SRP0676
Sortase A, S. aureus, His-tag
Staphylococcus aureus, recombinant, N-terminal His-Tag
Synonym(s):
SrtA, sortase A
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About This Item
UNSPSC Code:
41202061
Pricing and availability is not currently available.
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recombinant
expressed in E. coli
tag
His tagged
form
liquid
mol wt
27.7 kDa
UniProt accession no.
storage temp.
−70°C
General description
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Application
This product is suitable for in vitro ligation of proteins and peptides to other. Sortase A has been shown to create circularized proteins [1], as well as couple polypeptides to a wide range of substituents including polymers [2], lipids [3], fluorophores [4], sugars [5], microspheres [3], peptide nucleic acids [6], among others.
Biochem/physiol Actions
Staphylococcal Sortase A is a bacterial transpeptidase that covalently links proteins to the bacterial cell wall by cleaving between threonine and glycine at an LPXTG recognition motif and catalyzes the formation of an amide bond between the carboxyl-group of threonine and the amino-group of the cell-wall peptidoglycan [7]. This chemistry can be exploited to site-specifically link proteins/peptides with the C-terminal LPETGX motif to other proteins or molecules possessing a glycine or aminomethylene motif [8].
Physical form
Aqueous buffered solution containing: 40 mM Tris-HCl, pH 8.0, 110 mM NaCl, 2.2 mM KCl, 8 mM imidazole, 0.04% Tween-20, and 20% glycerol
Analysis Note
Analysis of this product can be performed in a reaction buffer (50 μl) containing 50 mM HEPES (pH=7.4), 150 mM NaCl, 5 mM CaCl2, 5 mM (Gly)3, 25 mM Abz/Dnp substrate, and Sortase A for 30 min at 30°C. Fluorescence intensity is measured at Ex320nm/Em420nm.
Storage Class Code
10 - Combustible liquids
WGK
WGK 2
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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Ranganath Parthasarathy et al.
Bioconjugate chemistry, 18(2), 469-476 (2007-02-17)
The Sortase family of transpeptidase enzymes catalyzes sequence-specific ligation of proteins to the cell wall of Gram-positive bacteria. Here, we describe the application of recombinant Staphylococcus aureus Sortase A to attach a tagged model protein substrate (green fluorescent protein) to
Peptide-sugar ligation catalyzed by transpeptidase sortase: a facile approach to neoglycoconjugate synthesis.
Sharmishtha Samantaray et al.
Journal of the American Chemical Society, 130(7), 2132-2133 (2008-01-31)
S K Mazmanian et al.
Science (New York, N.Y.), 285(5428), 760-763 (1999-07-31)
Surface proteins of Gram-positive bacteria are linked to the bacterial cell wall by a mechanism that involves cleavage of a conserved Leu-Pro-X-Thr-Gly (LPXTG) motif and that occurs during assembly of the peptidoglycan cell wall. A Staphylococcus aureus mutant defective in
Maximilian W Popp et al.
Proceedings of the National Academy of Sciences of the United States of America, 108(8), 3169-3174 (2011-02-08)
Recombinant protein therapeutics often suffer from short circulating half-life and poor stability, necessitating multiple injections and resulting in limited shelf-life. Conjugation to polyethylene glycol chains (PEG) extends the circulatory half-life of many proteins, but the methods for attachment often lack
Hongyuan Mao et al.
Journal of the American Chemical Society, 126(9), 2670-2671 (2004-03-05)
Sortase (SrtA), a transpeptidase from Staphylococcus aureus, catalyzes a cell-wall sorting reaction at an LPXTG motif by cleaving between threonine and glycine and subsequently joining the carboxyl group of threonine to an amino group of pentaglycine on the cell wall
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