MYC contains a basic helix-loop-helix (bHLH) domain. This protein is a multifunctional nuclear phosphoprotein, which plays a role in cell cycle process, apoptosis and cell transformation. As a transcription factor, it regulates the transcription of specific target genes. It seems to activate the transcription of growth-related genes. It binds to DNA in a nonspecific way, but also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. Mutation, overexpression, rearrangement and translocation of this gene are related to many hematopoietic tumors, leukemia and lymphoma (including Burkitt lymphoma). The antibody is a rabbit polyclonal antibody against human MYC recombinant protein. The 50kDa band recognized by antibody is the natural form of MYC, while other bands between 60 and 70 kDa are the phosphorylated form of MYC (PMID: 12189186). The latest research reveals a new key mechanism of MYC protein, which is independent of its classical transcriptional regulation function. It was found that under the stress of transcription, MYC was polymerized through its specific RNA binding domain (RBRIII), and exocrine was targeted at the nuclear R loop and double-stranded RNA. This process can effectively eliminate the immunogenic RNA-DNA hybrid from R-loop, thus preventing it from activating TLR3-TBK1 natural immune signaling pathway. This mechanism is very important for MYC to maintain tumor growth and achieve immune escape in vivo. (PMID: 41576951)