Anti-TRIM11 / Tripartite motif-containing protein 11

Adding 0.2 ml of distilled water will yield a concentration of 500 ug/ml. TRIM11 antibody recognizes Tripartite motif-containing protein 11, an E3 ubiquitin-protein ligase that plays a central role in protein quality control, neuronal regulation, and innate immunity. TRIM11 belongs to the TRIM family of proteins, which share a conserved architecture comprising a RING finger domain, one or two B-box motifs, and a coiled-coil region. This configuration enables TRIM11 to act as a multifunctional scaffold for substrate recognition and ubiquitin transfer. The TRIM11 antibody is extensively used in molecular and cellular biology research to study ubiquitination, neurodegeneration, and cancer signaling networks that depend on proteostasis and regulated protein degradation.Encoded by the TRIM11 gene located on human chromosome 1q42.13, the protein is composed of approximately 465 amino acids and localizes predominantly to the cytoplasm, although nuclear accumulation occurs under specific stress conditions. Functionally, TRIM11 mediates the ubiquitination and degradation of misfolded or aggregated proteins, thereby maintaining neuronal homeostasis. It directly interacts with substrates such as Humanin, a neuroprotective peptide, and acts as a negative regulator of stress-induced signaling. Through its ubiquitin ligase activity, TRIM11 contributes to proteasome-mediated clearance of abnormal proteins, preventing cytotoxic accumulation observed in neurodegenerative diseases like Alzheimer's and Parkinson's.The TRIM11 antibody is also valuable for studying tumorigenesis, as elevated TRIM11 expression has been reported in glioma, breast, and colorectal cancers. It promotes cell proliferation and migration by targeting tumor suppressors for degradation and by activating signaling pathways such as PI3K/AKT and ERK/MAPK. Additionally, TRIM11 can suppress interferon-stimulated gene expression, indicating a regulatory role in antiviral immunity. Western blot analyses using this antibody typically reveal a band near 52-55 kDa, corresponding to the full-length protein. Immunofluorescence assays show diffuse cytoplasmic localization with punctate distribution, consistent with its role in protein turnover and ubiquitin signaling.At the molecular level, TRIM11 associates with proteasomal subunits and chaperone complexes, enhancing clearance of misfolded proteins generated during oxidative stress or viral infection. Knockdown studies reveal increased accumulation of aggregation-prone proteins and elevated sensitivity to stress-induced apoptosis, demonstrating TRIM11's role as a cellular quality control factor. The protein also regulates transcriptional activity by modulating the degradation of transcriptional co-repressors and signaling intermediates. NSJ Bioreagents provides a validated TRIM11 antibody optimized for western blot, immunocytochemistry, and immunoprecipitation, offering researchers a reliable tool to investigate ubiquitin signaling, neuronal protection, and oncogenic pathways linked to TRIM11.