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AB27630

Biotin Anti-Apolipoprotein A I antibody

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(4 Publications)

Goat Polyclonal Apolipoprotein A I antibody - conjugated to Biotin. Suitable for ELISA, WB and reacts with Human samples. Cited in 4 publications. Immunogen corresponding to Native Full Length Protein corresponding to Human APOA1.

View Alternative Names

Apolipoprotein A-I, Apo-AI, ApoA-I, Apolipoprotein A1, APOA1

Key facts

Host species

Goat

Clonality

Polyclonal

Isotype

IgG

Conjugation

Biotin

Excitation/Emission
Carrier free

No

Reacts with

Human

Applications

ELISA, WB

applications

Immunogen

Native Full Length Protein corresponding to Human APOA1.

P02647

Specificity

This antibody specifically binds to human Apolipoprotein A I in plasma and lipoproteins.

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Purification notes
This antibody was purified by human Apolipoprotein A I-Sepharose™ affinity column.
Storage buffer
pH: 6.5 - 7.4 Preservative: 0.02% Sodium azide Constituents: 1.23% Sodium phosphate, 0.435% Sodium chloride, 0.01% EDTA
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
+4°C
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Apolipoprotein A-I (ApoA-I) is a major component of high-density lipoprotein (HDL) particles often referred to as 'good cholesterol'. It has a molecular mass of approximately 28 kDa. ApoA-I is mainly expressed in the liver and intestine. It plays a mechanical role in the reverse transport of cholesterol acting to facilitate the efflux of cholesterol from tissues to the liver for excretion. Its alternative names include ApoAI ApoA1 and a component of the AI kits used for measuring this protein.
Biological function summary

ApoA-I functions in cholesterol homeostasis and inflammation. It is a structural component of the HDL complex that mobilizes cholesterol. ApoA-I acts as an activator of the enzyme lecithin-cholesterol acyltransferase (LCAT) which is essential for the maturation of HDL particles. This maturation is necessary for effective cholesterol transport and clearance. ApoA-I's ability to stabilize HDL particles and enhance their functionality makes it significant for maintaining lipid balance and cellular homeostasis.

Pathways

The interaction of ApoA-I with HDL formation and function marks its role in lipid metabolism pathways. Its participation in the reverse cholesterol transport pathway highlights its influence on cardiovascular health. ApoA-I also interacts with other proteins like ApoA-II and paraoxonase-1 which further influence lipid metabolism and antioxidant activities. Understanding these relationships helps elucidate the dynamics of cholesterol removal from the bloodstream.

Disturbances in ApoA-I levels correlate with cardiovascular disease and atherosclerosis. Deficiency or dysfunction in ApoA-I can impair HDL function leading to poor cholesterol removal and buildup within arteries. It is also connected to amyloidosis where misfolded ApoA-I forms deposits in tissues. Understanding these pathological conditions helps researchers target ApoA-I in therapeutic strategies to mitigate disease progression often studying it alongside proteins like ApoB which is associated with low-density lipoprotein (LDL) particles.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility.
See full target information APOA1

Publications (4)

Recent publications for all applications. Explore the full list and refine your search

International journal of molecular sciences 24: PubMed36613763

2022

The Apparent Organ-Specificity of Amyloidogenic ApoA-I Variants Is Linked to Tissue-Specific Extracellular Matrix Components.

Applications

Unspecified application

Species

Unspecified reactive species

Rita Del Giudice,Mikaela Lindvall,Oktawia Nilsson,Daria Maria Monti,Jens O Lagerstedt

PloS one 16:e0243337 PubMed33826643

2021

Interaction of amphiphilic lipoarabinomannan with host carrier lipoproteins in tuberculosis patients: Implications for blood-based diagnostics.

Applications

Unspecified application

Species

Unspecified reactive species

Shailja Jakhar,Ramamurthy Sakamuri,Dung Vu,Priya Dighe,Loreen R Stromberg,Laura Lilley,Nicolas Hengartner,Basil I Swanson,Emmanuel Moreau,Susan E Dorman,Harshini Mukundan

Arteriosclerosis, thrombosis, and vascular biology 39:1884-1892 PubMed31315438

2019

Association Between ApoA-I (Apolipoprotein A-I) Immune Complexes and Adverse Cardiovascular Events-Brief Report.

Applications

Unspecified application

Species

Unspecified reactive species

David Henson,Ayman Samman Tahhan,David Nardo,Arshed Ali Quyyumi,Vincent J Venditto

Scientific reports 9:6203 PubMed30996333

2019

Direct detection of bacteremia by exploiting host-pathogen interactions of lipoteichoic acid and lipopolysaccharide.

Applications

Unspecified application

Species

Unspecified reactive species

Jessica Z Kubicek-Sutherland,Dung M Vu,Aneesa Noormohamed,Heather M Mendez,Loreen R Stromberg,Christine A Pedersen,Astrid C Hengartner,Katja E Klosterman,Haley A Bridgewater,Vincent Otieno,Qiuying Cheng,Samuel B Anyona,Collins Ouma,Evans Raballah,Douglas J Perkins,Benjamin H McMahon,Harshini Mukundan
View all publications

Product promise

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