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NKp65 (show KLRF2 Proteins) utilizes a hemi-immunoreceptor tyrosine-based activation motif -like motif for cellular activation that requires Syk, although Syk appears not to be recruited to NKp65 (show KLRF2 Proteins).
Syk is a key regulator of Hoxa9 (show HOXA9 Proteins)/Meis1 (show MEIS1 Proteins)-driven acute myeloid leukemia (show BCL11A Proteins).
Data show that spleen tyrosine kinase (SYK) and proto-oncogene (show RAB1A Proteins) protein c-akt (AKT1 (show AKT1 Proteins)) proteins were increased in the cytoplasm of the cells forming Mallory-Denk bodies.
B cell receptor signaling component, SYK, caused PAX5 (show PAX5 Proteins) tyrosine phosphorylation in vitro and in cells. Transcriptional repression on the BLIMP1 (show PRDM1 Proteins) promoter by PAX5 (show PAX5 Proteins) was attenuated by this phosphorylation.
Pharmacological inhibitors of SYK activity significantly reduced the engulfment of oxLDL microbeads in the presence of serum factors, but had little effect on IgG phagocytosis.
our data strongly suggest that AQCA-mediated suppression of inflammatory responses could be managed by a direct interference of signaling cascades including IRAK (show IRAK1 Proteins) and Syk, linked to the activation of NF-kappaB (show NFKB1 Proteins) and AP-1 (show FOSB Proteins).
a potential link between the upregulation of Syk and VEGF-C (show VEGFC Proteins) expression and lung adenocarcinoma.
The lack of Syk mRNA expression in lung cancer play an important role in angiogenesis.
Overall novel mutations in SYK gene and in silico analysis revealed that these mutations are crucial and might be responsible for altered expression of SYK.
this study shows that SYK increased MUC5AC expression via ERK2 (show MAPK1 Proteins) and p38 MAPK (show MAPK14 Proteins) signaling pathways in airway epithelial cells
Pharmacological Syk inhibition might provide a safe therapeutic strategy to prevent arterial thrombosis and to limit infarct progression in acute stroke.
Studies indicate that SHP1 (show PTPN6 Proteins) and SYK crosstalk as a critical regulator of MyD88 (show MYD88 Proteins) post-translational modifications and IL-1 (show IL1A Proteins)-driven inflammation.
dephosphorylation of Tyr (show TYR Proteins)(P)(346) may be considered an important "checkpoint" in the regulation of Syk activation process. Putative biological functions of TULA-2 (show STS1 Proteins)-mediated dephosphorylation of Tyr (show TYR Proteins)(P)(346) may include deactivation of receptor-activated Syk or suppression of Syk activation by suboptimal stimulation.
These studies define a pathologic role for myeloid Syk signaling in renal ischemia/reperfusion injury
Torreya nucifera butanol fraction exhibits anti-inflammatory activities by direct inhibition of macrophage Src (show SRC Proteins)/Syk/NF-kappaB (show NFKB1 Proteins) and IRAK1 (show IRAK1 Proteins)/AP-1 (show JUN Proteins) signaling.
Dectin-1 (show CLEC7A Proteins) and Dectin-2 (show CLEC6A Proteins) seem not to play a major role in Borrelia recognition or Borrelia-induced inflammation. However, Syk seems to be involved in Borrelia-induced cytokine production
TNF (show TNF Proteins) activates Mule by inducing the dissociation of Mule from its inhibitor ARF. Inhibition of Mule phosphorylation by silencing Syk prevents this, thereby inhibiting Mule E3 ligase activity and TNF (show TNF Proteins)-induced JNK (show MAPK8 Proteins) activation and cell death.
The effects of OXSI-2 identified in this study provide context for the role of Syk in inflammasome signaling and demonstrate its importance in oxidative signaling upstream of inflammasome activation and downstream of ion flux.
Mincle (show CLEC4E Proteins) Activation and the Syk/Card9 (show CARD9 Proteins) Signaling Axis Are Central to the Development of Autoimmune Disease of the Eye
Syk deletion in myeloid cells is protective in mouse nephrotoxic serum nephritis.
These data suggest that Syk mRNA expression dynamics is closely related to bovine leukemia virus-induced disease.
This gene encodes a member of the family of non-receptor type Tyr protein kinases. This protein is widely expressed in hematopoietic cells and is involved in coupling activated immunoreceptors to downstream signaling events that mediate diverse cellular responses, including proliferation, differentiation, and phagocytosis. It is thought to be a modulator of epithelial cell growth and a potential tumour suppressor in human breast carcinomas. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
Tyrosine-protein kinase SYK
, tyrosine-protein kinase SYK
, protein-tyrosine kinase