Recombinant human DUSP23 protein

DuSP23, also known as low molecular mass dual specificity phosphatase 3 (LDP-3), belongs to the protein-tyrosine phosphatase family. This protein is a protein phosphatase that mediates dephosphorylation of proteins phosphorylated on Tyr and Ser/Thr residues. In vitro, it can dephosphorylate p44-ERK1 (MAPK3) but not p54 SAPK-beta (MAPK10) in vitro. This protein able to enhance activation of JNK and p38 (MAPK14) . Recombinant human DuSP23 protein, fused to His-tag at N-terminus, was expressed in E. coli and purified by using conventional chromatography techniques.

Product Specifications

Product Name Alternative

Dual specificity protein phosphatase 23, DuSP25, LDP-3, MOSP, VHZ, Low molecular mass dual specificity phosphatase 3, VH1-like phosphatase Z

Expression System

E.coli

Antigen Species

Human

Tag

His-Tag

Applications

SDS-PAGE

Concentration

1 mg/mL (determined by Bradford assay)

Purity

> 90% by SDS-PAGE

Molecular Weight

18.8 kDa (170aa) confirmed by MALDI-TOF

Additionnal Information

DUSP23, Dual specificity protein phosphatase 23, DuSP25, LDP-3, MOSP, VHZ, ATGP1297-10 µg, ATGP1297-20 µg, ATGP1297-50 µg, ATGP1297-100 µg, ATGP1297-250 µg, ATGP1297-500 µg, ATGP1297-1 mg, ATGP1297-10, ATGP1297-20, ATGP1297-50, ATGP1297-100, ATGP1297-250, ATGP1297-500, ATGP1297-1

References & Citations

Alonso A., et al. (2004) J. Biol. Chem. 279:35768-35774; ; Wu Q, et al. (2004) Int J Biochem Cell Biol. 36 (8) :1542-53.

Storage Conditions

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.

Formulation

Liquid in. 20 mM Tris-HCl buffer (pH 8.0) containing 2mM DTT, 10% glycerol, 100 mM NaCl

Scientific Category

Cell Cycle

NCBI Accession Number

NP_060293

Uniprot Accession Number

Q9BVJ7

Species

Human

AA Sequence

MGSSHHHHHH SSGLVPRGSH MGVQPPNFSW VLPGRLAGLA LPRLPAHYQF LLDLGVRHLV SLTERGPPHS DSCPGLTLHR LRIPDFCPPA PDQIDRFVQI VDEANARGEA VGVHCALGFG RTGTMLACYL VKERGLAAGD AIAEIRRLRP GSIETYEQEK AVFQFYQRTK