Product Description
Size: 100µg
Recombinant kgp protein (Tagged) is a Porphyromonas gingivalis ATCC 33277 Fragment protein, in the 229 to 594 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, Mass Spec.
Key facts
Purity:>90% SDS-PAGE,
Expression system:Escherichia coli,
Tags:His tag N-Terminus,
Applications:Mass Spec, SDS-PAGESee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:No,
Accession:B2RLK2,
Animal free:No,
Carrier free:No,
Species:Porphyromonas gingivalis ATCC 33277,
Storage buffer:pH: 7.2 - 7.4Constituents: Tris buffer, 50% Glycerol (glycerin, glycerine)
Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage conditions--20°C, Appropriate long-term storage conditions--20°C, Storage information-Avoid freeze / thaw cycle
Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Kgp also known as lysine gingipain is a bacterially derived cysteine protease. This enzyme has an approximate mass of 50 kDa and exhibits its activity primarily in the bacterium Porphyromonas gingivalis. Kgp is found mainly in the outer membrane vesicles and is secreted in the extracellular environment of this bacterium. It is characterized by its specificity for peptide bonds at lysine residues which differentiates it from its counterpart arginine gingipain.
Biological function summary
Lysine gingipain contributes to the pathogenicity of Porphyromonas gingivalis by degrading host proteins and evading immune responses. It is an important component of the protein complex associated with the bacterium's ability to colonize and persist in the host's tissues. Kgp activity modulates interactions with the host facilitating bacterial adherence and invasion into tissues. Consequently it plays a significant role in the bacterium's capability to sustain infection and cause damage to the host's immune system.
Pathways
The involvement of lysine gingipain is important in pathways related to inflammatory response and immune evasion. The enzyme interacts with complement proteins and influences the kallikrein-kinin system. Additionally it relates functionally with proteins like gingipain R both involved in processing extracellular matrix components which furthers the pathogenic mechanisms of Porphyromonas gingivalis. This protease's activity influences critical host-pathogen interactions that drive inflammation and tissue destruction.
Lysine gingipain connects strongly with periodontitis and cardiovascular disease. Its enzymatic actions lead to the degradation of periodontal structures in periodontitis. Kgp can enter the bloodstream where it may modulate the immune system potentially affecting cardiovascular health. The protease interacts with proteins involved in these diseases such as gingipain R boosting inflammatory damage and contributing to systemic manifestations beyond oral health.
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Collaboration
Tony Tang
Email: Tony.Tang@iright.com
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