Datasheet

生物学的記述

Specificity	PGK1 Antibody [H17D18] detects endogenous levels of total PGK1 protein.
Background	PGK1 (phosphoglycerate kinase 1) is a core glycolytic enzyme that catalyzes the reversible transfer of a phosphate group from 1,3‑bisphosphoglycerate to ADP, generating ATP and 3‑phosphoglycerate and thereby linking the upper and lower halves of the glycolytic pathway in most mammalian cells. PGK1 also functions as a non‑canonical protein kinase that is itself regulated by post‑translational modifications, including autophosphorylation at Tyr324, which is required for its full activation and is reversed by the lipid and protein phosphatase PTEN; loss of PTEN in tumor cells consequently elevates phospho‑Tyr324‑PGK1, enhances glycolytic flux, and promotes tumor growth. In hypoxic or nutrient‑stressed conditions, PGK1 can translocate to the mitochondria where it phosphorylates the pyruvate dehydrogenase kinase PDK1 at Thr338, inhibiting the pyruvate dehydrogenase complex, suppressing mitochondrial pyruvate oxidation, and favoring lactate production and glycolytic dependency. Under glutamine‑starved or hypoxic stress, acetylated PGK1 interacts with Beclin1 and phosphorylates it to activate the VPS34 complex and initiate autophagy, thereby coordinating metabolic adaptation with selective degradation and recycling of cytoplasmic components. PGK1 expression and activity are upregulated in multiple cancer types, where its dual glycolytic and kinase functions support proliferation, invasion, and stress survival, and altered PTEN‑dependent regulation of PGK1 Tyr324‑phosphorylation is linked to aggressive brain‑tumor phenotypes and poor clinical outcomes.

Specificity

PGK1 Antibody [H17D18] detects endogenous levels of total PGK1 protein.

Background

PGK1 (phosphoglycerate kinase 1) is a core glycolytic enzyme that catalyzes the reversible transfer of a phosphate group from 1,3‑bisphosphoglycerate to ADP, generating ATP and 3‑phosphoglycerate and thereby linking the upper and lower halves of the glycolytic pathway in most mammalian cells. PGK1 also functions as a non‑canonical protein kinase that is itself regulated by post‑translational modifications, including autophosphorylation at Tyr324, which is required for its full activation and is reversed by the lipid and protein phosphatase PTEN; loss of PTEN in tumor cells consequently elevates phospho‑Tyr324‑PGK1, enhances glycolytic flux, and promotes tumor growth. In hypoxic or nutrient‑stressed conditions, PGK1 can translocate to the mitochondria where it phosphorylates the pyruvate dehydrogenase kinase PDK1 at Thr338, inhibiting the pyruvate dehydrogenase complex, suppressing mitochondrial pyruvate oxidation, and favoring lactate production and glycolytic dependency. Under glutamine‑starved or hypoxic stress, acetylated PGK1 interacts with Beclin1 and phosphorylates it to activate the VPS34 complex and initiate autophagy, thereby coordinating metabolic adaptation with selective degradation and recycling of cytoplasmic components. PGK1 expression and activity are upregulated in multiple cancer types, where its dual glycolytic and kinase functions support proliferation, invasion, and stress survival, and altered PTEN‑dependent regulation of PGK1 Tyr324‑phosphorylation is linked to aggressive brain‑tumor phenotypes and poor clinical outcomes.

使用情報

Application

WB

Dilution

WB

1:1000

Reactivity

Human, Mouse, Rat

Source

Rabbit Monoclonal Antibody

MW

43 kDa

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

プロトコール

References

https://pubmed.ncbi.nlm.nih.gov/28486006/
https://pubmed.ncbi.nlm.nih.gov/31492635/

Application Data

WB

Validated by Selleck

Lane 1: Hela, Lane 2: NIH/3T3, Lane 3: C6, Lane 4: HuH7