Datasheet

生物学的記述

Specificity	Phospho-ATGL (Ser406) Antibody [B14A21] detects endogenous levels of total ATGL protein only when it is phosphorylated at Ser406.
Background	Phospho-ATGL (Ser406) denotes the activated form of adipose triglyceride lipase in which a serine residue within the C‑terminal regulatory region is phosphorylated to enhance triacylglycerol hydrolase activity and drive the first step of intracellular lipid mobilization. This modification occurs on the patatin-domain lipase ATGL, a cytosolic lipid droplet–associated enzyme that hydrolyzes triacylglycerol to diacylglycerol and free fatty acids and functions in concert with cofactors such as CGI‑58 and with downstream lipases in the canonical lipolytic cascade. Phosphorylation at Ser406 is mediated by protein kinase A and AMP‑activated protein kinase in response to β‑adrenergic and energy-sensing pathways and increases catalytic activity toward triacylglycerol substrates, linking hormonal and nutrient cues to lipolytic flux and fatty acid release. The phospho‑Ser406 state aligns ATGL with hormone-sensitive lipase and monoacylglycerol lipase, coordinating sequential hydrolysis of stored neutral lipids and supporting fatty acid delivery to mitochondria for oxidation or to nuclear receptors such as PPARα as lipid-derived signaling molecules. In oxidative tissues including the heart and skeletal muscle, enrichment of phospho‑ATGL at this site supports high rates of fatty acid utilization and contributes to maintenance of energy supply and mitochondrial function under conditions of increased workload or fasting. Within adipose depots, the balance between phosphorylated and nonphosphorylated ATGL at Ser406 shapes basal versus stimulated lipolysis and interacts with distinct kinase inputs to differentiate catecholamine-driven activation from AMPK-mediated modulation of lipid breakdown. Phospho‑ATGL (Ser406) therefore marks a functionally engaged pool of the enzyme that reflects upstream signaling through cAMP/PKA and AMPK and defines the capacity of cells to mobilize triacylglycerol stores for systemic energy homeostasis. Altered levels or regulation of this phospho-species are associated with disturbed lipid handling, ectopic lipid accumulation, and cardiometabolic dysfunction.

Specificity

Phospho-ATGL (Ser406) Antibody [B14A21] detects endogenous levels of total ATGL protein only when it is phosphorylated at Ser406.

Background

Phospho-ATGL (Ser406) denotes the activated form of adipose triglyceride lipase in which a serine residue within the C‑terminal regulatory region is phosphorylated to enhance triacylglycerol hydrolase activity and drive the first step of intracellular lipid mobilization. This modification occurs on the patatin-domain lipase ATGL, a cytosolic lipid droplet–associated enzyme that hydrolyzes triacylglycerol to diacylglycerol and free fatty acids and functions in concert with cofactors such as CGI‑58 and with downstream lipases in the canonical lipolytic cascade. Phosphorylation at Ser406 is mediated by protein kinase A and AMP‑activated protein kinase in response to β‑adrenergic and energy-sensing pathways and increases catalytic activity toward triacylglycerol substrates, linking hormonal and nutrient cues to lipolytic flux and fatty acid release. The phospho‑Ser406 state aligns ATGL with hormone-sensitive lipase and monoacylglycerol lipase, coordinating sequential hydrolysis of stored neutral lipids and supporting fatty acid delivery to mitochondria for oxidation or to nuclear receptors such as PPARα as lipid-derived signaling molecules. In oxidative tissues including the heart and skeletal muscle, enrichment of phospho‑ATGL at this site supports high rates of fatty acid utilization and contributes to maintenance of energy supply and mitochondrial function under conditions of increased workload or fasting. Within adipose depots, the balance between phosphorylated and nonphosphorylated ATGL at Ser406 shapes basal versus stimulated lipolysis and interacts with distinct kinase inputs to differentiate catecholamine-driven activation from AMPK-mediated modulation of lipid breakdown. Phospho‑ATGL (Ser406) therefore marks a functionally engaged pool of the enzyme that reflects upstream signaling through cAMP/PKA and AMPK and defines the capacity of cells to mobilize triacylglycerol stores for systemic energy homeostasis. Altered levels or regulation of this phospho-species are associated with disturbed lipid handling, ectopic lipid accumulation, and cardiometabolic dysfunction.

使用情報

Application

WB, IP, IF, ELISA

Dilution

WB	IP	IF
1:1000	1:30	1:50

Reactivity

Mouse, Human

Source

Rabbit Monoclonal Antibody

MW

55 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/22733971/
https://pubmed.ncbi.nlm.nih.gov/28925902/

Phospho-ATGL (Ser406) Antibody [B14A21]

生物学的記述

使用情報

References

Application Data