Perilipin-1 Antibody [B3G1] Datasheet

Biological Description

Specificity	Perilipin-1 Antibody [B3G1] detects endogenous levels of total Perilipin-1 protein.
Background	Perilipin‑1 (PLIN1) is a lipid droplet–associated protein of the perilipin family that localizes to the surface of neutral lipid droplets in adipocytes and other lipid‑storing cells, where it acts as a key determinant of triacylglycerol storage and mobilization within adipose tissue and at lipid–endocrine interfaces. The protein contains central hydrophobic segments that target and anchor it into the phospholipid monolayer of lipid droplets, flanked by regulatory N‑ and C‑terminal regions enriched in consensus motifs for protein kinase A, which provide multiple serine residues that undergo phosphorylation during catecholamine‑driven cAMP signaling. Under basal or fed conditions, nonphosphorylated perilipin‑1 forms a protective coat that shields stored triacylglycerol from access by cytosolic lipases, promoting neutral lipid retention, stabilization of unilocular adipocyte droplets, and maintenance of adipocyte energy stores. Activation of β‑adrenergic receptors and cAMP‑dependent protein kinase leads to multisite phosphorylation of perilipin‑1, a modification that remodels the droplet surface, facilitates redistribution of the lipid droplet population from large perinuclear structures toward dispersed microdroplets, and enables efficient docking and activation of lipolytic machinery. Phosphorylation of defined N‑terminal PKA sites supports hormone‑sensitive lipase access to lipid substrates, whereas phosphorylation at C‑terminal sites contributes to maximal lipolysis, integrating perilipin‑1 into the core of the lipolytic pathway that converts stored triacylglycerol into glycerol and free fatty acids for systemic energy supply. The protein operates within a wider perilipin family context in which multiple splice variants and related paralogues decorate lipid droplets in a cell type–specific fashion, but perilipin‑1 dominates at the adipocyte droplet surface and functions as a principal gatekeeper that determines the balance between lipid storage and catecholamine‑stimulated fatty acid release. Functional analyses summarized in human and mouse work link perilipin‑1–dependent control of lipolysis to overall lipid metabolism, adipocyte size, and circulating lipid profiles, placing PLIN1 at a nodal point for whole‑body energy homeostasis and metabolic flexibility in response to nutritional status. Genetic variants in PLIN1 associate with severe familial partial lipodystrophy, early‑onset acute coronary syndrome, and altered cardiovascular risk, with variant position and type influencing whether the phenotype is characterized by ectopic lipid redistribution, dyslipidemia, or, in some cases, a protective lipid and cardiovascular profile. Perilipin‑1 expression and phosphorylation state also connect adipose lipid handling to atherosclerotic processes, as changes in adipocyte lipolytic output and inflammatory signaling correlate with modifications in vascular lipid deposition and plaque composition. Through its droplet‑anchored structure, PKA‑responsive regulatory motifs, and capacity to gate lipase access and droplet remodeling, perilipin‑1 defines a mechanistic platform that links catecholamine and cAMP signaling to controlled triglyceride hydrolysis and lipid storage.

Specificity

Perilipin-1 Antibody [B3G1] detects endogenous levels of total Perilipin-1 protein.

Background

Perilipin‑1 (PLIN1) is a lipid droplet–associated protein of the perilipin family that localizes to the surface of neutral lipid droplets in adipocytes and other lipid‑storing cells, where it acts as a key determinant of triacylglycerol storage and mobilization within adipose tissue and at lipid–endocrine interfaces. The protein contains central hydrophobic segments that target and anchor it into the phospholipid monolayer of lipid droplets, flanked by regulatory N‑ and C‑terminal regions enriched in consensus motifs for protein kinase A, which provide multiple serine residues that undergo phosphorylation during catecholamine‑driven cAMP signaling. Under basal or fed conditions, nonphosphorylated perilipin‑1 forms a protective coat that shields stored triacylglycerol from access by cytosolic lipases, promoting neutral lipid retention, stabilization of unilocular adipocyte droplets, and maintenance of adipocyte energy stores. Activation of β‑adrenergic receptors and cAMP‑dependent protein kinase leads to multisite phosphorylation of perilipin‑1, a modification that remodels the droplet surface, facilitates redistribution of the lipid droplet population from large perinuclear structures toward dispersed microdroplets, and enables efficient docking and activation of lipolytic machinery. Phosphorylation of defined N‑terminal PKA sites supports hormone‑sensitive lipase access to lipid substrates, whereas phosphorylation at C‑terminal sites contributes to maximal lipolysis, integrating perilipin‑1 into the core of the lipolytic pathway that converts stored triacylglycerol into glycerol and free fatty acids for systemic energy supply. The protein operates within a wider perilipin family context in which multiple splice variants and related paralogues decorate lipid droplets in a cell type–specific fashion, but perilipin‑1 dominates at the adipocyte droplet surface and functions as a principal gatekeeper that determines the balance between lipid storage and catecholamine‑stimulated fatty acid release. Functional analyses summarized in human and mouse work link perilipin‑1–dependent control of lipolysis to overall lipid metabolism, adipocyte size, and circulating lipid profiles, placing PLIN1 at a nodal point for whole‑body energy homeostasis and metabolic flexibility in response to nutritional status. Genetic variants in PLIN1 associate with severe familial partial lipodystrophy, early‑onset acute coronary syndrome, and altered cardiovascular risk, with variant position and type influencing whether the phenotype is characterized by ectopic lipid redistribution, dyslipidemia, or, in some cases, a protective lipid and cardiovascular profile. Perilipin‑1 expression and phosphorylation state also connect adipose lipid handling to atherosclerotic processes, as changes in adipocyte lipolytic output and inflammatory signaling correlate with modifications in vascular lipid deposition and plaque composition. Through its droplet‑anchored structure, PKA‑responsive regulatory motifs, and capacity to gate lipase access and droplet remodeling, perilipin‑1 defines a mechanistic platform that links catecholamine and cAMP signaling to controlled triglyceride hydrolysis and lipid storage.

Usage Information

Application

WB, IF

Dilution

WB	IF
1:1000-1:5000	1:100-1:250

Reactivity

Human

Source

Rabbit Monoclonal Antibody

MW

56 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

References

https://pubmed.ncbi.nlm.nih.gov/38214891/
https://pubmed.ncbi.nlm.nih.gov/19116774/

Perilipin-1 Antibody [B3G1]

Biological Description

Usage Information

References

Application Data