| Target | |
|---|---|
| Synonyms | srtA; Surface protein sorting A |
| Description | Recombinant Staphylococcus aureus sortase A 7M Protein with C-terminal 6×His tag |
| Delivery | In Stock |
| Uniprot ID | Q2FV99 |
| Expression Host | E.coli |
| Tag | C-6×His tag |
| Molecular Characterization | sortase A(Gln60-Lys206) 6×His tag |
| Molecular Weight | The protein has a predicted molecular mass of 17.8 kDa after removal of the signal peptide. |
| Purity | The purity of the protein is greater than 85% as determined by SDS-PAGE and Coomassie blue staining. |
| Formulation & Reconstitution | Lyophilized from Tris Buffer, pH 8.0. Normally 5 % – 8% trehalose is added as protectants before lyophilization. Please see Certificate of Analysis for specific instructions of reconstitution. |
| Storage&Shipping | Store at -20°C to -80°C for 12 months in lyophilized form. After reconstitution, if not intended for use within a month, aliquot and store at -80°C (Avoid repeated freezing and thawing).Lyophilized proteins are shipped at ambient temperature. |
| Sterility | Products are supplied non-sterile. For cell culture applications, dilute in appropriate medium and sterile-filter (0.22 µm) prior to use. |
| Background | Sortase A (SrtA) is a bacterial transpeptidase derived from *Staphylococcus aureus* that catalyzes site-specific protein ligation by recognizing the LPXTG motif and forming a covalent bond with an N-terminal oligoglycine-containing substrate. Staphylococcus aureus Sortase A 7M is an engineered heptamutant containing seven amino acid substitutions (P94R, E105K, E108A, D160N, D165A, K190E, and K196T). The five mutations P94R, D160N, D165A, K190E, and K196T enhance catalytic efficiency, while E105K and E108A confer calcium-independent activity. Compared with wild-type Sortase A, this engineered variant combines enhanced catalytic performance with the ability to function without added Ca²⁺. It is widely applicable to site-specific protein labeling, protein conjugation, antibody modification, and protein immobilization. |
| Usage | Research use only |
| Conjugate | Unconjugated |
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