Product Description |
Recombinant Canine TAG-72 Protein is expressed from E.coli with His tag at the C-Terminus.It contains Met1-Gln478. |
Product 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. |
Product Category |
Recombinant Protein |
Target |
TAG-72 |
Synonyms |
mRNA (guanine-N(7))-methyltransferase; mRNA-methyltransferase; TAG 72; TAG72 |
Accession |
|
Species |
Canine |
Biotinylated |
no |
Amino Acid Range |
Met1-Gln478 |
Molecular Weight |
The protein has a predicted MW of 56.19 kDa same as Bis-Tris PAGE result. |
Product Tag |
C-His |
Express System |
E.coli |
Purity |
> 95% as determined by Bis-Tris PAGE;> 95% as determined by HPLC |
Endotoxin |
Less than 1EU per ug by the LAL method. |
Form |
Lyophilized |
Shipping |
Shipped at ambient temperature. |
Formulation |
Lyophilized from 0.22um filtered solution in PBS (pH 7.4). Normally 8% trehalose is added as protectant before lyophilization. |
Reconstitution |
Centrifuge the tube before opening. Reconstituting to a concentration more than 100 ug/ml is recommended. Dissolve the lyophilized protein in distilled water. |
Stability And Storage |
Reconstituted protein stable at -80°C for 12 months, 4°C for 1 week. Use a manual defrost freezer and avoid repeated freeze-thaw cycles. |
|
|
Canine TAG-72 on Bis-Tris PAGE under reduced condition. The purity is greater than 95%. |
|
|
The purity of Canine TAG-72 is greater than 95% as determined by SEC-HPLC. |
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