| ￥3500 | |
| Z04718-100 | |
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| Species | Canine | ||||
| Protein Construction |
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| Purity |
> 95% as determined by BisTris PAGE > 95% as determined by HPLC |
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| Endotoxin Level | Less than 1EU per μg by the LAL method. | ||||
| Expression System | E.coli | ||||
| Theoretical Molecular Weight | 56.19 kDa | ||||
| Apparent Molecular Weight | The protein has a predicted MW of 56.19 kDa same as Bis-Tris PAGE result. | ||||
| Formulation | Lyophilized from 0.22μm filtered solution in PBS (pH 7.4). | ||||
| Reconstitution | Centrifuge the tube before opening. Reconstituting to a concentration more than 100 μg/ml is recommended. Dissolve the lyophilized protein in distilled water. | ||||
| Storage & Stability | Upon receiving, the product remains stable up to 6 months at -20 °C or below. Upon reconstitution, the product should be stable for 3 months at -80 °C. Avoid repeated freeze-thaw cycles. |
The purity of TAG-72, His, Canine is greater than 95% as determined by SEC-HPLC. »
TAG-72, His, Canine on Bis-Tris PAGE under reduced condition. The purity is greater than 95%. »
| Target Background | The guanine-N7 methyltransferase domain of vaccinia virus mRNA capping enzyme is a heterodimer composed of a catalytic subunit and a stimulatory subunit. Cap (guanine-N7) methylation is an essential step in eukaryal mRNA synthesis and a potential target for antiviral, antifungal, and antiprotozoal drug discovery. |
| Synonyms | mRNA (guanine-N(7))-methyltransferase; mRNA-methyltransferase; TAG 72; TAG72 |
For research use only. Not intended for human or animal clinical trials, therapeutic or diagnostic use.
