QTRTD1, 1-415aa, Human

Category: Proteins
Catalog
01-P2868
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Product Name QTRTD1, 1-415aa, Human
Description QTRTD1 interacts with QTRT1 to form an active queuine tRNA-ribosyltransferase. This enzyme exchanges queuine for the guanine at the wobble position of tRNAs with GuN anticodons (tRNA-Asp, -Asn, -His and -Tyr), thereby forming the hypermodified nucleoside queuosine. Recombinant human QTRTD1 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.
Synonyms Queuine tRNA-ribosyltransferase subunit QTRTD1, Queuine tRNA-ribosyltransferase subunit QTRTD1, FLJ12960, Queuine tRNA-ribosyltransferase domain-containing protein 1, Queuine tRNA ribosyltransferase subunit QTRTD1
Host E. coli
Molecular Weight 20.4 kDa (179aa)
Amino Acid Sequence MGSSHHHHHH SSGLVPRGSH MGSMKLSLTK VVNGCRLGKI KNLGKTGDHT MDIPGCLLYT KTGSAPHLTH HTLHNIHGVP AMAQLTLSSL AEHHEVLTEY KEGVGKFIGM PESLLYCSLH DPVSPCPAGY VTNKSVSVWS VAGRVEMTVS KFMAIQKALQ PDWFQCLSDG EVSCKEATSI KRVRKSVDRS LLFLDNCLRL QEESEVLQKS VIIGVIEGGD VMEERLRSAR ETAKRPVGGF LLDGFQGNPT TLEARLRLLS SVTAELPEDK PRLISGVSRP DEVLECIERG VDLFESFFPY QVTERGCALT FSFDYQPNPE ETLLQQNGTQ EEIKCMDQIK KIETTGCNQE ITSFEINLKE KKYQEDFNPL VRGCSCYCCK NHTRAYIHHL LVTNELLAGV LLMMHNFEHY FGFFHYIREA LKSDKLAQLK ELIHRQAS
Tag His-tag
Reactivity Human
Applications SDS-PAGE
Form Liquid, in Phosphate buffer saline (pH 7.4) containing 10% glycerol
Concentration 1mg/ml (determined by Bradford assay)
Purity > 95% by SDS-PAGE
Storage Can be stored at +4C short term (1-2 weeks). For long term storage, aliquot and store at -2°C or -7°C. Avoid repeated freezing and thawing cycles.
References Chen,Y.C., et al. (2010) RNA 16 (5), 958-968
Background QTRTD1 interacts with QTRT1 to form an active queuine tRNA-ribosyltransferase. This enzyme exchanges queuine for the guanine at the wobble position of tRNAs with GuN anticodons (tRNA-Asp, -Asn, -His and -Tyr), thereby forming the hypermodified nucleoside queuosine. Recombinant human QTRTD1 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.
Supplier ARP

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