Recombinant Streptomyces hygroscopicus Bar Protein
SKU: PKSQ050087-50
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Recombinant Streptomyces hygroscopicus Bar Protein
| SKU # | PKSQ050087 |
| Expression Host | E.coli |
Description
| Synonyms | PPT N-acetyltransferase, Phosphinothricin N-acetyltransferase, Phosphinothricin-resistance protein, bar |
| Species | Streptomyces hygroscopicus |
| Expression Host | E.coli |
| Sequence | Met1-Ile183 |
| Accession | P16426 |
| Calculated Molecular Weight | 20.6 kDa |
| Observed Molecular Weight | 18-20 kDa |
| Tag | None |
| Bio-activity | Not validated for activity |
Properties
| Purity | > 95 % as determined by reducing SDS-PAGE. |
| Endotoxin | < 1.0 EU per μg of the protein as determined by the LAL method. |
| Storage | Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months. |
| Shipping | This product is provided as lyophilized powder which is shipped with ice packs. |
| Formulation | Lyophilized from a 0.2 μm filtered solution of 12.5mM Tris-HCl, 50mM NaCl, 5% Trehalose, 5% Mannitol, 0.01% Tween 80, 2mM DTT, 1mM EDTA, pH8.5. Normally 5% - 8% trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the printed manual. |
| Reconstitution | Please refer to the printed manual for detailed information. |
Phosphinothricin N-acetyltransferase (PAT) is an enzyme that acetylates the free NH2 group of L-phosphinothricin (L-PPT) in the presence of acetyl-CoA as a co-substrate. It is highly specific for L-PPT and does not acetylate other L-amino acids or structurally similar molecules. L-PPT is a glutamate analog that can inhibit glutamine synthetase activity in plants, resulting in the accumulation of ammonia to toxic levels and impairment of photosynthesis. The introduction of a PAT gene into a plant genome can confer resistance to glufosinate herbicide during post-emergent applications.