Description
Recombinant Human WDYHV1/NTAQ1 Protein (GST Tag) | PKSH032966 | Gentaur US, UK & Europe Disrtribition
Synonyms: Protein N-terminal glutamine amidohydrolase;WDYHV1;Protein NH2-terminal glutamine deamidase;N-terminal Gln amidase;Nt(Q)-amidase;C8orf32; NTAQ1
Active Protein: N/A
Activity: Recombinant Human Protein N-terminal glutamine amidohydrolase is produced by our E.coli expression system and the target gene encoding Met1-Cys205 is expressed with a GST tag at the N-terminus.
Protein Construction: Recombinant Human Protein N-terminal glutamine amidohydrolase is produced by our E.coli expression system and the target gene encoding Met1-Cys205 is expressed with a GST tag at the N-terminus.
Fusion Tag: N-GST
Species: Human
Expressed Host: E.coli
Shipping: This product is provided as liquid. It is shipped at frozen temperature with blue ice/gel packs. Upon receipt, store it immediately at<-20°C.
Purity: > 95 % as determined by reducing SDS-PAGE.
Endotoxin: < 1.0 EU per µg as determined by the LAL method.
Stability and Storage: Store at < -20°C, stable for 6 months. Please minimize freeze-thaw cycles.
Molecular Mass: 49.8 kDa
Formulation: Supplied as a 0.2 μm filtered solution of PBS, 100mM GSH, 15% Glycerol, pH7.4.
Reconstitution: Not Applicable
Background: Human protein N-terminal glutamine amidohydrolase (WDYHV1) is an enzyme that in humans is encoded by the WDYHV1 gene, belongs to the NTAQ1 family.WDYHV1 mediates the side-chain deamidation of N-terminal glutamine residues to glutamate, which is an important step in N-end rule pathway of 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. However, it does not act on substrates with internal or C-terminal glutamine andnon-glutamine residues in any position. With the exception of proline, all tested second-position residues on substrate peptides do not greatly influence the activity. In contrast, a proline at position 2, virtually abolishes deamidation of N-terminal glutamine.
Research Area: Cell biology
