Y.Enterocolitica (O:9) YopE
Escherichia Coli.
Outer membrane virulence protein YopE, yopE, yop25.
Sterile Filtered clear solution.
Greater than 80.0% as determined by SDS-PAGE.
Description
Recombinant Yersinia Enterocolitica (O:9) YopE in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 24kDa.
Y.Enterocolitica (O:9) YopE is expressed with a -10x His tag at N-terminus and purified by proprietary chromatographic techniques.
Product Specs
Outer membrane virulence protein YopE, yopE, yop25.
Escherichia Coli.
Product Science Overview
Yersinia enterocolitica is a pathogenic bacterium responsible for causing yersiniosis, a zoonotic disease that affects both humans and animals. This bacterium is known for its diverse serotypes and biotypes, with O:9 being one of the significant serotypes. A key virulence factor of pathogenic Yersinia enterocolitica strains is the Yersinia outer protein E (YopE), which plays a crucial role in the bacterium’s ability to infect and survive within the host.
YopE is a part of the type III secretion system (T3SS), a sophisticated mechanism used by Yersinia enterocolitica to inject virulence proteins directly into the host cells. This system is encoded by a plasmid and is essential for the bacterium’s pathogenicity. YopE functions as a GTPase-activating protein (GAP), which targets and inactivates small Rho GTPases in the host cell. This action leads to the inhibition of actin polymerization, disrupting the host cell’s cytoskeleton and aiding in the bacterium’s evasion of the host’s immune response .
Recombinant YopE is produced using Escherichia coli (E. coli) as a host for expression. The recombinant protein is typically non-glycosylated and has a calculated molecular mass of approximately 24 kDa. It is often expressed with a His-tag at the N-terminus to facilitate purification through chromatographic techniques .
The recombinant YopE protein is supplied in a buffer solution containing HEPES, NaCl, and glycerol to ensure stability. It is crucial to store the protein at low temperatures, typically at -20°C or below, to maintain its integrity and avoid multiple freeze-thaw cycles .
Recombinant YopE is primarily used for laboratory research purposes. It is instrumental in studying the molecular mechanisms of Yersinia enterocolitica’s pathogenicity and the host-pathogen interactions. By understanding how YopE manipulates the host cell’s cytoskeleton, researchers can develop targeted therapies and preventive measures against yersiniosis.
Additionally, recombinant YopE can be used in immunological studies to investigate the immune response elicited by this virulence factor. It binds to IgG- and IgM-type human antibodies, making it a valuable tool for developing diagnostic assays and vaccines .
