| Code | CSB-RA547153A0HU |
| 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 |
EHD1 (EH domain-containing protein 1) plays a central role in endocytic recycling, regulating the transport of internalized membrane proteins back to the cell surface. This function makes EHD1 essential for maintaining receptor homeostasis and has implicated it in diverse cellular processes including cell migration, cytokinesis, and ciliary function. Dysregulation of EHD1 has been associated with cancer progression and metastasis, positioning it as a meaningful target for researchers investigating membrane trafficking dynamics and disease mechanisms.
This recombinant monoclonal antibody, generated from clone 13D3 in rabbit host, offers the reproducibility that demanding experimental workflows require. Because the antibody sequence is defined and production occurs through recombinant expression, researchers benefit from consistent performance across lots—eliminating the variability that can complicate long-term studies or multi-site collaborations. Affinity chromatography purification ensures high specificity for your target.
Validation data demonstrates robust performance across multiple applications. Western blot analysis detects a clean band at the predicted 61 kDa molecular weight across human cell lines including SW620, A-431, A549, and HeLa, with cross-species reactivity confirmed in mouse samples including NIH/3T3 cells and brain tissue lysate. Immunohistochemistry staining has been validated in paraffin-embedded human cervical cancer tissue, revealing clear target localization. Flow cytometry analysis in PC-3 cells shows distinct positive signal separation from isotype control, enabling quantitative assessment of EHD1 expression at the single-cell level.
Whether investigating endosomal trafficking pathways, exploring EHD1's role in tumor biology, or characterizing membrane dynamics in cellular models, this antibody provides the validated, consistent performance needed for publication-quality results.
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