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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 Antibodies (95) and many more products for this protein.
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Human DUSP10 Protein expressed in Escherichia coli (E. coli) - ABIN668018
Jeong, Yoon, Kim, Shim, Jung, Son, Ryu, Kim: Crystal structure of the catalytic domain of human MAP kinase phosphatase 5: structural insight into constitutively active phosphatase. in Journal of molecular biology 2006
Show all 2 references for ABIN668018
Increased Dusp10 expression is associated with better survival rate in colorectal cancer patients.
Data suggest that vitamin D receptor (show VDR Proteins) target genes (DUSP10; THBD (show THBD Proteins), thrombomodulin (show THBD Proteins); NRIP1 (show NRIP1 Proteins), nuclear receptor interacting protein 1 (show NRIP1 Proteins); TRAK1 (show TRAK1 Proteins), trafficking protein kinesin binding 1 (show TRAK1 Proteins)) 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 Proteins)-181 family members by miRNA inhibitors enhanced the expression of MKP-5 and suppressed the phosphorylation of p38 MAPK (show MAPK14 Proteins) after exposure to PAHs, which promotes cancer cell migration.
Data indicate that the activities of phosphoprotein phosphatases MKP5 and MKP7 (show DUSP16 Proteins) were determined in the system.
MKP-5 interacts with ERK (show EPHB2 Proteins), retains it in the cytoplasm, suppresses its activation and downregulates ERK (show EPHB2 Proteins)-dependent transcription.
A distinct interaction mode revealed by the crystal structure of the kinase p38alpha (show MAPK14 Proteins) with the MAPK (show MAPK1 Proteins) 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 Proteins) and ERK (show EPHB2 Proteins) pathways.
a function for ASC (show PYCARD Proteins) that is distinct from the inflammasome in modulating MAPK (show MAPK1 Proteins) activity and chemokine (show CCL1 Proteins) expression and further identify DUSP10 as a novel ASC (show PYCARD Proteins) 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 Proteins) activity
These results suggest that p38 (show CRK Proteins) phosphorylation is controlled by DUSP10 expression.
MAPK (show MAPK1 Proteins) 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 Proteins) activation in inflammatory responses.
a function for ASC (show STS Proteins) that is distinct from the inflammasome in modulating MAPK (show MAPK1 Proteins) activity and chemokine (show CCL1 Proteins) expression and further identify DUSP10 as a novel ASC (show STS Proteins) 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 Proteins)-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