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Western blot analysis of GSK3 in MCF-7 cell extracts. Proteins were resolved by SDS-PAGE, transferred to a PVDF membrane and incubated with GSK-3 alpha/beta monoclonal antibody (Product # MA1-7621) at a dilution of 0.5 µg/mL. The signal was detected using a goat F(ab')2 anti-mouse IgG Alkaline Phosphatase conjugated antibody at a 1:5000 dilution and the membrane was incubated with CDP-substrate using the WesternStar™ method (Tropix). The membrane was then exposed to Kodak BioMax film.
|Tested species reactivity||Human, Rat, Clawed frog|
|Published species reactivity||Rat|
|Host / Isotype||Mouse / IgG2a|
|Immunogen||Purified recombinant Xenopus laevis protein.|
|Contains||0.01% sodium azide|
|Storage Conditions||Store at 4°C short term. For long term storage, store at -20°C, avoiding freeze/thaw cycles.|
|Tested Applications||Dilution *|
|Immunohistochemistry (IHC)||Assay Dependent|
|Immunoprecipitation (IP)||5-10 µg|
|Western Blot (WB)||1:1000|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
|Western Blot (WB)||See 1 publications below|
MA1-7621 detects GSK3 Beta from human, rat, and Xenopus laevis samples.
MA1-7621 has been successfully used in ELISA, Western blot, immunoprecipitation and immunohistochemistry procedures.
The MA1-7621 immunogen is a purified recombinant Xenopus laevis protein.
Store at 4°C short term. For extended storage, keep at -80°C.
Glycogen synthase kinase-3 (GSK3) is a protein kinase that was originally identified as a regulator of 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. GSK3"e;s 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, GSK3 alpha and GSK3 beta, and they are strictly regulated via phosphorylation. Phosphorylation of GSK3beta 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 (HSF-1), 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"e;s disease.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Soluble amyloid beta-protein dimers isolated from Alzheimer cortex directly induce Tau hyperphosphorylation and neuritic degeneration.
MA1-7621 was used in western blot to investigate the effect of Abeta on the regulation of tau modification and neuronal function
|Jin M,Shepardson N,Yang T,Chen G,Walsh D,Selkoe DJ||Proceedings of the National Academy of Sciences of the United States of America (108:5819)||2011|
EC 126.96.36.199; FA; factor A; Glycogen Synthase Kinase 3 beta; glycogen synthase kinase-3 beta; GSK-3 beta; GSK3beta isoform; intracellular kinase; serine/threonine-protein kinase GSK3B
7330414F15Rik; 8430431H08Rik; C86142; GSK-3; GSK-3beta; GSK3; gsk3-beta; GSK3B; gsk3beta; Xgsk-3