Product Description
Dual specificity phosphatase 18, also known as DuSP18, is a member of the dual-specificity phosphatase (DSP) family, which catalyzes dephosphorylation of phosphotyrosine and phosphothreonine residues. DuSP18 is inhibited by iodoarectic acid and is activated by manganese ions. Along with having preferential enzymatic activity against phosphorylated tyrosine residues over threonine residues, DuSP18 also dephosphorylates p-nitrophenyl phosphate (pNPP) in vitro. This protein is widely expressed with highest levels in liver, brain, ovary and testis. Recombinant human DuSP18 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.
Biovision | 7815 | DUSP18 human recombinant DataSheet
Biomolecule/Target: DUSP18
Synonyms: Dual specificity protein phosphatase 18, DUSP20
Alternates names: Dual specificity protein phosphatase 18, DUSP20
Taglines: Catalyzes dephosphorylation of phosphotyrosine and phosphothreonine residues.
NCBI Gene ID #: Mm.252481
NCBI Gene Symbol: EGF
Gene Source: Human
Accession #: P01132
Recombinant: Yes
Source: E. coli.
Purity by SDS-PAGEs: 98%
Assay: SDS-PAGE
Purity: N/A
Assay #2: N/A
Endotoxin Level: N/A
Activity (Specifications/test method): N/A
Biological activity: Specific activity: >1,100 units/mg. Enzymatic activity was confirmed by measuring the amount of enzyme hydrolyzing 1 nmole of p-nitrophenyl phosphate (pNPP) per minute at 37ºC, pH 7.5 using 10 mM of substrate
Results: Specific activity: >1,100 units/mg
Binding Capacity: N/A
Unit Definition: N/A
Molecular Weight: 40.4 kDa (359 aa, 149-482 aa + His Tag)
Concentration: 0.5 mg/ml
Appearance: Liquid
Physical form description: 0.5 mg/ml solution in 20 mM Tris-HCl buffer (pH 8.0) containing 40% glycerol, 0.1 mM PMSF, 1 mM EDTA and 1 mM DTT
Reconstitution Instructions: N/A
Amino acid sequence: MGSSHHHHHH SSGLVPRGSH MGSHMTAPSC AFPVQFRQPS VSGLSQITKS LYISNGVAAN NKLMLSSNQI TMVINVSVEV VNTLYEDIQY MQVPVADSPN SRLCDFFDPI ADHIHSVEMK QGRTLLHCAA GVSRSAALCL AYLMKYHAMS LLDAHTWTKS CRPIIRPNSG FWEQLIHYEF QLFGKNTVHM VSSPVGMIPD IYEKEVRLMI PL