ApoA5 Antibody [H10J23]

Catalog No.: F9446

Application: Reactivity: Human

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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
WB1:1000 IP1:50

Application
WB, IP

Source
Mouse Monoclonal Antibody

Reactivity
Human

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
41 kDa

Datasheet & SDS

生物学的記述

Specificity
ApoA5 Antibody [H10J23] detects endogenous levels of total ApoA5 protein.

Clone
H10J23

Synonym(s)
Apolipoprotein A-V; Apo-AV; ApoA-V; Apolipoprotein A5; Regeneration-associated protein 3; APOA5; RAP3

Background
ApoA5 (apolipoprotein A-V) is a hydrophobic, amphipathic 343-amino-acid protein in the apolipoprotein gene family (APOA1/C3/A4 cluster) and serves as a crucial regulator of plasma triglyceride levels, particularly on triglyceride-rich lipoproteins such as chylomicrons and VLDL. ApoA5 features an N-terminal water-soluble helix bundle (residues 1–146), a C-terminal lipid-binding domain (295–343), and a proteoglycan-binding site (186–227) that facilitates interactions with lipoproteins and the endothelium, with coiled-coil domains enhancing lipid droplet and endothelial binding. ApoA5 binds triglyceride-rich lipoproteins and recruits lipoprotein lipase (LPL) via GPIHBP1 on capillary endothelial cells, stabilizing the lipolytic complex in membrane subdomains to accelerate chylomicron and VLDL lipolysis, and also suppresses ANGPTL3/8-mediated LPL inhibition through its C-terminal region. Within hepatocytes, ApoA5 targets ER-localized lipid droplets to regulate hepatic triglyceride flux, directing cytosolic lipid droplet formation over secretion and influencing lipoprotein assembly. Loss-of-function mutations or polymorphisms in APOA5 impair lipolysis and remnant clearance, leading to hypertriglyceridemia and increased cardiovascular risk.

Background

ApoA5 (apolipoprotein A-V) is a hydrophobic, amphipathic 343-amino-acid protein in the apolipoprotein gene family (APOA1/C3/A4 cluster) and serves as a crucial regulator of plasma triglyceride levels, particularly on triglyceride-rich lipoproteins such as chylomicrons and VLDL. ApoA5 features an N-terminal water-soluble helix bundle (residues 1–146), a C-terminal lipid-binding domain (295–343), and a proteoglycan-binding site (186–227) that facilitates interactions with lipoproteins and the endothelium, with coiled-coil domains enhancing lipid droplet and endothelial binding. ApoA5 binds triglyceride-rich lipoproteins and recruits lipoprotein lipase (LPL) via GPIHBP1 on capillary endothelial cells, stabilizing the lipolytic complex in membrane subdomains to accelerate chylomicron and VLDL lipolysis, and also suppresses ANGPTL3/8-mediated LPL inhibition through its C-terminal region. Within hepatocytes, ApoA5 targets ER-localized lipid droplets to regulate hepatic triglyceride flux, directing cytosolic lipid droplet formation over secretion and influencing lipoprotein assembly. Loss-of-function mutations or polymorphisms in APOA5 impair lipolysis and remnant clearance, leading to hypertriglyceridemia and increased cardiovascular risk.

References
[1] Mendoza-Barberá E, et al. J Lipid Res. 2013 Mar;54(3):649-661. [2] Forte TM, et al. Curr Drug Targets. 2015;16(12):1274-80.

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%