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Human GSK3 alpha Protein expressed in Escherichia coli (E. coli) - ABIN411907
Edwards: Neisseria gonorrhoeae survival during primary human cervical epithelial cell infection requires nitric oxide and is augmented by progesterone. in Infection and immunity 2010
Human GSK3 alpha Protein expressed in HEK-293 Cells - ABIN2722263
Dunning, McGauran, Willén, Gouras, OConnell, Linse: Direct High Affinity Interaction between Aβ42 and GSK3α Stimulates Hyperphosphorylation of Tau. A New Molecular Link in Alzheimer's Disease? in ACS chemical neuroscience 2016
Using integrated analysis of genome-wide short hairpin RNA (shRNA) screening data in combination with genome-wide gene expression data, the study identified GSK3 as one of the key factors in p53 (show TP53 Proteins)-mediated apoptosis in human lung cancer cells.
demonstrated that GSK-3alpha is regulated by CREB (show CREB1 Proteins) in lung cancer and is required for the cell viability. These findings implicate CREB (show CREB1 Proteins)-GSK-3alpha axis as a novel therapeutic target for lung cancer treatment
GSK3 acts through APC motifs R2 and B to regulate APC:Axin interactions, promoting high-throughput of betacatenin to destruction.
reveals that GSK-3alpha- and GSK-3beta-regulated pathways can be responsible for stepwise transition to myelodysplastic syndromes and subsequent acute myeloid leukemia (show BCL11A Proteins)
CHP3 (show TESC Proteins) functions as a novel negative regulator of cardiomyocyte hypertrophy via inhibition of GSK3alpha/beta phosphorylation.
Elevated GSK3 protein kinase activity is associated with non-small cell lung carcinoma
GSK3A is redundant with GSK3B in regulating drug-resistance and chemotherapy-induced necroptosis
ER stress-PERK-GSK3alpha/beta signaling promotes proatherogenic macrophage lipid accumulation
glycogen synthase kinase 3 alpha and beta activity is increased in foetal membranes after term and preterm labour
TRAIL-induced apoptosis in pancreatic ductal adenocarcinoma cell lines is enhanced by pharmacological inhibition of glycogen synthase kinase-3 (GSK-3) or by shRNA-mediated depletion of either GSK-3alpha or GSK-3beta.
GSK3 is regulated through mechanisms independent of N-terminal serine phosphorylation in order for beta-catenin (show CTNNB1 Proteins) to be stabilized.
The expression of PI3K-insensitive GSK3 stimulates the production of adiponectin and protects from diet-induced metabolic syndrome.
Gsk3 play a role in the maintenance of DNA methylation (show HELLS Proteins) at a majority of the imprinted loci in embryonic stem cells
Sperm GSK3A is essential for male fertility.
The absence of oocyte GSK3 isoforms in the periconceptional period does not alter fertility yet causes offspring cardiac hyperplasia, cardiovascular defects, and significant neonatal death.
results support the model that GSK3 activity status is regulated by the circadian clock and that GSK3 feeds back to regulate the molecular clock amplitude in the suprachiasmatic nucleus
Gsk3-deleted neurons expressing upper layer markers exhibited striking migration failure in all areas of the cortex.
PI3K/AKT-mediated inhibitory phosphorylation of GSK3 limits the regenerative outcome after peripheral nerve injury.
double-knockout embryonic stem cells, as well as GSK-3beta(-/-) mouse embryonic fibroblast cells in which GSK-3alpha was knocked down to demonstrate that both isoforms of GSK-3, GSK-3alpha and GSK-3beta, are required for antiviral immune response.
GSK3A serine phosphorylation was positively correlated with embryo development
signal pathways converged on inhibitory phosphorylation of glycogen synthase kinase-3beta, decreasing tau phosphorylation
A mechanism whereby LRP6 (show LRP6 Proteins) stabilizes beta-catenin (show CTNNB1 Proteins) independently of Axin (show AXIN1 Proteins) degradation by directly inhibiting GSK3's phosphorylation of beta-catenin (show CTNNB1 Proteins), is identified.
we demonstrate that PKA, PKC (show FYN Proteins) and PI3K pathways crosstalk in porcine male germ cells to crucially regulate GSK3A phosphorylation which subsequently controls cell motility.
lycogen synthase kinase-3 (GSK3) was identified as a substrate of protein kinase c delta (show PKCd Proteins) in breast cancer cells.
GSK3alpha, but not GSK3beta, is necessary in cardiomyocyte survival
This gene encodes a multifunctional Ser/Thr protein kinase that is implicated in the control of several regulatory proteins including glycogen synthase, and transcription factors, such as JUN. It also plays a role in the WNT and PI3K signaling pathways, as well as regulates the production of beta-amyloid peptides associated with Alzheimer's disease.
glycogen synthase kinase-3 alpha
, glycogen synthase kinase 3 alpha
, GSK-3 alpha
, serine/threonine-protein kinase GSK3A
, factor A