Fimbrial Protein (pilA), His-tag


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SKU: P2020-143 trenzyme

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Pilin monomers form polar and retractable fibers that represent the major adhesin of bacteria allowing attachment to host cells. Interestingly, pilin variants are sometimes highly divergent among different bacterial strains, thereby impeding the development of effective, universal vaccines targeting bacterial adhesin molecules. Here, an N-terminally truncated pilin monomer (named pilA) from both the Pseudomonas aeruginosa strain PAK and Pa110594 was purified by affinity chromatography. Since the N-terminus is highly hydrophobic, its truncation results in increased solubility while retaining a functional receptor-binding site.

The Fimbrial Protein (pilA) is available from the strain PAK or Pa110594. The strain and size can be selected by using the buttons.


  • Product Name: Fimbrial Protein (pilA), His-tag
  • Catalog No.: P2020-143 strain: PAK; P2020-145 strain: Pa110594
  • RefSeq Links:
    PAK: PDBe 1dzo A; UniProt: P02973
    Pa110594: pdb3JZZ; UniProt: Q8KQ36
  • Synonyms: PAK pilA, pilA, Pilin, fimbrial protein, type 4 fimbrial protein PilA, type IV fimbrial protein
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Sequence Information

  • Species: Pseudomonas aerigunosa
  • Tags: His-tag, N-terminal
  • Sequence without tags - strain: PAK (AA 35-150):
  • Sequence without tags - strain: Pa110594 (AA 34-178):

Product Information

  • Expression Host: E. coli
  • Formulation: PBS; pH 7.4. 
  • Format: Liquid, stored and shipped at -80 °C
  • Purity: > 85% as determined by SDS-PAGE
  • Application: Immunogen, vaccine development

Background Information

Pathogenic bacteria, such as Pseudomonas aeruginosa, have developed a variety of virulence factors facilitating the infection process. A prominent virulence factor are pilins essentially required for attachment of the pathogen to the host cell and thus to initiate an infection. Pilins of P. aeruginosa are polymers of non-covalently associated pilA monomers that form a fiber with a diameter of six nm and a length of up to several micrometers. These fibers are polar and dynamic, retractable structures that are regarded as prototypes of type IV pili. Although each pilA monomer has a receptor binding site, only the monomers at the pilus tip have functional binding sites mediating adhesion. Binding occurs at glycosylated receptors that contain a β-D-GalNAc (1 → 4)-β-D-Gal moiety, such as the glycolipids asialo-GM1 and asialo-GM2. Strikingly, pilin fibers of different bacterial strains are sometimes highly divergent, but all strains still seem to bind a common receptor, asialo-GM1. Structural elucidation of pilin variants is essential for the development of effective vaccines that block adhesion of pathogens to host cells. Successful crystallization of the pilin monomer pilA from the P. aeruginosa strain Pa110594 as well as PAK was enabled by truncation of the hydrophobic N-terminus to increase solubility without hindering receptor binding capacities.


Additional information strain: PAK

SDS-PAGE/Coll. Coomassie

Histogram of marked lane in gel picture

SDS-Page Fimbrial Protein (pilA), His-tag
Histogram Fimbrial Protein pilA His-tag


Additional information strain: Pa110594

SDS-PAGE/Coll. Coomassie

Histogram of marked lane in gel picture


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