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Human DUSP14 / MKP-6 Protein (His & MBP Tag)

MKP-L,MKP6

Catalog Number P12443-H10E
Organism Species Human
Host E. coli
Synonyms MKP-L,MKP6
Molecular Weight The recombinant human DUSP14/MBP fusion protein consists of 587 amino acids and has a calculated molecular mass of 65 kDa. It migrates as an approximately 60 kDa band in SDS-PAGE under reducing conditions.
predicted N Met
SDS-PAGE
Purity > 88 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the human DUSP14 (O95147) (Met 1 –His 191) was fused with an N-terminal polyhistidine-tagged MBP tag at the N-terminus.
Bio-activity
Research Area Signaling |Signal Transduction |Protein Phosphorylation |Tyrosine Phosphatase
Formulation Lyophilized from sterile PBS, pH 7.5
1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background Dual specific phosphatase 14 / MAP-kinase phophatase-6 (DUSP14 / MKP6) is a member of Dual-specificity phosphatases that is a subclass of protein tyrosine phosphatases (PTP) families that can dephosphorylate bothe phosphotyrosine and phosphoserine / phosphothreonine residues in substrates. Unlike many other DUSPs, DUSP14 only contains a catalytic domain within the C-terminal region. In signal transduction, DUSP14 has been considered as negative regulator of the mitogen-activated protein kinase (MAPK) / extracellular signal-regulated kinase 1 / 2 (ERK 1 / 2) pathway. DUSP14 phosphatase activity has been confirmed to be inhibited by PTP inhibitor Ⅳ. PTP inhibitor binds to the catalytic site of DUSP14. PTP inhibitor Ⅳ effectively and specifically inhibited DUSP14-mediated dephosphorylation of JNK, a member of the mitogen-activated protein kinase (MAPK) family through dephosphorylation of both the Ser / Thr and Tyr residues of MAPKs. 
Reference
  • Yoshihara Y, et al. (1996) Overlapping and differential expression of BIG-2, BIG-1, TAG-1, and F3: four members of an axon-associated cell adhesion molecule subgroup of the immunoglobulin superfamily. J Neurobiol. 28 (1): 51-69.
  • Klinger S, et al. (2008) Increasing GLP-1-induced beta-cell proliferation by silencing the negative regulators of signaling cAMP response element modulator-alpha and DUSP14. Diabetes. 57 (3): 584-93.
  • Park JE, et al. (2009) PTP inhibitor IV protects JNK kinase activity by inhibiting dual-specificity phosphatase 14 (DUSP14). Biochem Biophys Res Commun. 387 (4): 795-9.