| Code | CSB-RA444398A0HU |
| Size | US$210 |
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| Application | Recommended Dilution |
|---|---|
| WB | 1:500-1:2000 |
| FC | 1:50-1:200 |
CUL1 serves as the essential scaffold protein within SCF (Skp1-Cullin-F-box) E3 ubiquitin ligase complexes, orchestrating the ubiquitination and subsequent proteasomal degradation of numerous regulatory proteins. This central role in controlling cell cycle progression, signal transduction, and transcriptional regulation makes CUL1 a critical target for researchers investigating cancer biology, cell proliferation mechanisms, and protein homeostasis pathways.
This recombinant monoclonal antibody, generated against a synthetic peptide derived from human CUL1, offers the reproducibility and consistency that demanding experimental workflows require. As a sequence-defined recombinant clone, it eliminates the lot-to-lot variability inherent in traditional hybridoma-derived antibodies, ensuring your results remain comparable across extended studies and collaborative projects.
Validation data demonstrates reliable performance across multiple experimental platforms. Western blot analysis confirms specific detection at the expected 90 kDa molecular weight in human K562 and Jurkat cell lysates, as well as mouse NIH/3T3 cells, supporting cross-species reactivity between human and mouse samples. The antibody performs effectively at dilutions ranging from 1:500 to 1:2000 for immunoblotting applications. Flow cytometry validation in HeLa cells shows clear separation between specific staining and isotype control populations, with optimal results achieved at 1:50 to 1:200 dilutions following fixation and permeabilization.
The unconjugated format provides flexibility for pairing with your preferred secondary detection systems, while the glycerol-stabilized formulation supports long-term storage stability. Whether you are investigating SCF complex assembly, characterizing ubiquitin-proteasome pathway dynamics, or exploring CUL1's emerging roles in tumorigenesis, this antibody delivers the specificity and consistency your research demands.
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