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Anti-Phospho-GSK-3β (Ser9) Rabbit Antibody [G6H5]

Catalog No.: F4124

Application: Reactivity: Human, Mouse, Rat, Monkey

Usage Information

Dilution
WB1:1000 IHC1:50 IF1:100

Application
WB , IHC, IF

Reactivity
Human, Mouse, Rat, Monkey

Source
Rabbit

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW
46 kDa

Datasheet & SDS

Biological Description

Specificity
Anti-Phospho-GSK-3β (Ser9) Rabbit Antibody [G6H5] detects endogenous levels of total GSK-3β protein only when phosphorylated at Ser 9.

Clone
G6H5

Synonym(s)
Glycogen synthase kinase-3 beta, GSK-3 beta, Serine/threonine-protein kinase GSK3B, GSK3B

Background
Phospho-GSK-3β (Ser9) is the inactive form of glycogen synthase kinase-3 beta (GSK-3β), a serine/threonine kinase involved in metabolism, cell survival, and gene regulation. Phosphorylation at the N-terminal Ser9 residue inhibits GSK-3β by preventing substrate binding and enzymatic activity. Active GSK-3β phosphorylates substrates involved in glycogen metabolism, Wnt/β-catenin signaling, apoptosis, and neurodevelopment. Inhibition by Ser9 phosphorylation, mainly mediated by kinases such as Akt downstream of insulin or growth factor signaling, is a key regulatory mechanism controlling glucose homeostasis, cell proliferation, and neuronal survival. Regulation of GSK-3β activity involves dual phosphorylation: Tyr216 phosphorylation activates the kinase, while Ser9 phosphorylation inhibits it. The balance of these modifications determines GSK-3β activity and influences downstream cellular pathways. Phospho-Ser9 levels increase in response to insulin and other signals that activate Akt, leading to reduced GSK-3β activity, increased glycogen synthesis, and changes in cell signaling. Dysregulation of phospho-GSK-3β (Ser9) is associated with aging, cancer, diabetes, and neurodegenerative diseases.

Background

Phospho-GSK-3β (Ser9) is the inactive form of glycogen synthase kinase-3 beta (GSK-3β), a serine/threonine kinase involved in metabolism, cell survival, and gene regulation. Phosphorylation at the N-terminal Ser9 residue inhibits GSK-3β by preventing substrate binding and enzymatic activity. Active GSK-3β phosphorylates substrates involved in glycogen metabolism, Wnt/β-catenin signaling, apoptosis, and neurodevelopment. Inhibition by Ser9 phosphorylation, mainly mediated by kinases such as Akt downstream of insulin or growth factor signaling, is a key regulatory mechanism controlling glucose homeostasis, cell proliferation, and neuronal survival. Regulation of GSK-3β activity involves dual phosphorylation: Tyr216 phosphorylation activates the kinase, while Ser9 phosphorylation inhibits it. The balance of these modifications determines GSK-3β activity and influences downstream cellular pathways. Phospho-Ser9 levels increase in response to insulin and other signals that activate Akt, leading to reduced GSK-3β activity, increased glycogen synthesis, and changes in cell signaling. Dysregulation of phospho-GSK-3β (Ser9) is associated with aging, cancer, diabetes, and neurodegenerative diseases.

References
https://pubmed.ncbi.nlm.nih.gov/34778891/ https://pubmed.ncbi.nlm.nih.gov/28819213/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

Tech Support

Answers to questions you may have can be found in the inhibitor handling instructions. Topics include how to prepare stock solutions, how to store inhibitors, and issues that need special attention for cell-based assays and animal experiments.

Handling Instructions

Tel: +1-832-582-8158 Ext:3
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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%