Recombinant Human APOC3 His-tag Protein, CF

Measured by its binding ability in a functional ELISA. Recombinant Human APOC3 His-tag Protein (Catalog # 11826-AC) binds to Anti-human APOC3 with an ED50 of 1.00-10.0 ng/mL.

2 μg/lane of Recombinant Human APOC3 His-tag Protein (Catalog # 11826-AC) was resolved with SDS-PAGE under reducing (R) condition and visualized by Coomassie® Blue staining, showing bands at 19-23 kDa.

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human APOC3 His-tag Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. Recombinant Human APOC3 His-tag binds to Anti-human APOC3 with an ED₅₀ of 1.00-10.0 ng/mL.
• Source: E. coli-derived human APOC3 protein
  Ser21-Ala99, with an N-terminal His6 SUMO tag
• N-terminal Sequence: Met-His
• Protein/Peptide Type: 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:
  • Bioactivity
• Theoretical MW: 21 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: 19-23 kDa, under 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 Tris, NaCl and TCEP with Trehalose.
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining
• Reconstitution Instructions: Reconstitute at 250 μg/mL in water.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human APOC3 His-tag Protein, CF

• APOC3
• Apo-C3
• ApoC-3
• APOCIII
• Apo-CIII
• apoC-III
• Apolipoprotein C3
• apolipoprotein C-III
• MGC150353

Background

Apolipoprotein C-III (ApoC3) is a small exchangeable apolipoprotein that plays a central role in triglyceride-rich lipoprotein metabolism and lipid homeostasis. ApoC3 is encoded by the APOC3 gene and is primarily synthesized in the liver and, to a lesser extent, the intestine, where it associates with very low-density lipoproteins (VLDL), chylomicrons, and high-density lipoproteins (HDL) (1). Under physiological conditions, ApoC3 modulates plasma triglyceride levels by inhibiting lipoprotein lipase (LPL) activity and delaying hepatic clearance of triglyceride-rich particles (2). Human ApoC3 is a ~8.8 kDa protein composed of 79 amino acids and exists in multiple glycoforms depending on the extent of O-linked glycosylation at a single threonine residue (3). These glycoforms differentially influence lipoprotein binding and metabolic function. ApoC3 adopts amphipathic alpha -helical structures that facilitate reversible association with lipid surfaces and lipoprotein particles (3, 4). Elevated ApoC3 levels impair triglyceride hydrolysis and promote accumulation of atherogenic remnant lipoproteins, contributing to dyslipidemia and cardiovascular disease risk (2, 4). In addition to its canonical role in lipid metabolism, ApoC3 has been implicated in inflammation and vascular biology. It can promote endothelial activation, enhance monocyte adhesion, and contribute to a pro-inflammatory milieu that accelerates atherogenesis (4, 5). ApoC3 also influences hepatic lipid handling and insulin sensitivity, linking it to broader metabolic disorders including type 2 diabetes and nonalcoholic fatty liver disease (5). These diverse activities position ApoC3 as a key regulator of lipid-driven metabolic and cardiovascular processes. Genetic and clinical studies have demonstrated that loss-of-function mutations in APOC3 are associated with reduced plasma triglyceride levels and decreased risk of coronary artery disease, highlighting ApoC3 as a compelling therapeutic target (2, 6). Pharmacological strategies aimed at reducing ApoC3 expression or function, including antisense oligonucleotides and RNA-targeting therapies, have shown significant efficacy in lowering triglycerides in patients with hypertriglyceridemia (6, 7). Recombinant human ApoC3 is therefore an essential research reagent for studies of lipoprotein metabolism, protein–lipid interactions, glycoprotein biology, metabolic disease mechanisms, and therapeutic development targeting triglyceride regulation and cardiovascular risk.

1. Ginsberg, H.N. and Packard, C.J. (2021) Nat. Rev. Cardiol. 18:569.
2. Stahlman, M. et al. (2019) J. Lipid Res. 60:569.
3. Kozarsky, K.F. et al. (2018) Biochim. Biophys. Acta 1863:1466.
4. Gordts, P.L.S.M. et al. (2016) Circulation 133:2246.
5. Kawakami, A. et al. (2022) Front. Cardiovasc. Med. 9:822345.
6. Jørgensen, A.B. et al. (2014) N. Engl. J. Med. 371:32.
7. Witztum, J.L. et al. (2019) N. Engl. J. Med. 380:23.