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Data show that the intracellular domain of PAPC interacts with Sprouty (Spry), and upon binding to PAPC, Spry function is inhibited and PCP signaling is enhanced.
Here we show that Xenopus laevis Sprouty2 (XSpry2) controls the duration of ERK (show MAPK1 Proteins) activity and thereby contributes to the establishment of dorsoventral patterning during mesoderm formation.
Overexpression of miR (show MLXIP Proteins)-592 promotes GC proliferation, migration, and invasion and induces the EMT (show ITK Proteins) via the PI3K (show PIK3CA Proteins)/AKT (show AKT1 Proteins) and MAPK/ERK (show MAPK1 Proteins) signaling pathways by inhibiting Spry2, suggesting a potential therapeutic target for Gastric cancer.
nuclear Spry2 acts as a molecular link which co-ordinates airway and vascular growth of the cardiopulmonary system.
activation of ERK1/2 signaling was required for hCG-induced up-regulation of SPRY2 expression. Further, SPRY2 knockdown attenuated the AREG-induced COX-2 expression and PGE2 production by inhibiting AREG-activated ERK1/2 signaling.
Result demonstrated that SPRY2 low-expression was significantly associated with unfavorable prognosis of gastric adenocarcinoma and that SPRY2 could inhibit FGFR2 (show FGFR2 Proteins)-induced ERK (show EPHB2 Proteins) phosphorylation and suppress FGFR2 (show FGFR2 Proteins)-elicited gastric cancer cell proliferation and invasion.
Sprouty2 inhibits amphiregulin (show AREG Proteins)-induced down-regulation of E-cadherin (show CDH1 Proteins) and cell invasion in human ovarian cancer cells.
Sprouty2 (Spry2), a negative regulator of the extracellular signal regulated kinase/mitogen-activated protein kinase (show MAPK1 Proteins) (Erk/MAPK (show MAPK1 Proteins)) signalling pathway, was a downstream target of miR (show MLXIP Proteins)-122-5p possibly involved in regulating the keratinocyte proliferation.
results shows the involvement of Spry2 in regulation of FosB (show FOSB Proteins) and Runx2 (show RUNX2 Proteins) genes, MAPK (show MAPK1 Proteins) signaling and proliferation of mesenchymal stem cells.
MYB (show MYB Proteins) acts on MAPK (show MAPK1 Proteins) signaling by directly regulating transcription of the gene encoding the negative modulator SPRY2.
ZEB1 upregulation by SPRY2 results from the combined induction of ETS1 transcription factor and the repression of microRNAs (miR-200 family, miR-150) that target ZEB1 RNA. Moreover, SPRY2 increased AKT activation by epidermal growth factor, whereas AKT and also Src inhibition reduced the induction of ZEB1.
upregulated in human CRC (show CALR Proteins). Suppression of SPRY2 repressed AKT2 (show AKT2 Proteins) and EMT (show ITK Proteins)-inducing transcription factors and significantly increased E-cadherin (show CDH1 Proteins) expression. Concurrent downregulation of SPRY1 (show SPRY1 Proteins) and SPRY2 also increased E-cadherin (show CDH1 Proteins) and suppressed mesenchymal markers in colon cancer cells.
These results identify Spry2 as a critical regulator of endochondral bone formation that modulates signaling in both osteoblast and chondrocyte lineages.
Spry2 is a novel unfolded protein response target and its upregulation is dependent on PERK (show EIF2AK3 Proteins). Knockdown of Spry2 resulted in reduced expression of Serca2 (show ATP2A2 Proteins), reduced endoplasmic reticulum calcium levels, and induction of the UPR. Spry2 deletion in the adult mouse beta-cell caused hyperglycemia and hypoinsulinemia.
these results establish SPRY2 as a critical negative regulator of BCR (show BCR Proteins)-mediated MAPK-Erk (show MAPK1 Proteins) signaling in chronic lymphocytic leukemia , thereby providing one of the molecular mechanisms to explain the clinical heterogeneity of chronic lymphocytic leukemia.
In the present study, it is demonstrated that Spry2 and -4 participate in KA induced neurodegeneration possibly through inhibition of ERK (show EPHB2 Proteins) signaling.
Study revealed that suppression of Spry2 expression induced proliferation and differentiation of osteoblastic cells upon bFGF (show FGF2 Proteins) and EGF (show EGF Proteins) stimulation, whereas it diminished proliferation of gingival epithelial cells.
Cosuppression of Sprouty and Sprouty-related negative regulators of FGF signalling in prostate cancer
in embryos with lower Spry2;Spry4 (show SPRY4 Proteins) gene dosages, we observed a non-fusion of original R2 and M1 Shh (show SHH Proteins) signaling domains with consequent formation of a supernumerary tooth primordium from the isolated R2 bud
The data showed enhanced axon outgrowth and improved long-distance axon regeneration in sprouty2 deficient mice
Sprouty2 acts as an inhibitor of CrkL-Rap1 signaling.
This gene encodes a protein belonging to the sprouty family. The encoded protein contains a carboxyl-terminal cysteine-rich domain essential for the inhibitory activity on receptor tyrosine kinase signaling proteins and is required for growth factor stimulated translocation of the protein to membrane ruffles. In primary dermal endothelial cells this gene is transiently upregulated in response to fibroblast growth factor two. This protein is indirectly involved in the non-cell autonomous inhibitory effect on fibroblast growth factor two signaling. The protein interacts with Cas-Br-M (murine) ectropic retroviral transforming sequence, and can function as a bimodal regulator of epidermal growth factor receptor/mitogen-activated protein kinase signaling. This protein may play a role in alveoli branching during lung development as shown by a similar mouse protein.
protein sprouty homolog 2
, sprouty 2