Anti-DHX33 antibody [EPR14093] - BSA and Azide free

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

DEAD-Box Helicase 33 (DHX33) is an important enzyme involved in unwinding RNA. Often known as DDX33 its molecular mass is approximately 81 kDa. DHX33 functions as an ATP-dependent RNA helicase actively participating in the processing of ribosomal RNA (rRNA) during ribosome biogenesis. The expression of DHX33 is found largely in tissue where cell growth is high such as embryonic and cancerous cells. By altering the secondary structure of RNA DHX33 plays a direct role in the modification and maturation of rRNA.

Biological function summary

DHX33 plays a role in cellular processes that involve RNA metabolism. It forms part of a larger ribonucleoprotein complex taking an active role in ribosome assembly. This complex promotes the synthesis of ribosomes which are vital for protein synthesis in cells. Proper functioning of DHX33 is important for maintaining the balance of cell proliferation and differentiation largely due to its involvement in the production and processing of rRNA. DHX33's activity is essential for effective ribosome function which impacts cellular function and growth.

Pathways

DHX33 integrates into the ribosome biogenesis and p53 signaling pathways. Within these it interacts with proteins such as nucleophosmin (NPM1) and nucleolin which are influential in nucleolar structure and function. In the p53 pathway DHX33 influences the cellular stress response by affecting the regulation of the tumor suppressor protein p53. By acting within these pathways DHX33 affects protein synthesis and cell cycle progression linking it to cellular homeostasis and stress response.

Associated diseases and disorders

DHX33 has associations with cancer and ribosomopathies. Overexpression or mutations of DHX33 can link it to tumorigenesis given its role in uncontrolled cell growth and proliferation. In ribosomopathies alterations in DHX33 function can result in defective ribosome biogenesis impacting cell division and growth. The disruption of DHX33's interaction with NPM1 in particular is observed in several forms of cancer highlighting its potential as a target for cancer therapy.