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Human Polyclonal DUSP3 Primary Antibody for IHC (p), ELISA - ABIN545101
Todd, Tanner, Denu: Extracellular regulated kinases (ERK) 1 and ERK2 are authentic substrates for the dual-specificity protein-tyrosine phosphatase VHR. A novel role in down-regulating the ERK pathway. in The Journal of biological chemistry 1999
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Human Polyclonal DUSP3 Primary Antibody for IHC (p), ELISA - ABIN545053
Alonso, Saxena, Williams, Mustelin: Inhibitory role for dual specificity phosphatase VHR in T cell antigen receptor and CD28-induced Erk and Jnk activation. in The Journal of biological chemistry 2001
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Human Polyclonal DUSP3 Primary Antibody for IHC (p), WB - ABIN392924
Wang, Yeh, Chou, Yang, Fu, Chen, Cheng, Huang, Liu, Huang, Chen: Vaccinia H1-related phosphatase is a phosphatase of ErbB receptors and is down-regulated in non-small cell lung cancer. in The Journal of biological chemistry 2011
Human Monoclonal DUSP3 Primary Antibody for IP, WB - ABIN532715
Ishibashi, Bottaro, Chan, Miki, Aaronson: Expression cloning of a human dual-specificity phosphatase. in Proceedings of the National Academy of Sciences of the United States of America 1993
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Nuclear HSP70 leads to enhancement of vaccinia H1-related phosphatase (VHR) activity via protein-protein interaction rather than its molecular chaperone activity, thereby suppressing excessive ERK activation. Downregulation of either VRK3 or HSP70 rendered cells vulnerable to glutamate-induced apoptosis.
Data indicated that regulating non-receptor tyrosine kinase FAK and cell migration is a newly revealed function of VHR/DUSP3.
The loss of DUSP3 activity markedly increases gamma radiation-induced DNA strand breaks, suggesting a potential novel role for DUSP3 in DNA repair.
In PTP1B and VHR, two new allosteric clusters were identified in each enzyme.
In the phosphatase-silenced cells, the normal bipolar spindle structure was restored by chemical inhibition of Erk1/2 and ectopic overexpression of Dusp3. We propose that at M phase Dusp3 keeps Erk1/2 activity in check to facilitate normal mitosis.
Data suggest levels of gene expression of both DUSP3 (dual specificity phosphatase 3) and PSME3 (proteasome activator subunit 3) are associated with susceptibility to Staphylococcus aureus infection/sepsis in humans and in mouse disease model.
Our results demonstrate that DUSP3 plays a key and nonredundant role as a regulator of innate immune responses
VHR can dimerize inside cells, and that VHR catalytic activity is reduced upon dimerization.
DUSP3 is a pro-angiogenic atypical dual-specificity phosphatase.
DUSP3 interacting partners are nucleolar proteins involved in processes related to DNA repair and senescence.
we report the first successful site-specific incorporation of sulfotyrisine into VHR through the use of expanding genetic code
Proteins containing the class II motifs are efficient VHR substrates in vitro, suggesting that VHR may act on a novel class of yet unidentified Tyr(P) proteins in vivo.
Enteric commensal bacteria induce extracellular signal-regulated kinase pathway signaling via formyl peptide receptor-dependent redox modulation of dual specific phosphatase 3
VHR expression enhances the signaling of ErbB receptors and may be involved in NSCLC pathogenesis.
VHR, a Vaccinia virus VH1-related dual-specific protein phosphatase, is phosphorylated at Y138 by ZAP-70.
VHR is required for cell-cycle progression as it modulates MAP kinase activation in a cell-cycle phase-dependent manner.
deregulated expression of BRCA1-IRIS is likely to reduce dependence on normal physiological growth stimuli
Small dual-specificity phosphatase VHR selectively dephosphorylates tyrosine-phosphorylated interferon-alpha- and beta-activated transcription factor STAT5, leading to the subsequent inhibition of STAT5 function.
Results highlight the importance of a high intracellular Zn(2+) content and the VHR/ZAP-70/ERK1,2-associated pathways in the modulation of LNCaP prostate cancer cell growth.
VHR can be considered as a new marker for cancer progression in cervix carcinoma and potential new target for anticancer therapy
DUSP3 phosphatase plays a key role in metastatic growth.
At the molecular level, DUSP3 deletion was associated with estrogen-dependent decreased phosphorylation of ERK1/2 and Akt in peritoneal macrophages stimulated ex vivo by LPS; results demonstrate that estrogens may modulate M2-like responses during endotoxemia in a DUSP3-dependent manner
Data suggest levels of gene expression of both Dusp3 (dual specificity phosphatase 3) and Psme3 (proteasome activator subunit 3) are associated with susceptibility to Staphylococcus aureus infection/sepsis in humans and in mouse disease model.
Platelets from DUSP3-deficient mice displayed a selective impairment of aggregation and granule secretion.
The protein encoded by this gene is 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 (MAPK/ERK, SAPK/JNK, p38), which are associated with cellular proliferation and differentiation. Different members of the family of dual specificity phosphatases show distinct substrate specificities for various MAP kinases, different tissue distribution and subcellular localization, and different modes of inducibility of their expression by extracellular stimuli. This gene maps in a region that contains the BRCA1 locus which confers susceptibility to breast and ovarian cancer. Although DUSP3 is expressed in both breast and ovarian tissues, mutation screening in breast cancer pedigrees and in sporadic tumors was negative, leading to the conclusion that this gene is not BRCA1.
dual specificity phosphatase 3 (vaccinia virus phosphatase VH1-related)
, dual specificity phosphatase 3
, dual specificity protein phosphatase 3
, dual specificity protein phosphatase VHR
, serine/threonine specific protein phosphatase
, vaccinia H1-related phosphatase
, vaccinia virus phosphatase VH1-related