GSK3 (Glycogen Synthase Kinase-3 differs from most serine/threonine kinases) in that it is active in the absence of the action of signaling pathways. Two isoforms exist, GSK-3a and GSK-3ß. The function of GSK-3 is to phosphorylate glycogen synthase and thereby inactivate it. Insulin action stimulates the PI 3-kinase pathway, resulting in Akt activation, which phosphorylates and inactivates GSK-3.
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Primary antibody说明GSK3 (Glycogen Synthase Kinase-3 differs from most serine/threonine kinases) in that it is active in the absence of the action of signaling pathways. Two isoforms exist, GSK-3a and GSK-3ß. The function of GSK-3 is to phosphorylate glycogen synthase and thereby inactivate it. Insulin action stimulates the PI 3-kinase pathway, resulting in Akt activation, which phosphorylates and inactivates GSK-3.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Use at an assay dependent concentration. PubMed: 22003387
Use at an assay dependent concentration. Predicted molecular weight: 52 kDa.
Use at an assay dependent concentration. 1/100 for 10 min at RT. Staining of formalin-fixed tissues requires boiling tissue sections in 10mM citrate, pH 6.0 for 10 min followed by cooling at RT for 20 min.
相关性Glycogen synthase kinase 3 (GSK3) is a proline directed serine threonine kinase that was initially identified as a phosphorylating and inactivating glycogen synthase, a key enzyme in glycogen metabolism. Since then, it has been shown to be involved in the regulation of a diverse array of cellular functions, including protein synthesis, cell proliferation, cell differentiation, microtubule assembly/disassembly, and apoptosis. GSK3s substrate specificity is unique in that phosphorylation of substrate only occurs if a phosphoserine or phosphotyrosine is present four residues C terminal to the site of GSK phosphorylation.
There exists two isoforms of GSK3, alpha and beta, and they show a high degree of amino acid homology. The two isoforms of GSK3 are strictly regulated via phosphorylation. Phosphorylation of GSK3 beta on Ser9 (Ser21 in GSK3 alpha) by protein kinase B (PKB) causes its inactivation is the primary mechanism responsible for growth factor inhibition of this kinase. Activation of GSK3 beta is dependent upon the phosphorylation of Tyr216 (Tyr279 in GSK3 alpha). Upon activation, it has been shown to phosphorylate a number of different cellular proteins, including p53, c-Myc, c-Jun, heat shock factor 1 (HSF1), and cyclin D1. GSK3 beta also has been shown to phosphorylate aberrant sites on the microtubule associated protein tau, which is critical for the progression of Alzheimer's disease. GSK3B is involved in energy metabolism, neuronal cell development, and body pattern formation.
ab15314 (1/100) staining GSK3 in formalin fixed, paraffin-embbeded human brain tissue sections. Antigen retrieval was performed by boiling tissue sections in 10mM citrate buffer, pH 6.0 for 10 min followed by cooling at RT for 20 min.
Immunocytochemistry - Anti-GSK3 (alpha + beta) antibody (ab15314)Image from Wozniak MA et al., PLoS One. 2011;6(10):e25152. Epub 2011 Oct 7. Fig 10.; doi:10.1371/journal.pone.0025152; October 7, 2011, PLoS ONE 6(10): e25152.
ab15314 staining GSK3 (alpha + beta) in Vero cells infected with HSV1 by Immunocytochemistry.
Cells were infected with HSV1 SC16 at an MOI of 1 for 16 hours, fixed with formaldehyde and blocked by TBS containing 0.025% Triton X-100. Samples were incubated with primary antibody (1/100 in diluent) for 10 minutes.
Anti-GSK3 (alpha + beta) antibody (ab15314)参考文献
This product has been referenced in:
Wozniak MA et al. Antivirals reduce the formation of key Alzheimer's disease molecules in cell cultures acutely infected with herpes simplex virus type 1. PLoS One6:e25152 (2011).
African green monkey
Read more (PubMed: 22003387) »
Wozniak MA et al. Alzheimer's disease-specific tau phosphorylation is induced by herpes simplex virus type 1. J Alzheimers Dis16:341-50 (2009).
Read more (PubMed: 19221424) »