Recombinant Human Apolipoprotein A-IV/ApoA4 Protein, CF
Recombinant Human Apolipoprotein A-IV/ApoA4 Protein, CF Summary
Product Specifications
Glu21-Ser396, with an N-terminal Met
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
9606-AP
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
Reconstitution | Reconstitute at 250 μg/mL in PBS. |
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Reconstitution Calculator
Background: Apolipoprotein A-IV/ApoA4
Apolipoprotein A-IV (ApoA4) is a 45 kDa glycoprotein of the lipid transport system. Secreted in plasma, ApoA4 is a major component of high density lipoprotein (HDL) particles and chylomicrons, and is thought to act in intestinal lipid absorption. Levels of ApoA4 may influence HDL metabolism and modulate its effects on atherogenesis (1). ApoA4 synthesis in humans is mainly confined to the small intestine, while in mice and rats, production occurs in the liver as well (2). ApoA4 shares several structural characteristics with ApoA1 and other exchangeable apolipoproteins. The core domain of human ApoA4 contains thirteen 22-amino acid tandem repeats, and nine of which are predicted to be amphipathic alpha -helical repeats that are critical for lipid binding and self-association (3). The overall structure of a long rod‑like dimer consisting of two 4-helix bundles stacked end-to-end in opposing orientations (4). Human ApoA4 is synthesized as a 396 amino acid (aa) precursor, from which a 20 aa N-terminal signal peptide is removed. Mature human ApoA4 shares 61% and 62% aa sequence identity with mouse and rat ApoA4, respectively.
- Duverger N. et al. (1991) Eur. J. Biochem. 201:373.
- Maeda, N. et al. (1994) J. Biol. Chem. 269:23610.
- Segrest, J. P. et al. (1994). Adv. Protein. Chem. 45:303.
- Deng, X. et al. (2012) Structure 20:767.
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