Single-stranded DNA-binding serine protease that mediates the proteolytic cleavage of covalent DNA-protein cross-links during DNA synthesis, thereby playing a key role in maintaining genomic integrity . DPCs are highly toxic DNA lesions that interfere with essential chromatin transactions, such as replication and transcription, and which are induced by reactive agents, such as UV light or formaldehyde . Protects replication fork from stalling by removing DPCs, such as covalently trapped topoisomerase 1 adducts on DNA lesion, or poly polymerase 1 -DNA complexes trapped by PARP inhibitors . Required for PCNA loading on replication sites . Promotes S-phase entry and DNA synthesis . Also acts as a restriction factor for some viruses including SV40 polyomavirus and vaccinia virus . Mechanistically, affects nuclear barrier function during viral replication by mediating the disruption of the nuclear pore complex via its protease activity . In turn, interacts with vaccinia virus DNA-binding protein OPG079 in the cytoplasm and promotes its degradation without the need of its protease activity but through autophagy .

Serine protease FAM111A (EC 3.4.21.-)

q96pz2

Human

WB,IF,ICC

WB 1:1000-1:5000
IF 1:100
ICC 1:100

~71 kD

Rabbit

50mM Tris-Glycine(pH 7.4), 0.15M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.

Store at -20°C. Stable for 12 months from date of receipt.