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The protein encoded by DUSP2 is a member of the dual specificity protein phosphatase subfamily. Additionally we are shipping DUSP2 Kits (2) and and many more products for this protein.
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Authors report that hypoxia-mediated downregulation of the dual specificity phosphatase 2 (DUSP2) is critical for the accumulation of CSC in colorectal cancer.
Hypoxia inhibits DUSP2 expression in colon cancer, leading to up-regulation of IL-8 (show IL8 Antibodies), which facilitates angiogenesis and tumour metastasis.
Our data show that aberrant epigenetic inactivation of DUSP2 occurs in carcinogenesis and that CTCF (show CTCF Antibodies) is involved in the epigenetic regulation of DUSP2 expression.
Highly recurrent mutation of DUSP2 is associated with nodular lymphocyte predominant Hodgkin lymphoma.
Data show that hypoxia promotes lapatinib resistance in ERBB2 (show ERBB2 Antibodies)-positive breast cancer cells through activation of the MEK (show MAP2K1 Antibodies)-ERK (show EPHB2 Antibodies) pathway a HIF-1 (show HIF1A Antibodies)-dependent manner via regulation of dual-specificity phosphatase 2 (DUSP2).
DUSP2 is an important molecule in endometrial physiology and that hypoxia-inhibited DUSP2 expression is a critical factor for the development of endometriosis.
Dipyridamole reduced expression of PAC-1 (show ADCYAP1R1 Antibodies) and CD62p (show SELP Antibodies) in patients with malignant lymphoma.
DUSP2 is a key downstream regulator of HIF-1 (show HIF1A Antibodies)-mediated tumor progression and chemoresistance
During apoptosis, p53 (show TP53 Antibodies) activates transcription of PAC1 (show ADCYAP1R1 Antibodies) by binding to a palindromic site in the PAC1 (show ADCYAP1R1 Antibodies) promoter
relationships between the expression levels of CD61 (show ITGB3 Antibodies), CD63 (show CD63 Antibodies), and PAC-1 (show ADCYAP1R1 Antibodies) on the platelet surface and the incidences of acute rejection and tubular necrosis as well as the recovery of graft function after renal transplantation
Data indicate that dual specificity phosphatase 2 protein (DUSP2) is a true STAT3 (show STAT3 Antibodies) transcription factor phosphatase that modulates the development of TH17 cells in the autoimmune response and inflammation.
DUSP2 plays no role in regulating obesity-associated inflammation and only a minor role in controlling insulin (show INS Antibodies) sensitivity following high-fat diet in female, but not male, mice.
the expression of PAC1 in the thymus changes in reverse ratio with thymus index and in direct ratio with cell apoptosis and only low dose of PACAP had positive effects against the CPS-induced thymus atrophy.
Arg294 and Arg295 play an important role in PAC-1 (show ADCYAP1R1 Antibodies) catalytic activation induced by ERK2 (show MAPK1 Antibodies) binding
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 product inactivates ERK1 and ERK2, is predominantly expressed in hematopoietic tissues, and is localized in the nucleus.
dual specificity protein phosphatase 2
, dual specificity protein phosphatase PAC-1
, dual-specificity phosphatase 2
, serine/threonine specific protein phosphatase