Datasheet

生物学的記述

Specificity	Apolipoprotein CI/Apo-CI Antibody [N16B24] detects endogenous levels of total Apolipoprotein CI/Apo-CI protein.
Background	Apolipoprotein CI (c), the smallest exchangeable apolipoprotein, is derived from an 83-residue precursor and is mainly expressed in the liver and macrophages. It circulates on HDL, VLDL, and chylomicrons, adopting a structure of two antiparallel α-helices connected by a flexible hinge with hydrophobic stacking interactions, and a lysine/arginine-rich C-terminal region that enables lipoprotein binding through electrostatic and amphipathic lipid interactions. ApoC-I strongly inhibits cholesteryl ester transfer protein (CETP) by increasing HDL electronegativity via its positively charged C-terminal helix, disrupting HDL-CETP complexes and thereby restricting neutral lipid transfer between HDL and triglyceride-rich lipoproteins (TRLs). ApoC-I competitively displaces apoE from β-VLDL, impairing receptor-mediated clearance via the LDL receptor-related protein (LRP), VLDL receptor, and LDL receptor, which leads to prolonged TRL circulation and triglyceride accumulation. These actions promote hypertriglyceridemia, foam cell formation, plaque inflammation, and the progression of atherosclerosis. Elevated ApoC-I levels are associated with increased risk of cardiovascular disease, enhanced Aβ aggregation and Alzheimer's disease, and macrovascular complications in type 1 diabetes due to CETP dysregulation and impaired reverse cholesterol transport.

Specificity

Apolipoprotein CI/Apo-CI Antibody [N16B24] detects endogenous levels of total Apolipoprotein CI/Apo-CI protein.

Background

Apolipoprotein CI (c), the smallest exchangeable apolipoprotein, is derived from an 83-residue precursor and is mainly expressed in the liver and macrophages. It circulates on HDL, VLDL, and chylomicrons, adopting a structure of two antiparallel α-helices connected by a flexible hinge with hydrophobic stacking interactions, and a lysine/arginine-rich C-terminal region that enables lipoprotein binding through electrostatic and amphipathic lipid interactions. ApoC-I strongly inhibits cholesteryl ester transfer protein (CETP) by increasing HDL electronegativity via its positively charged C-terminal helix, disrupting HDL-CETP complexes and thereby restricting neutral lipid transfer between HDL and triglyceride-rich lipoproteins (TRLs). ApoC-I competitively displaces apoE from β-VLDL, impairing receptor-mediated clearance via the LDL receptor-related protein (LRP), VLDL receptor, and LDL receptor, which leads to prolonged TRL circulation and triglyceride accumulation. These actions promote hypertriglyceridemia, foam cell formation, plaque inflammation, and the progression of atherosclerosis. Elevated ApoC-I levels are associated with increased risk of cardiovascular disease, enhanced Aβ aggregation and Alzheimer's disease, and macrovascular complications in type 1 diabetes due to CETP dysregulation and impaired reverse cholesterol transport.

使用情報

Application

WB, IP, IHC

Dilution

WB	IP	IHC
1:1000	1:40	1:800

Reactivity

Human

Source

Rabbit Monoclonal Antibody

MW

9 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/36471375/
https://pubmed.ncbi.nlm.nih.gov/30559175/

Application Data

WB

Validated by Selleck

Lane 1: Human plasma