|Other Accession||Q17QM8, NP_008957.1|
|Other Names||Dual specificity protein phosphatase 14, MKP-1-like protein tyrosine phosphatase, MKP-L, Mitogen-activated protein kinase phosphatase 6, MAP kinase phosphatase 6, MKP-6, DUSP14, MKP6|
|Target/Specificity||The synthetic peptide sequence is selected from aa 91-105 of HUMAN DUSP14|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Involved in the inactivation of MAP kinases. Dephosphorylates ERK, JNK and p38 MAP-kinases.|
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Provided below are standard protocols that you may find useful for product applications.
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]).
Thye, T., et al. Nat. Genet. 42(9):739-741(2010)
Lountos, G.T., et al. Acta Crystallogr. D Biol. Crystallogr. 65 (PT 10), 1013-1020 (2009) :
Patterson, K.I., et al. Biochem. J. 418(3):475-489(2009)
Elass, E., et al. FEBS Lett. 582(3):445-450(2008)
Nyati, M.K., et al. Cancer Res. 66(24):11554-11559(2006)
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