Dual specificity protein phosphatase 23, Low molecular mass dual specificity phosphatase 3, LDP-3, VH1-like phosphatase Z, DUSP23, LDP3, VHZ, VH1-Like Member Z, EC 3.1.3.16, EC 3.1.3.48, DUSP25, MOSP, LDP3, Dual Specificity Phosphatase 23, VH1-Like Phosphatase Z, LDP-3, VHZ, Low-Molecular-Mass Dual-Specificity Phosphatase 3, Low Molecular Mass Dual Specificity Phosphatase 3, Dual Specificity Protein, Phosphatase 23, Testicular Tissue Protein Li 59.
Greater than 90% as determined by SDS-PAGE.
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DUSP23 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 170 amino acids (1-150 a.a) and having a molecular mass of 18.8kDa.
DUSP23 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Dual specificity protein phosphatase 23, Low molecular mass dual specificity phosphatase 3, LDP-3, VH1-like phosphatase Z, DUSP23, LDP3, VHZ, VH1-Like Member Z, EC 3.1.3.16, EC 3.1.3.48, DUSP25, MOSP, LDP3, Dual Specificity Phosphatase 23, VH1-Like Phosphatase Z, LDP-3, VHZ, Low-Molecular-Mass Dual-Specificity Phosphatase 3, Low Molecular Mass Dual Specificity Phosphatase 3, Dual Specificity Protein, Phosphatase 23, Testicular Tissue Protein Li 59.
MGSSHHHHHH SSGLVPRGSH MGVQPPNFSW VLPGRLAGLA LPRLPAHYQF LLDLGVRHLV SLTERGPPHS DSCPGLTLHR LRIPDFCPPA PDQIDRFVQI VDEANARGEA VGVHCALGFG RTGTMLACYL VKERGLAAGD AIAEIRRLRP GSIETYEQEK AVFQFYQRTK.
DUSP23 is a protein-coding gene that plays a crucial role in various cellular processes by regulating the phosphorylation state of target proteins . Phosphorylation and dephosphorylation of proteins are essential mechanisms for controlling cellular activities such as signal transduction, cell division, and metabolism . DUSP23 is involved in the dephosphorylation of specific substrates, thereby modulating their activity and function .
The recombinant form of DUSP23 is typically produced using recombinant DNA technology. This involves cloning the DUSP23 gene into an expression vector, which is then introduced into a suitable host cell, such as Escherichia coli or mammalian cells . The host cells are cultured under conditions that promote the expression of the DUSP23 protein. After sufficient expression, the protein is purified using various chromatographic techniques to obtain the active recombinant enzyme .
DUSP23 mediates the dephosphorylation of proteins phosphorylated on tyrosine and serine/threonine residues . In vitro studies have shown that DUSP23 can dephosphorylate p44-ERK1 (MAPK3) but not p54 SAPK-beta (MAPK10) . Additionally, DUSP23 has been found to enhance the activation of JNK and p38 (MAPK14), which are important components of the mitogen-activated protein kinase (MAPK) signaling pathways . These pathways are involved in various cellular responses, including inflammation, stress response, and apoptosis .
DUSP23 also plays a role in the regulation of the transcription factor GCM1 (Glial Cells Missing Homolog 1), which is essential for placental development . The interaction between DUSP23 and GCM1 is enhanced by PKA-dependent phosphorylation of GCM1, leading to the dephosphorylation of GCM1 and its subsequent activation . This regulation is crucial for promoting placental cell fusion and vasculogenesis .