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Dual specificity protein phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. Additionally we are shipping Dual Specificity Phosphatase 10 Proteins (7) and many more products for this protein.
Showing 10 out of 97 products:
Human Polyclonal DUSP10 Primary Antibody for WB - ABIN1881272
Tephly, Carter: Asbestos-induced MKP-3 expression augments TNF-alpha gene expression in human monocytes. in American journal of respiratory cell and molecular biology 2008
Show all 5 references for ABIN1881272
Human Polyclonal DUSP10 Primary Antibody for EIA, IHC (p) - ABIN360788
Tanoue, Moriguchi, Nishida: Molecular cloning and characterization of a novel dual specificity phosphatase, MKP-5. in The Journal of biological chemistry 1999
Show all 4 references for ABIN360788
Cow (Bovine) Polyclonal DUSP10 Primary Antibody for WB - ABIN2785082
Teng, Huang, Meng: Several dual specificity phosphatases coordinate to control the magnitude and duration of JNK activation in signaling response to oxidative stress. in The Journal of biological chemistry 2007
Human Polyclonal DUSP10 Primary Antibody for ELISA, WB - ABIN564881
Wang, Daouti, Li, Wen, Rizzo, Higgins, Packman, Rosen, Boylan, Heimbrook, Niu: Identification of the MEK1(F129L) activating mutation as a potential mechanism of acquired resistance to MEK inhibition in human cancers carrying the B-RafV600E mutation. in Cancer research 2011
Increased Dusp10 expression is associated with better survival rate in colorectal cancer patients.
Data suggest that vitamin D receptor (show VDR Antibodies) target genes (DUSP10; THBD (show THBD Antibodies), thrombomodulin (show THBD Antibodies); NRIP1 (show NRIP1 Antibodies), nuclear receptor interacting protein 1 (show NRIP1 Antibodies); TRAK1 (show TRAK1 Antibodies), trafficking protein kinesin binding 1 (show TRAK1 Antibodies)) can be used as markers for individual's response to vitamin D3 supplements.
Certain mutations in DUSP10 correlate with the incidence of colorectal cancer(CRC). Thus, the function of the DUSP10 gene product may contribute toward CRC in the Han Chinese population.
Single nucleotide polymorphism in DUSP10 gene is associated with celiac disease.
Depletion of miR (show MLXIP Antibodies)-181 family members by miRNA inhibitors enhanced the expression of MKP-5 and suppressed the phosphorylation of p38 MAPK (show MAPK14 Antibodies) after exposure to PAHs, which promotes cancer cell migration.
Data indicate that the activities of phosphoprotein phosphatases MKP5 and MKP7 (show DUSP16 Antibodies) were determined in the system.
MKP-5 interacts with ERK (show EPHB2 Antibodies), retains it in the cytoplasm, suppresses its activation and downregulates ERK (show EPHB2 Antibodies)-dependent transcription.
A distinct interaction mode revealed by the crystal structure of the kinase p38alpha (show MAPK14 Antibodies) with the MAPK (show MAPK1 Antibodies) binding domain of the phosphatase MKP5.
DUSPs 10 and 16 are positive regulators of activation, apparently acting by modulating cross-talk between the p38 (show CRK Antibodies) and ERK (show EPHB2 Antibodies) pathways.
a function for ASC (show PYCARD Antibodies) that is distinct from the inflammasome in modulating MAPK (show MAPK1 Antibodies) activity and chemokine (show CCL1 Antibodies) expression and further identify DUSP10 as a novel ASC (show PYCARD Antibodies) target.
DUSP10 regulates intestinal epithelial cell growth and colorectal tumorigenesis.
In mouse macrophages, MKP-5 down-regulates the release of inflammatory mediators by controlling p38 MAPK (show MAPK14 Antibodies) activity
These results suggest that p38 (show CRK Antibodies) phosphorylation is controlled by DUSP10 expression.
MAPK (show MAPK1 Antibodies) phosphotase 5 deficiency contributes to protection against blood-stage Plasmodium yoelii 17XL infection in mice.
MKP-5 is an essential negative regulator of the promyogenic actions of the MAPKs and may serve as a target to promote muscle stem cell function in the treatment of degenerative skeletal muscle diseases
MKP5 deficiency significantly reduces foam cell formation.
MKP5 is crucial to homeostatic regulation of MAPK (show MAPK1 Antibodies) activation in inflammatory responses.
a function for ASC (show STS Antibodies) that is distinct from the inflammasome in modulating MAPK (show MAPK1 Antibodies) activity and chemokine (show CCL1 Antibodies) expression and further identify DUSP10 as a novel ASC (show STS Antibodies) target.
MKP5 has a principal function in both innate and adaptive immune responses, and represents a novel target for therapeutic intervention of immune diseases
The results show an earlier unrecognized and non-redundant function of MKP-5 in restraining p38 MAPK (show MAPK14 Antibodies)-mediated neutrophil oxidant production, thereby preventing lipopolysaccharide-induced vascular injury.
Dual specificity protein phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. They negatively regulate members of the MAPK superfamily (MAPK/ERK, SAPK/JNK, p38), which is associated with cellular proliferation and differentiation. Different members of this family of dual specificity phosphatases show distinct substrate specificities for MAPKs, different tissue distribution and subcellular localization, and different modes of inducibility of their expression by extracellular stimuli. This gene product binds to and inactivates p38 and SAPK/JNK, but not MAPK/ERK. Its subcellular localization is unique\; it is evenly distributed in both the cytoplasm and the nucleus. This gene is widely expressed in various tissues and organs, and its expression is elevated by stress stimuli. Three transcript variants encoding two different isoforms have been found for this gene.
dual specificity protein phosphatase 10
, dual specificity phosphatase 10
, dual specificity protein phosphatase 10-like
, dual specificity phosphatase MKP-5
, map kinase phosphatase 5
, mitogen-activated protein kinase phosphatase 5
, serine/threonine specific protein phosphatase
, MAP kinase phosphatase 5