostasis, or validating it as a biomarker candidate, this antibody provides the multi-application flexibility and recombinant consistency essential for rigorous research.
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