DUSP14 / MKP-6 Protein (MBP Tag)

Dual specificity phosphatase 14 Protein Datasheet

DUSP14 / MKP-6 Protein Product Information

• Synonym: MKP-L, MKP6
• 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.
• Source: Human
• Expression Host: E.coli

DUSP14 / MKP-6 Protein QC Testing

• Purity: > 88 % as determined by SDS-PAGE.
• Endotoxin: Please contact us for more information.
• Stability: Samples are stable for up to twelve months from date of receipt at -70℃
• Predicted N terminal: Met
• Molecular Mass: 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 60kDa band in SDS-PAGE under reducing conditions.
• Formulation: Lyophilized from sterile PBS, pH7.5
  1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
  2. Please contact us for any concerns or special requirements.
• SDS-PAGE: DUSP14 / MKP-6 protein

DUSP14 / MKP-6 Protein Usage Guide

• Storage: Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
• Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

DUSP14 / MKP-6 Protein Description

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.

References

1. Yoshihara Y. et al., 1996, J Neurobiol. 28 (1): 51-69.
2. Klinger S. et al., 2008, Diabetes. 57 (3): 584-93.
3. Park JE. et al., 2009, Biochem Biophys Res Commun. 387 (4): 795-9.