| Application | Recommended Dilution |
|---|---|
| WB | 1:500-1:5000 |
| IHC | 1:50-1:200 |
ULK1, also known as Unc-51-like kinase 1, serves as a master regulator of autophagy initiation in mammalian cells. As the human homolog of yeast ATG1, this serine/threonine kinase integrates nutrient and energy signals to control the formation of autophagosomes, making it a critical node in cellular stress responses, metabolic adaptation, and quality control mechanisms. Dysregulation of ULK1-mediated autophagy has been implicated in cancer progression, neurodegenerative diseases, and metabolic disorders, positioning this kinase as an important target for researchers investigating these pathways.
This recombinant monoclonal antibody, generated against a synthetic peptide derived from human ULK1, offers the reproducibility and consistency that demanding experimental workflows require. Because the antibody sequence is defined and production occurs in controlled recombinant systems, you can expect reliable performance across experiments and between lots, eliminating a common source of variability in long-term studies.
Validation data demonstrates robust detection of ULK1 in Western blot applications across multiple human cell lines, including A549, HEK293, Jurkat, and MCF-7 lysates at 1:1000 dilution. The observed band at approximately 130 kDa runs slightly higher than the predicted 113 kDa molecular weight, a shift commonly attributed to post-translational modifications such as phosphorylation, which is particularly relevant given ULK1's role as an actively regulated kinase. For tissue-based studies, immunohistochemistry validation confirms effective staining in paraffin-embedded human skeletal muscle and colorectal cancer specimens at 1:100 dilution using citrate buffer antigen retrieval.
This antibody supports researchers investigating autophagy regulation, signal transduction pathways, and the metabolic reprogramming that characterizes both normal physiology and disease states.
Email: support@cusabio.com
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