Recombinant Human Apolipoprotein A-IV/ApoA4 Protein, CF Summary
Details of Functionality |
Bioassay data are not available. |
Source |
E. coli-derived human Apolipoprotein A-IV/ApoA4 protein Glu21-Ser396, with an N-terminal Met |
Accession # |
|
N-terminal Sequence |
Met |
Protein/Peptide Type |
Innovator Recombinant Proteins |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
44 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
SDS-PAGE |
43 kDa, reducing conditions |
Packaging, Storage & Formulations
Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 3 months, -20 to -70 °C under sterile conditions after reconstitution.
|
Buffer |
Lyophilized from a 0.2 μm filtered solution in PBS. |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 250 μg/mL in PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Apolipoprotein A-IV/ApoA4 Protein, CF
Background
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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