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The antibody against DUSP14 was raised in rabbit using the Fusion protein of Human DUSP14 as the immunogen. This antibody exists as a non-conjugated isotype IgG, Antigen affinity purified. This antibody has been validated on ELISA, IHC.
The antibody against DUSP14 was raised in rabbit using the Fusion protein of Human DUSP14 as the immunogen. This antibody exists as a non-conjugated isotype IgG, Antigen affinity purified. This antibody has been validated on ELISA, IHC.
$299.00
| Cat.No | ADC-31978A | Clonality | Polyclonal |
|---|---|---|---|
| Host Species | Rabbit | Target Name | DUSP14 |
| Form | Liquid | Species Reactivity | Human, Mouse |
| Isotype | IgG | Storage Buffer | 0.05% NaN3, 40% Glycerol., pH7.4 PBS |
| Purification Method | Antigen affinity purified | Conjugate | Non-conjugated |
| Application | ELISA, IHC | Storage | Upon receipt |
| Immunogen Description | Fusion protein of Human DUSP14 | Target Species | Human |
|---|---|---|---|
| Immunogen Sequence | Complete sequences for the immunogen, target protein, and peptides are available upon request. | Uniprot ID | O95147 |
Uniprot Id
O95147
Target Species
Human
Target Name
DUSP14
Target Full Name
Dual specificity protein phosphatase 14
Target Function
Involved in the inactivation of MAP kinases. Dephosphorylates ERK, JNK and p38 MAP-kinases.
Target Protein Families
Protein-tyrosine phosphatase family, Non-receptor class dual specificity subfamily
Target Research Area
Signal Transduction
Target Synonyms
Dual specificity phosphatase 14; Dual specificity protein phosphatase 14; DUS14_HUMAN; DUSP 14; DUSP14; DUSP14 protein; MAP kinase phosphatase 6; Mitogen activated protein kinase phosphatase 6; Mitogen-activated protein kinase phosphatase 6; MKP 1 like protein tyrosine phosphatase; MKP 6; MKP L; MKP-1-like protein tyrosine phosphatase; MKP-6; MKP-L; MKP1 like protein tyrosine phosphatase; MKP6; MKPL
Target Background
Dual-specificity phosphatases (DUSPs) constitute a large heterogeneous subgroup of the type I cysteine-based protein-tyrosine phosphatase superfamily. DUSPs are characterized by their ability to dephosphorylate both tyrosine and serine/threonine residues. They have been implicated as major modulators of critical signaling pathways. DUSP14 contains the consensus DUSP C-terminal catalytic domain but lacks the N-terminal CH2 domain found in the MKP (mitogen-activated protein kinase phosphatase) class of DUSPs (see MIM 600714) (summary by Patterson et al., 2009 [PubMed 19228121]).
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