Phospho-GSK3β (Y216)/GSK3α (Y279) Antibody [F22P22]

Catalog No.: F2359

Application: Reactivity: Rat, Human, Zebrafish, Mouse

Lane 1: PC12, Lane 2: PC12 (nerve growth factor-β, 100ng/ml, 5 min), Lane 3: PC12 (nerve growth factor-β, 100ng/ml, 5 min; phosphatase treated), Lane 4: Mouse brain

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代表番号: 045-509-1970|電子メール：sales@selleck.co.jp

使用情報

Dilution
WB1:500-1:2000 IP1:40 IHC1:50

Application
WB, IP, IHC

Source
Rabbit Monoclonal Antibody

Reactivity
Rat, Human, Zebrafish, Mouse

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 Observed MW
50 kDa 47-52 kDa
^*なぜ予測分子量と実際の分子量が異なるのか？下記の原因により、実際の分子量が予測と異なる：タンパク質の翻訳後修飾（リン酸化/糖鎖付加），スプライシングバリアント，イソフォーム，相対的な電荷，ポリマー。

Datasheet & SDS

生物学的記述

Specificity
Phospho-GSK3β (Y216)/GSK3α (Y279) Antibody [F22P22] detects endogenous levels of total GSK3β and GSK3α protein only when it is phosphorylated at Y216 and Y279 respectively.

Clone
F22P22

Synonym(s)
Glycogen synthase kinase-3 beta/alpha; GSK3B; GSK3A

Background
Phosphorylated GSK3β (Y216) and GSK3α (Y279) denote activation‑loop tyrosine phosphorylation events on the two closely related glycogen synthase kinase 3 isoforms, which are constitutively active serine/threonine kinases that regulate multiple signaling cascades in the brain, liver, and other tissues. GSK3α and GSK3β both contain an N‑terminal kinase domain with a T‑loop whose phosphorylation at Y279 and Y216, respectively, stabilizes an open, active conformation that enhances substrate recognition and phosphotransfer to key effectors such as β‑catenin, glycogen synthase, and Tau. In the Wnt/β‑catenin pathway, active GSK3α and GSK3β phosphorylate β‑catenin within the destruction complex, promoting its ubiquitination and proteasomal degradation unless upstream Wnt ligands inhibit the complex through Dishevelled‑ and Axin‑dependent mechanisms, whereas in the insulin/PI3K/Akt axis Akt‑dependent inhibitory phosphorylation at Ser21 in GSK3α and Ser9 in GSK3β acts as a negative feedback node that dampens GSK3 activity and licenses glycogen synthase activation and normalized glucose metabolism. Phospho‑GSK3β (Y216)‑enriched states correlate with increased phosphorylation of Tau at multiple sites, contributing to Tau misfolding, tangle‑like assembly, and synaptic dysfunction in Alzheimer’s disease, while in metabolic tissues elevated GSK3β (Y216) phosphorylation is associated with impaired insulin signaling through IRS1, reduced glycogen synthesis, and dysglycemia in diabetes mellitus.

Background

Phosphorylated GSK3β (Y216) and GSK3α (Y279) denote activation‑loop tyrosine phosphorylation events on the two closely related glycogen synthase kinase 3 isoforms, which are constitutively active serine/threonine kinases that regulate multiple signaling cascades in the brain, liver, and other tissues. GSK3α and GSK3β both contain an N‑terminal kinase domain with a T‑loop whose phosphorylation at Y279 and Y216, respectively, stabilizes an open, active conformation that enhances substrate recognition and phosphotransfer to key effectors such as β‑catenin, glycogen synthase, and Tau. In the Wnt/β‑catenin pathway, active GSK3α and GSK3β phosphorylate β‑catenin within the destruction complex, promoting its ubiquitination and proteasomal degradation unless upstream Wnt ligands inhibit the complex through Dishevelled‑ and Axin‑dependent mechanisms, whereas in the insulin/PI3K/Akt axis Akt‑dependent inhibitory phosphorylation at Ser21 in GSK3α and Ser9 in GSK3β acts as a negative feedback node that dampens GSK3 activity and licenses glycogen synthase activation and normalized glucose metabolism. Phospho‑GSK3β (Y216)‑enriched states correlate with increased phosphorylation of Tau at multiple sites, contributing to Tau misfolding, tangle‑like assembly, and synaptic dysfunction in Alzheimer’s disease, while in metabolic tissues elevated GSK3β (Y216) phosphorylation is associated with impaired insulin signaling through IRS1, reduced glycogen synthesis, and dysglycemia in diabetes mellitus.

References
[1] Ke B, et al. Med Sci Monit. 2019 May 6;25:3336-3343. [2] Khoury M, et al. JHEP Rep. 2024 Mar 26;6(6):101073.

PVDFメンブレン孔径参考表

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

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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%