Recombinant Human C11orf72 Protein，His

C9orf72 gene, located on chromosome 9, is the most common genetic cause of frontotemporal dementia (FTD) and amyotrophic lateral sclerosis (ALS). The disease is associated with an expanded hexanucleotide repeat (GGGGCC) in the non-coding region of the gene, leading to the production of toxic dipeptide repeat proteins (DPRs) through a process called repeat-associated non-AUG (RAN) translation. These DPRs, which include poly-Glycine (Gly), poly-Arginine (Arg), and poly-Proline (Pro), accumulate in neuronal and glial cells, contributing to cellular dysfunction and neurodegeneration. Research has shown that these proteins can disrupt various cellular functions, including nucleocytoplasmic transport, RNA metabolism, and mitochondrial integrity. Moreover, the presence of DPRs has been linked to pathological features such as the formation of intracellular aggregates and impairment of autophagy. Understanding the mechanisms by which C9orf72-derived proteins lead to neurodegeneration is crucial for developing targeted therapeutic strategies. Studies continue to explore the pathophysiological roles of these proteins, with a focus on their toxic effects and potential interventions that could mitigate their impact on neuron health and function. Investigating the interactions between DPRs and cellular pathways may reveal new insights into the underlying mechanisms of FTD and ALS, ultimately guiding the development of effective treatments for these debilitating diseases.