NTAQ1 Protein, Human (GST)

NTAQ1 Protein is a monomeric globular protein with alpha-beta-alpha three-layer sandwich architecture. NTAQ1 converts N-terminal glutamine to glutamate by eliminating the amine group and plays an essential role in the N-end rule pathway for protein degradation. The active site and catalytic mechanism of NTAQ1 are similar to those of transglutaminases. NTAQ1 Protein, Human (GST) is the recombinant human-derived NTAQ1 protein, expressed by E. coli , with N-GST labeled tag. The total length of NTAQ1 Protein, Human (GST) is 205 a.a., with molecular weight of 45-50 kDa.

Protein N-terminal glutamine amidohydrolase (NTAQ1) is a monomeric globular protein with alpha-beta-alpha three-layer sandwich architecture. The catalytic triad located in the active site, Cys-His-Asp, is highly conserved among Ntaq family and transglutaminases from diverse organisms. NTAQ1 converts N-terminal glutamine to glutamate by eliminating the amine group and plays an essential role in the N-end rule pathway for protein degradation. Conversion of the resulting N-terminal glutamine to glutamate renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. NTAQ1 does not act on substrates with internal or C-terminal glutamine and does not act on non-glutamine residues in any position. In addition, it does not deaminate acetylated N-terminal glutamine. The active site and catalytic mechanism of NTAQ1 are similar to those of transglutaminases^[1][2].

Human

E. coli

N-GST

AAH08781.1 (M1-C205)

55093  [NCBI]

MEGNGPAAVHYQPASPPRDACVYSSCYCEENVWKLCEYIKNHDQYPLEECYAVFISNERKMIPIWKQQARPGDGPVIWDYHVVLLHVSSGGQSFIYDLDTVLPFPCLFDTYVEDAIKSDDDIHPQFRRKFRVICADSYLKNFASDRSHMKDSSGNWREPPPPYPCIETGDSKMNLNDFISMDPKVGWGAVYTLSEFTHRFGSKNC

45-50 kDa

Greater than 95% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.