

| Catalog No. | JN051042 |
|---|---|
| Description |
Recombinant Staphylococcus aureus Sortase A/SrtA Protein, N-His (JN051042) expressed in E. coli. Purity: >90% as determined by SDS-PAGE..
Highlights
|
| Expression system | E. coli |
| Accession | Q2FV99 |
| Protein length | Gln60-Lys206 |
| Applications | ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress |
| Species | Staphylococcus aureus |
| Nature | Recombinant |
| Endotoxin level | Please contact with the lab for this information. |
| Purity | >90% as determined by SDS-PAGE. |
| Form | Lyophilized |
| Storage buffer | Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol. Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA. |
| Reconstitution | Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details. |
| Shipping | In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise. |
| Stability and Storage | Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt. |
| Alternate Names | EC:3.4.22.70, Sortase A, Surface protein sorting A, srtA |
| Background | Sortase A is a ~23 kDa protein. Transpeptidase that anchors surface proteins to the cell wall. Recognizes and modifies its substrate by proteolytic cleavage of a C-terminal sorting signal. Following cleavage, a covalent intermediate is formed via a thioester bond between the sortase and its substrate, which is then transferred and covalently attached to the cell wall. This sortase recognizes a Leu-Pro-x-Thr-Gly (LPXTG) motif, which is cleaved by the sortase between the threonine and glycine residues. Utilizes lipid II as the peptidoglycan substrate for the sorting reaction. 1. Mazmanian, SK. et al. (1999) Science (New York, N.Y.) 285, 760-3. PMID: 10427003 2. Ton-That, H. et al. (1999) The Journal of biological chemistry 274, 24316-20. PMID: 10446208 3. Ton-That, H. et al. (1999) Proceedings of the National Academy of Sciences of the United States of America 96, 12424-9. PMID: 10535938 4. Ton-That, H. et al. (2002) The Journal of biological chemistry 277, 7447-52. PMID: 11714722 5. Kruger, RG. et al. (2004) Biochemistry 43, 1541-51. PMID: 14769030 6. Marraffini, LA. et al. (2004) The Journal of biological chemistry 279, 37763-70. PMID: 15247224 |
| Note | For research use only |




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