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Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
DUSP23 Antibody / Dual specificity protein phosphatase 23 Antibody recognizes DUSP23, also called VHZ, a compact member of the dual-specificity phosphatase family. Reversible protein phosphorylation regulates signaling, localization, and protein-protein interactions throughout the cell. Kinases add phosphate groups to selected amino acid residues, while phosphatases remove them. Dual-specificity phosphatases can act on phosphotyrosine and, depending on the enzyme and substrate, phosphoserine or phosphothreonine. DUSP23 belongs to the smaller phosphatases whose structures are dominated by the catalytic domain rather than extensive accessory regions.
The DUSP23 active site contains the conserved cysteine-based motif characteristic of protein tyrosine phosphatases. Catalysis involves attack on the phosphate group by the active-site cysteine, formation of a transient phosphorylated enzyme intermediate, and hydrolysis that restores the catalytic site. Although this chemistry is shared by many phosphatases, substrate recognition depends on additional structural and cellular features. A small catalytic domain does not imply that DUSP23 acts indiscriminately on every phosphorylated protein it encounters.
The DUSP23 Antibody recognizes a phosphatase with a particularly compact architecture, making the question of how it selects physiological substrates especially interesting. Experimental studies have linked DUSP23 to processes involving cell proliferation, migration, and adhesion-associated signaling. Some reports describe increased DUSP23 expression in particular tumor settings and changes in cellular behavior following experimental manipulation of its abundance. These findings have stimulated interest in its possible contribution to cancer-associated signaling networks. However, altered expression and effects observed after overexpression or depletion do not by themselves establish which endogenous proteins are directly dephosphorylated by DUSP23.
Substrate identification is therefore a central unresolved issue. Distinguishing direct catalytic targets from secondary consequences of altered signaling requires attention to enzyme localization, substrate accessibility, and the effects of catalytically inactive variants. It is also important to separate the biochemical capacity to remove a phosphate group from evidence that the reaction occurs under physiological conditions. A clearer map of DUSP23 substrates would explain how this unusually small phosphatase achieves signaling selectivity and why changes in its activity have different consequences across cellular contexts.
Explore related research targets in our Signal Transduction Antibodies for Cell Signaling and Regulatory Pathway Research collection.
The recommended approach is to establish the optimal working dilution of the DUSP23 Antibody / Dual specificity protein phosphatase 23 Antibody through preliminary testing.
The DUSP23 Antibody was generated using e. coli-derived human DUSP23 recombinant protein (amino acids S41-K150).
The DUSP23 Antibody is stable for up to one month at 4oC after reconstitution. For longer-term storage, aliquot and store at -20oC for up to six months. Do not repeatedly freeze and thaw.
DUSP23 antibody, Dual specificity protein phosphatase 23 antibody, dual specificity phosphatase 23 antibody, DUSP25 antibody, LDP 3 antibody, LDP3 antibody, MOSP antibody, RP11 190A12.1 antibody, VH1 like phosphatase Z antibody, VHZ antibody
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