Recombinant Pseudomonas aeruginosa Lysyl endopeptidase protein (His tag)
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Recombinant Pseudomonas aeruginosa Lysyl endopeptidase protein (His tag) is a Pseudomonas aeruginosa PAO1 Full Length protein, in the 212 to 462 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE.
View Alternative Names
PA4175, prpL, Lysyl endopeptidase, Protease IV, PvdS-regulated endoprotease
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Pseudomonas aeruginosa Lysyl endopeptidase protein (His tag) (AB225969)
(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) analysis of ab225969 with 5% enrichment gel and 15% separation gel.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Lysyl endopeptidase plays a role in breaking down proteins into smaller peptides or amino acids an essential part of protein metabolism. This enzyme does not function as part of a larger protein complex but its activity is critical in the proteolytic processing of proteins. It has importance in cellular processes like protein turnover and maturation by degrading misfolded or damaged proteins.
Pathways
Lysyl endopeptidase involves itself in metabolic and signaling pathways responsible for protein degradation and turnover. It participates in the ubiquitin-proteasome pathway a central path for degrading excess or defective proteins. Related proteins include ubiquitin-conjugating enzymes which tag proteins for breakdown and the 26S proteasome complex where proteins are processed and recycled.
Specifications
Form
Liquid
General info
Function
Lysine-specific endoprotease (PubMed : 12419815). Involved in corneal virulence.
Sequence similarities
Belongs to the peptidase S1 family.
Post-translational modifications
Experiments performed in E.coli. Processing of pro-endopeptidase to mature endopeptidase is probably autocatalytic, as mutations in the probable active site residues prevent processing, and purified inactive pro-endopeptidase disappears in the presence of active endopeptidase.
Target data
Complementary Products
Proteins & Peptides
AB273530
Recombinant Human coronavirus SARS-CoV-2 nucleocapsid protein (His tag)
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Product promise
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