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TAG-72, His, Canine

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.
$390.00
Z04718-100

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Product Introduction
Species Canine
Protein Construction
TAG-72 (Met1-Gln478)
Accession # XP_005615459.2		 His
N-term C-term
Purity > 95% as determined by Bis­Tris PAGE
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 for 6 months at -20℃ or below. Upon reconstitution, the product should be stable for 3 months at -80℃. Avoid repeated freeze-thaw cycles.
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TAG-72, His, Canine

The purity of TAG-72, His, Canine is greater than 95% as determined by SEC-HPLC. »

TAG-72, His, Canine

TAG-72, His, Canine on Bis-Tris PAGE under reduced condition. The purity is greater than 95%. »

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Background
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
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For research use only. Not intended for human or animal clinical trials, therapeutic or diagnostic use.