Rabbit anti-Human DUSP12 Polyclonal Antibody

Uniprot Id

Q9UNI6

Target Species

Human

Target Name

DUSP12

Target Full Name

Dual specificity protein phosphatase 12

Target Function

Dual specificity phosphatase; can dephosphorylate both phosphotyrosine and phosphoserine or phosphothreonine residues. Can dephosphorylate glucokinase (in vitro). Has phosphatase activity with the synthetic substrate 6,8-difluoro-4-methylumbelliferyl phosphate and other in vitro substrates.

Target Subcellular Location

Nucleus. Cytoplasm, cytosol.

Target Protein Families

Protein-tyrosine phosphatase family, Non-receptor class dual specificity subfamily

Target Tissue Specificity

Ubiquitous, highest expression in spleen, testis, ovary, and peripheral blood leukocytes and lower expression in liver and lung.

Target Synonyms

Dual specificity phosphatase 12; Dual specificity protein phosphatase 12; Dual specificity tyrosine phosphatase YVH1; DUS12_HUMAN; DUSP 1; DUSP 12; DUSP1; DUSP12; Serine/threonine specific protein phosphatase; TDSP4; YVH 1; YVH1; YVH1 protein tyrosine phosphatase (S. cerevisiae) ortholog; YVH1 protein tyrosine phosphatase ortholog

Target Background

The protein encoded by this gene is a member of the dual specificity protein phosphatase subfamily. These phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. They negatively regulate members of the mitogen-activated protein (MAP) kinase superfamily (MAPK/ERK, SAPK/JNK, p38), which is associated with cellular proliferation and differentiation. Different members of the family of dual specificity phosphatases show distinct substrate specificities for various MAP kinases, different tissue distribution and subcellular localization, and different modes of inducibility of their expression by extracellular stimuli. This gene product is the human ortholog of the Saccharomyces cerevisiae YVH1 protein tyrosine phosphatase. It is localized predominantly in the nucleus, and is novel in that it contains, and is regulated by a zinc finger domain.