Name : Canine TAG-72 Protein

Product Source :
Recombinant Canine TAG-72 Protein is expressed from E.coli with His tag at the C-Terminus. It contains Met1-Gln478.[Accession | XP_005615459.2]

Molecular Weight :
The protein has a predicted MW of 56.19 kDa same as Tris-Bis PAGE result.

Endotoxin Level :
Less than 1EU per μg by the LAL method.

Purity :
> 95% as determined by Tris-Bis PAGE> 95% as determined by HPLC

Formulation :
Lyophilized from 0.22μm 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 μg/ml is recommended. Dissolve the lyophilized protein in distilled water.

Storage and Stability :
-20 to -80°C for 12 months as supplied from date of receipt.-80°C for 3-6 months after reconstitution.2-8°C for 2-7 days after reconstitution.Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.

Product Concentration :
Tris-Bis PAGE Canine TAG-72 on Tris-Bis PAGE under reduced condition. The purity is greater than 95%. SEC-HPLC The purity of Canine TAG-72 is greater than 95% as determined by SEC-HPLC.

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

References & Citations :
(1) Zheng S, Shuman S. Structure-function analysis of vaccinia virus mRNA cap (guanine-N7) methyltransferase. RNA. 2008 Apr;14(4):696-705. doi: 10.1261/rna.928208. Epub 2008 Feb 6. PMID: 18256245; PMCID: PMC2271365.(2) Zheng S, Hausmann S, Liu Q, Ghosh A, Schwer B, Lima CD, Shuman S. Mutational analysis of Encephalitozoon cuniculi mRNA cap (guanine-N7) methyltransferase, structure of the enzyme bound to sinefungin, and evidence that cap methyltransferase is the target of sinefungin’s antifungal activity. J Biol Chem. 2006 Nov 24;281(47):35904-13. doi: 10.1074/jbc.M607292200. Epub 2006 Sep 12. PMID: 16971388.

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