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Foot-and-mouth disease virus VP1 as an interferon (show IFNA Proteins)-suppressor by interacting with sorcin.
Sorcin is able to limit the toxic effects of the chemotherapeutic agent in the cell. In addition, Sorcin silencing increases cell death upon treatment with doxorubicin, increases the accumulation of doxorubicin in cell nucleus, decreases the expression of MDR1 and doxorubicin efflux via MDR1.
Sorcin overexpression in HCT116 cells resulted in a significant increase in cell migration and invasion. Sorcin stimulated epithelial-mesenchymal transition through activating PI3K (show PIK3CA Proteins)/Akt (show AKT1 Proteins) signaling.
The authors verified that NS5A of hepatitis C virus interacted with sorcin through domain I of NS5A, and phosphorylation of the threonine residue 155 of sorcin played a crucial role in protein interaction.
Drug resistance can be effectively reversed in cisplatin-resistance and adriamycin-resistant myeloma cells through delivery of siRNAs targeting sorcin.
Sorcin is highly expressed in the heart and in the brain, and overexpressed in many cancer cells. [Review]
Sorcin antibody as a possible predictive factor in conversion from radiologically isolated syndrome to multiple sclerosis: a preliminary study
Sorcin links calcium signaling to vesicle trafficking, regulates Polo-like kinase 1 and is necessary for mitosis.
Key cellular signaling pathways were triggered by sorcin silencing in the drug resistance of human nasopharyngeal carcinoma.
sorcin regulates epithelial-mesenchymal transition and cancer stem cells partly through E-cadherin (show CDH1 Proteins) and vascular endothelial growth factor (show VEGF Proteins) expression.
overexpression of sorcin increased the phosphorylation of CREB1 (show CREB1 Proteins) and the binding of CREB1 (show CREB1 Proteins) to the CRE sequence of mdr1/p-gp (show ABCB4 Proteins) promoter, and induced the expression of MDR1/P-gp (show ABCB4 Proteins)
Sorcin links pancreatic beta cells lipotoxicity to calcium stores and provides a target for intervention in type 2 diabetes.
Regulation of calcium signaling and cardiac contractility by miR-1 regulated sorcin expression plays a fundamental role in the maintenance of normal cardiac function and in the pathogenesis of cardiac dysfunction.
sorcin is a potent inhibitor of both spontaneous and ICa-triggered RyR (show RYR1 Proteins) activity and is kinetically capable of playing a role in terminating the positive feedback loop of Ca2 (show CA2 Proteins)+-induced Ca2 (show CA2 Proteins)+ release
Data further define the role of sorcin in cardiac excitation-contraction coupling and highlight its negative regulation of sarcoplasmic reticulum calcium release.
Interaction of calcium/calmodulin-dependent protein kinase IIdeltaC with sorcin indirectly modulates ryanodine receptor (show RYR3 Proteins) function in cardiac myocytes.
This gene encodes a calcium-binding protein with multiple E-F hand domains that relocates from the cytoplasm to the sarcoplasmic reticulum in response to elevated calcium levels. In addition to regulating intracellular calcium homeostasis it also modulates excitation-contraction coupling in the heart. Alternative splicing results in multiple transcript variants encoding distinct proteins. Multiple pseudogenes exist for this gene.
, 22 kDa protein
, calcium binding protein amplified in mutlidrug-resistant cells