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Human APOA1 / ApoAI Protein (His Tag)

Apolipoprotein A-I

Catalog Number P10686-H07E
Organism Species Human
Host E. coli
Synonyms Apolipoprotein A-I
Molecular Weight The recombinant human APOA1 consists of 263 amino acids and predicts a molecular mass of 30.7 KDa. It migrates as an approximately 27-31 KDa band in SDS-PAGE under reducing conditions.
predicted N His
SDS-PAGE
Purity > 95 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the mature form of human APOA1 (P02647) (Asp25-Gln267) was expressed with a polyhistidine tag at the N-terminus.
Bio-activity
Research Area Cardiovascular |Atherosclerosis |Lipoprotein metabolism
Formulation Lyophilized from sterile PBS, 10% Glycerol, pH 7.4.
1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background Apolipoprotein A1 (APOA1) is a member of the apolipoprotein family whose members are proteins bind with lipids and form lipoproteins to translate these oil-soluble lipids such as fat and cholesterol through lymphatic and circulatory system. APOA1 is the main component of high density lipoprotein (HDL) in plasma and is involved in the esterification of cholesterol as a cofactor of lecithin-cholesterol acyltransferase (LCAT) which is responsible for the formation of most plasma cholesteryl esters, and thus play a major role in cholesterol efflux from peripheral cells. As a major component of the HDL complex, APOA1 helps to clear cholesterol from arteries. APOA1 is also characterized as a prostacyclin stabilizing factor, and thus may have an anticlotting effect. Defects in encoding gene may result in HDL deficiencies, including Tangier disease, and with systemic non-neuropathic amyloidosis. Men carrying a mutation may develop premature coronary artery disease.
Reference
  • Toptas B, et al. (2011) Comparison of lipid profiles with APOA1 MspI polymorphism in obese children with hyperlipidemia. In Vivo. 25(3): 425-30.
  • Haase CL, et al. (2011) Mutation in APOA1 predicts increased risk of ischaemic heart disease and total mortality without low HDL cholesterol levels. J Intern Med. 270(2): 136-46.
  • Wu Z, et al. (2011) The low resolution structure of ApoA1 in spherical high density lipoprotein revealed small angle neutron scattering. J Biol Chem. 286(14): 12495-508.