Recombinant Human DUSP14 Protein (His & MBP Tag)

Name: Recombinant Human DUSP14 Protein (His & MBP Tag)
Brand: Beta LifeScience
SKU: BLPSN-1667
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	His&MBP
Host Species	Human
Accession	O95147
Synonym	MKP-L, MKP6
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 -…£. 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.
Description	A DNA sequence encoding the human DUSP14 (O95147) (Met 1 -His 191) was fused with an N-terminal His-tagged MBP tag at the N-terminus.
Source	E.coli
Predicted N Terminal	Met
AA Sequence	Met 1 -His 191
Molecular Weight	The recombinant human DUSP14/MBP fusion protein consists of 587 a.a. and has a calculated molecular mass of 65 kDa. It migrates as an approximately 60 kDa band in SDS-PAGE under reducing conditions.
Purity	>88% as determined by SDS-PAGE
Endotoxin	Please contact us for more information.
Bioactivity	Please contact us for detailed information
Formulation	Lyophilized from sterile PBS, pH 7.5.
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function	Involved in the inactivation of MAP kinases. Dephosphorylates ERK, JNK and p38 MAP-kinases.
Protein Families	Protein-tyrosine phosphatase family, Non-receptor class dual specificity subfamily
Database References	HGNC: 17007 OMIM: 606618 KEGG: hsa:11072 STRING: 9606.ENSP00000377910 UniGene: Hs.91448

Gene Functions References

Hepatocyte DUSP14 is required for maintaining hepatic metabolic homeostasis and for suppressing inflammation, a novel function that relies on constraining TAK1 hyperactivation PMID: 29077210
The AA genotype was associated with protection against active TB. Among disease-free individuals, T-helper type-1 related genes, IFNGR2 and STAT1 mRNA levels significantly increased as the number of A alleles of rs1051838 increased. PMID: 26938665
levels significantly decreased in failing hearts PMID: 26891723
these findings reveal a novel mechanism by which TRAF2 mediates Lys63-linked ubiquitination of DUSP14, leading to DUSP14 activation in T cells PMID: 26521044
findings suggest that DUSP14 negatively regulates TNF- or IL-1-induced NF-kappaB activation by dephosphorylating TAK1 at Thr-187 PMID: 23229544
DUSP14 may be a susceptibility gene for pulmonary tuberculosis. PMID: 22233810
The overproduction, purification and crystal structure at 1.88 A resolution of human dual-specificity phosphatase 14, DUSP14 (MKP6), are reported. PMID: 19770498
Activation of ATM by radiation down-regulates phospho-ERK1/2 and its downstream signaling via increased expression of mitogen-activated protein kinase phosphatase MKP-1. PMID: 17178844
The binding of Lipomannan to TLR2 triggers MAPK activation, followed by an up-regulation of MKP-1 expression, which in turn may act as a negative regulator of MAPK activation. PMID: 18201568

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.