About DUSP14
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]).[supplied by OMIM, Dec 2009]

About DyLight 350
DyLight™ 350 has an excitation peak of 353 nm and an emission peak of 432 nm. It is spectrally similar to Alexa Fluor™ 350, iFluor® 350, AMCA, and Thioflavin T. DyLight™ 350 is most commonly used in flow cytometery and fluorescence microscopy applications.