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.

推荐稀释比 IHC:1/50-1/100

Immunohistochemistry analysis of paraffin-embedded Human esophagus cancer using DUSP14 antibody. High-pressure and temperature Sodium Citrate pH 6.0 was used for antigen retrieval.

-25 ~ -15℃保存，收到货之后有效期1年，避免反复冻融。