Fagus Antibody Services

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

£684.00£855.00 excluding VAT

SKU FAS-030837-P Category Tag

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. 

Size

100µg

Active Protein
Activity
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.

Sequence

Met 1 –His 191

Fusion Tag

N-His & MBP

Accession

O95147

Species

Human

Expressed Host

E.coli

Shipping

This product is provided as lyophilized powder which is shipped with ice packs.

Purity

> 88 % as determined by reducing SDS-PAGE.

Endotoxin

Please contact us for more information.

Stability and Storage

Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

Mol Mass

65 kDa

AP Mol Mass

60 kDa

Formulation

Lyophilized from sterile PBS, pH 7.5

Research Areas

Signal Transduction

Reconstitution

Please refer to the printed manual for detailed information.

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