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Sortase

Custom & Catalog Recombinant Proteins

Sortases are a family of membrane–anchored transpeptidases expressed by Gram–positive bacteria.1 Sortase A catalyzes the cleavage of C-terminal recognition motif (LPXTG) of multiple structurally unrelated proteins followed by formation of an amide bond with the peptidoglycan layer of the bacteria.2 Since Sortases are widely distributed among a variety of bacterial pathogens and required for virulence, Sortases represent a promising therapeutic target for the development of novel anti-infective agents.3 In addition, Sortase A can be used as a biotechnology tool for a variety of protein modifications and immobilization by sortase-mediated protein ligation.4

DescriptionSize Reference USD Qty  
Sortase A protease, recombinant - 10 µg10 µg AS-72229 374.00Add to cart


Size:

  10 µg

Storage:

  Store at -80°C. Avoid multiple freeze/thaw cycles.

Sortases are a family of membrane–anchored transpeptidases expressed by Gram–positive bacteria.1 Sortase A catalyzes the cleavage of C-terminal recognition motif (LPXTG) of multiple structurally unrelated proteins followed by formation of an amide bond with the peptidoglycan layer of the bacteria.2 Since Sortases are widely distributed among a variety of bacterial pathogens and required for virulence, Sortases represent a promising therapeutic target for the development of novel anti-infective agents.3 In addition, Sortase A can be used as a biotechnology tool for a variety of protein modifications and immobilization by sortase-mediated protein ligation.4

Sortase A from Staphylcoccus aureus was expressed in E. coli expression system with a Nterminal His tag. It is comprised of 26-206 amino acids and its MW is 21.7-kDa.

Sortase A is stored in 40 mM Tris-HCl, pH 8.0, 110 mM NaCl, and 2.2 mM KCl, 8 mM imidazole, 0.04% Tween 20, and 20 % glycerol.

The purity is >87% as estimated on SDS PAGE.


References:


  1. Spirig T, et al. Mol Microbiol 82, 1044 (2011).
  2. Marraffini LA, et al. Microbiol Mol Biol Rev 70, 192 (2006).
  3. Maresso AW, et al. Pharmacol Rev 60, 128 (2008).
  4. Proft T. Biotechnol Lett 32, 1 (2010).
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