Recombinant humaan DUSP18-eiwit

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.

Specific activity is > 300 units/mg, and is defined as the amount of enzyme that hydrolyze 1.0 nmole of p-nitrophenyl phosphate (pNPP) per minute at pH 7.5 at 37C

Dual specificity protein phosphatase 18, DSP18, DUSP20, Low molecular weight dual specificity phosphatase 20, LMW-DSP20, LMWDSP20

E.coli

Human

His-Tag

SDS-PAGE, Enzyme Activity

0.5 mg/mL (determined by Bradford assay)

> 95% by SDS-PAGE

Specific activity is > 300unit/mg, and is defined as the amount of enzyme that hydrolyze 1.0 nmole of p-nitrophenyl phosphate (pNPP) per minute at pH 7.5 at 37C

23.6 kDa (212aa) confirmed by MALDI-TOF

DUSP18, Dual specificity protein phosphatase 18, DSP18, DUSP20, ATGP3562-10 µg, ATGP3562-20 µg, ATGP3562-50 µg, ATGP3562-100 µg, ATGP3562-250 µg, ATGP3562-500 µg, ATGP3562-1 mg, ATGP3562-10, ATGP3562-20, ATGP3562-50, ATGP3562-100, ATGP3562-250, ATGP3562-500, ATGP3562-1

Jeong D G., et al. (2006) Acta Crystallogr. 62:582-588.; ; Aoki N., et al. (2001) J Biochem. 130:133-140.

Can be stored at 2°C to 8°C for 1 week. For long term storage, aliquot and store at -20C to -80C. Avoid repeated freezing and thawing cycles.

Liquid in. 20 mM Tris-HCl buffer (pH 8.0) containing 1mM DTT, 40% glycerol, 0.1mM PMSF, 1mM EDTA

Enzymes & Proteases

NP_689724

Q8NEJ0

Human

MGSSHHHHHH SSGLVPRGSH MGSHMTAPSC AFPVQFRQPS VSGLSQITKS LYISNGVAAN NKLMLSSNQI TMVINVSVEV VNTLYEDIQY MQVPVADSPN SRLCDFFDPI ADHIHSVEMK QGRTLLHCAA GVSRSAALCL AYLMKYHAMS LLDAHTWTKS CRPIIRPNSG FWEQLIHYEF QLFGKNTVHM VSSPVGMIPD IYEKEVRLMI PL