APOLIPOPROTEIN A-I, HUMAN
APOLIPOPROTEIN A-I, HUMAN Basic information
- Product Name:
- APOLIPOPROTEIN A-I, HUMAN
- Synonyms:
-
- ApoA-1 from rat
- Apolipoprotein A-I histidine-tagged
- C117399
- MGC117399
- HUMAN APOA-I
- HUMAN APOLIPOPROTEIN A I
- HUMAN APOLIPOPROTEIN A I (MASS CONCENTRATION)
- APO A-1
- MW:
- 0
- Product Categories:
-
- Application CRMs
- Certified Reference Materials (CRMs)
- Clinical Chemistry CRMAlphabetic
- H
- HU - HZ
- Mol File:
- Mol File
APOLIPOPROTEIN A-I, HUMAN Chemical Properties
- storage temp.
- −20°C
- solubility
- H2O: 1 mg/mL, clear, colorless
- form
- solution (clear)
- color
- colorless
MSDS
- Language:English Provider:SigmaAldrich
APOLIPOPROTEIN A-I, HUMAN Usage And Synthesis
Uses
Apolipoprotein A-I human has been used in the cholesterol efflux assay.
General Description
ApoA-I, which is found exclusively in HDL, has a unique ability to capture and solubilize free cholesterol. This apoA-I ability enables HDL to remove excess peripheral cholesterol and return it to the liver for recycling and excretion. This process, called reverse cholesterol transport, is though to inhibit atherogenesis. For this reason HDL is also known as the "good cholesterol." The therapeutic potential of apoA-I has been recently assessed in patients with acute coronary syndromes, using a recombinant form of a naturally occurring variant of apoA-I (called apoA-I Milano). The availability of recombinant normal apoA-I should facilitate further investigation into the potential usefulness of apoA-I in preventing atherosclerotic vascular diseases.
Biochem/physiol Actions
ApoA-I (apolipoprotein A-I), which is found exclusively in HDL (high-density lipoprotein), has a unique ability to capture and solubilize free cholesterol. This apoA-I ability enables HDL to remove excess peripheral cholesterol and return it to the liver for recycling and excretion. This process, called reverse cholesterol transport, is thought to inhibit atherogenesis. For this reason HDL is also known as the "good cholesterol." The therapeutic potential of apoA-I has been recently assessed in patients with acute coronary syndromes, using a recombinant form of a naturally occurring variant of apoA-I (called apoA-I Milano). The availability of recombinant normal apoA-I should facilitate further investigation into the potential usefulness of apoA-I in preventing atherosclerotic vascular diseases. Changes in the level of serum apoA-I may serve as a prognostic marker for non-metastatic nasopharyngeal carcinoma. Low levels of apoA-I in the plasma is linked to hyperhomocysteinemia.
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