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% purity and suitable for SDS-PAGE.
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Key facts
- Purity
>90% SDS-PAGE
- Expression system
Escherichia coli
- Tags
His tag N-Terminus
- Applications
SDS-PAGE
- Biologically active
No
Amino acid sequence
A G Y R D G F G A S G S C E V D A V C A T Q S G T R A Y D N A T A A V A K M V F T S S A D G G S Y I C T G T L L N N G N S P K R Q L F W S A A H C I E D Q A T A A T L Q T I W F Y N T T Q C Y G D A S T I N Q S V T V L T G G A N I L H R D A K R D T L L L E L K R T P P A G V F Y Q G W S A T P I A N G S L G H D I H H P R G D A K K Y S Q G N V S A V G V T Y D G H T A L T R V D W P S A V V E G G S S G S G L L T V A G D G S Y Q L R G G L Y G G P S Y C G A P T S Q R N D Y F S D F S G V Y S Q I S R Y F A P
Reactivity data
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Associated Products
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Target data
Function
Lysine-specific endoprotease (PubMed:12419815). Involved in corneal virulence.
Alternative names
Lysyl endopeptidase, Protease IV, PvdS-regulated endoprotease, PA4175, prpL
Recommended products
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% purity and suitable for SDS-PAGE.
Key facts
- Purity
>90% SDS-PAGE
- Expression system
Escherichia coli
- Tags
His tag N-Terminus
- Applications
SDS-PAGE
- Biologically active
No
- Accession
- Q9HWK6-1
- Animal free
No
- Species
Pseudomonas aeruginosa PAO1
- Concentration
- Storage buffer
pH: 7.2 - 7.4
Constituents: Tris buffer, 50% Glycerol (glycerin, glycerine)
Sequence info
Amino acid sequence
A G Y R D G F G A S G S C E V D A V C A T Q S G T R A Y D N A T A A V A K M V F T S S A D G G S Y I C T G T L L N N G N S P K R Q L F W S A A H C I E D Q A T A A T L Q T I W F Y N T T Q C Y G D A S T I N Q S V T V L T G G A N I L H R D A K R D T L L L E L K R T P P A G V F Y Q G W S A T P I A N G S L G H D I H H P R G D A K K Y S Q G N V S A V G V T Y D G H T A L T R V D W P S A V V E G G S S G S G L L T V A G D G S Y Q L R G G L Y G G P S Y C G A P T S Q R N D Y F S D F S G V Y S Q I S R Y F A P
- Accession
- Protein length
Full Length
- Predicted molecular weight
42.4 kDa
- Amino acids
212 to 462
- Nature
Recombinant
- Tags
His tag N-Terminus
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.
Storage
- Shipped at conditions
Blue Ice
- Appropriate short-term storage conditions
-20°C
- Appropriate long-term storage conditions
-20°C
- Aliquoting information
Upon delivery aliquot
- Storage information
Avoid freeze / thaw cycle
Supplementary info
This supplementary information is collated from multiple sources and compiled automatically.
- Activity summary
Lysyl endopeptidase also known as Lys-C or lysyl proteinase is an enzyme that cleaves peptide bonds at the carboxyl side of lysine residues. It is a serine protease with a molecular mass of approximately 30 kDa. This enzyme is expressed in various tissues including the vascular system where it contributes to protein modification processes. Lysyl endopeptidase exhibits high specificity for lysine residues making it useful in protein studies and peptide mapping.
- 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.
- Associated diseases and disorders
Lysyl endopeptidase connects to pathological conditions such as cancer and inflammatory disorders. Malfunctions in its proteolytic activity can result in unregulated protein degradation contributing to cancer progression. Additionally its interaction with matrix metalloproteinases such as MMP2 and MMP9 is significant in tissue remodeling and inflammation processes linking lysyl endopeptidase to inflammatory diseases where the excess breakdown of tissue contributes to pathology.
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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.
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