Phospho-ATGL (Ser406) Antibody [B14A21]

Application: Reactivity: Mouse, Human

Usage Information

Dilution
WB1:1000 IP1:30 IF1:50

Application
WB, IP, IF, ELISA

Reactivity
Mouse, Human

Source
Rabbit Monoclonal Antibody

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
55 kDa 55 kDa,36 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Datasheet & SDS

Biological Description

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

Clone
B14A21

Synonym(s)
Atgl, Pnpla2, Patatin-like phospholipase domain-containing protein 2, Adipose triglyceride lipase, Calcium-independent phospholipase A2-zeta, Desnutrin, iPLA2-zeta

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.

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.

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

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

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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%