Recombinant Porphyromonas gingivalis Lys-gingipain (kgp), partial
| Product Name | Recombinant Porphyromonas gingivalis Lys-gingipain (kgp), partial |
|---|---|
| Description | Cysteine proteinase with a strong preference for substrates with Lys in the P1 position. Hydrolyzes bovine hemoglobin, bovine serum albumin, casein, human placental type I collagen and human IgA and IgG. Disrupts the functions of polymorphonuclear leukocytes. May act as a virulence factor in the development of peridontal disease. Involved in the coaggregation of P.gingivalis with other oral bacteria. |
| Synonyms | Lysine-specific cysteine proteinase Kgp |
| Host | E.coli |
| Molecular Weight | 56.6 |
| Amino Acid Sequence | DVYTDHGDLYNTPVRMLVVAGAKFKEALKPWLTWKAQKGFYLDVHYTDEAEVGTTNASIKAFIHKKYNDGLAASAAPVFLALVGDTDVISGEKGKKTKKVTDLYYSAVDGDYFPEMYTFRMSASSPEELTNIIDKVLMYEKATMPDKSYLEKALLIAGADSYWNPKIGQQTIKYAVQYYYNQDHGYTDVYSYPKAPYTGCYSHLNTGVGFANYTAHGSETSWADPSLTATQVKALTNKDKYFLAIGNCCVTAQFDYPQPCFGEVMTRVKEKGAYAYIGSSPNSYWGEDYYWSVGANAVFGVQPTFEGTSMGSYDATFLEDSYNTVNSIMWAGNLAATHAGNIGNITHIGAHYYWEAYHVLGDGSVM |
| Protein Length | Partial, 229-594aa |
| Tag | N-terminal 6xHis-SUMO-tagged |
| Reactivity | Bacteria |
| Applications | SDS-PAGE |
| Form | Liquid, in Tris-based buffer, 50% glycerol |
| Purity | Greater than 90% as determined by SDS-PAGE. |
| References | "Biochemical and functional properties of lysine-specific cysteine proteinase (Lys-gingipain) as a virulence factor of Porphyromonas gingivalis in periodontal disease."Abe N., Kadowaki T., Okamoto K., Nakayama K., Ohishi M., Yamamoto K.J. Biochem. 123:305-312(1998) |
| Background | Cysteine proteinase with a strong preference for substrates with Lys in the P1 position. Hydrolyzes bovine hemoglobin, bovine serum albumin, casein, human placental type I collagen and human IgA and IgG. Disrupts the functions of polymorphonuclear leukocytes. May act as a virulence factor in the development of peridontal disease. Involved in the coaggregation of P.gingivalis with other oral bacteria. |
| Supplier | Cusabio |
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