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SDS-PAGE

DUSP14 / MKP-6 recombinant protein

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

Gene Names
DUSP14; MKP6; MKP-L
Purity
> 88 % as determined by SDS-PAGE
Synonyms
DUSP14 / MKP-6; Recombinant Human DUSP14 / MKP-6 Protein (His & MBP tag); MKP-L; MKP6; DUSP14 / MKP-6 recombinant protein
Ordering
For Research Use Only!
Host
E Coli
Purity/Purification
> 88 % as determined by SDS-PAGE
Form/Format
Lyophilized from sterile PBS, pH 7.5
Sequence Length
198
Application Notes
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 Terminal
Met
Preparation and Storage
Samples are stable for up to twelve months from date of receipt at -70 degree C

SDS-PAGE

SDS-PAGE
Related Product Information for DUSP14 / MKP-6 recombinant protein
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. 

Description: 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.

NCBI and Uniprot Product Information

NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Accession #
Molecular Weight
22,255 Da
NCBI Official Full Name
dual specificity protein phosphatase 14
NCBI Official Synonym Full Names
dual specificity phosphatase 14
NCBI Official Symbol
DUSP14
NCBI Official Synonym Symbols
MKP6; MKP-L
NCBI Protein Information
dual specificity protein phosphatase 14
UniProt Protein Name
Dual specificity protein phosphatase 14
UniProt Gene Name
DUSP14
UniProt Synonym Gene Names
MKP6; MKP-L; MAP kinase phosphatase 6; MKP-6

NCBI Description

Dual-specificity phosphatases (DUSPs) constitute a large heterogeneous subgroup of the type I cysteine-based protein-tyrosine phosphatase superfamily. DUSPs are characterized by their ability to dephosphorylate both tyrosine and serine/threonine residues. They have been implicated as major modulators of critical signaling pathways. DUSP14 contains the consensus DUSP C-terminal catalytic domain but lacks the N-terminal CH2 domain found in the MKP (mitogen-activated protein kinase phosphatase) class of DUSPs (see MIM 600714) (summary by Patterson et al., 2009 [PubMed 19228121]).[supplied by OMIM, Dec 2009]

Uniprot Description

MKP-6: a member of the dual specificity protein phosphatase subfamily. These phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. They negatively regulate members of the mitogen-activated protein (MAP) kinase superfamily (ERK, JNK, p38). Is a negative regulator of T cell costimulation via CD28.

Protein type: EC 3.1.3.16; EC 3.1.3.48; Motility/polarity/chemotaxis; Protein phosphatase, dual-specificity

Chromosomal Location of Human Ortholog: 17q12

Molecular Function: protein binding

Research Articles on DUSP14 / MKP-6

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Product Notes

The DUSP14 / MKP-6 dusp14 (Catalog #AAA2545507) is a Recombinant Protein produced from E Coli and is intended for research purposes only. The product is available for immediate purchase. 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. Researchers should empirically determine the suitability of the DUSP14 / MKP-6 dusp14 for an application not listed in the data sheet. Researchers commonly develop new applications and it is an integral, important part of the investigative research process. It is sometimes possible for the material contained within the vial of "DUSP14 / MKP-6, Recombinant Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.

Precautions

All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.

Disclaimer

Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.

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