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 ?. PTP inhibitor binds to the catalytic site of DUSP14. PTP inhibitor ? 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.
Product Name:
Human DUSP14/MKP-6 Recombinant Protein (RPES2740)
Product Code:
RPES2740
Size:
20µg
Species:
Human
Expressed Host:
E.coli
Synonyms:
MKP-L,MKP6
Accession:
O95147
Sequence:
Met 1 –His 191
Fusion tag:
N-His & MBP
Endotoxin:
Please contact us for more information.
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.
Purity:
> 88 % as determined by reducing SDS-PAGE.
Mol Mass:
65 kDa
AP Mol Mass:
60 kDa
Formulation:
Lyophilized from sterile PBS, pH 7.5
Shipping:
This product is provided as lyophilized powder which is shipped with ice packs.
Stability and Storage:
Lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.
system_update_alt데이터시트Human Syntaxin-6/STX6 Recombinant Protein Syntaxin-6 (STX6) is a single-pass type IV membrane protein, which belongs to the Syntaxin family. STX6 is mainly localized in the
