Peptides

Bacterial Sortase Substrate I, FRET - 1 mg

$256.00
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  • Cat.Number : AS-62231
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    In stock

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This 5-amino acid peptide is a sortase substrate, C-terminal sorting signal. Sortase cleaves surface proteins at the LPXTG motif and catalyzes the formation of an amide bond between the carboxyl group of threonine and the amino group of cell-wall crossbridges. Sortases are a family of Gram-positive transpeptidases responsible for anchoring surface protein virulence factors to the peptidoglycan cell wall layer. Cleavage of this FRET substrate by sortase reveals the fluorescent signal, Abs/Em = 340/490 nm.

Specifications

Chemistry
Sequence one letter code
  • DABCYL-LPETG-EDANS
Sequence three letter code
  • DABCYL-Leu-Pro-Glu-Thr-Gly-EDANS
Molecular Mass/ Weight
  • 1015.2
Properties
Absorbance (nm)
  • 340
Emission (nm)
  • 490
Modification
Conjugation type
  • Double dyes
Modification Name
Conjugation
  • Conjugated
Quantity & Purity
Purity
  • Peak Area by HPLC ≥95%
Storage & stability
Form
  • Lyophilized
Storage Conditions
  • - 20 °C Protected from light
Activity
Application
Biomarker Target
Detection Method
Research Area
Sub-category Research Area
Usage
  • Research use
Source
Source / Species
  • bacteria

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References

An iron-regulated sortase anchors a class of surface protein during Staphylococcus aureus pathogenesis

PNAS . 2002 Feb 19 ; 99(4) 2293 | DOI : https://doi.org/10.1073/pnas.032523999

  • S. Mazmanian
  • et al

Surface proteins of gram-positive bacteria and mechanisms of their targeting to the cell wall envelope

Mol. Biol. Rev. . 1999 Mar 01 ; 63(1) 174 | DOI : https://doi.org/10.1128/MMBR.63.1.174-229.1999

  • W. Navarre
  • O. Schneewind

Structure of sortase, the transpeptidase that anchors proteins to the cell wall of Staphylococcus aureus

PNAS . 2001 May 02 ; 98(11) 6056 | DOI : https://doi.org/10.1073/pnas.101064198

  • U. Ilangovan
  • et al

Purification and characterization of sortase, the transpeptidase that cleaves surface proteins of Staphylococcus aureus at the LPXTG motif

PNAS . 1999 Oct 26 ; 96(22) 12424 | DOI : https://doi.org/10.1073/pnas.96.22.12424

  • H. Ton-That
  • et al