Anti-SARS-CoV-2 (COVID-19) 3CLpro (nsp5) antibody [HL1367] - BSA and Azide free

Supplementary info

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

Activity summary

The SARS-CoV-2 3CLpro also known as 3C-like protease or nsp5 is a protease enzyme with a critical role in the viral life cycle. It has an estimated mass of about 33.8 kDa. It performs its function primarily in the cytoplasm of the host cell. This protease cleaves the viral polyprotein at specific sites to generate functional proteins necessary for the viral replication and transcription process. It consists of a catalytic dyad made up of cysteine and histidine which aids in the hydrolysis of peptide bonds.

Biological function summary

The 3CLpro ensures the maturation of non-structural proteins necessary for SARS-CoV-2 replication. It is part of a larger polyprotein complex that the virus produces upon infection. The 3CLpro processes this polyprotein to release various functional viral proteins that aid in RNA synthesis and modification. It is a target for antiviral drug development due to its importance in viral propagation and lack of homologous human proteases reducing the likelihood of off-target effects.

Pathways

The function of 3CLpro is integral in the viral replication pathway of SARS-CoV-2. Within this pathway it interacts with viral RNA-dependent RNA polymerase essential for transcribing and replicating the viral genome. Another significant connection occurs with non-structural protein 8 (nsp8) where 3CLpro aids by cleaving the polyprotein to release the mature form of this accessory protein facilitating RNA replication.

Associated diseases and disorders

SARS-CoV-2 3CLpro's function targets COVID-19 caused by the novel coronavirus. Its proteolytic activity is directly linked to the pathogenesis of COVID-19 as it enables viral replication within host cells. In this context 3CLpro is associated with other viral proteins such as nsp12 the main RNA polymerase critical for the replication process thereby representing a potential therapeutic target to disrupt viral life cycle and mitigate disease progression.