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Rabbit Anti-APOC3 Recombinant Antibody (SR1078) (CBMAB-A3199-YC)

Provided herein is a Rabbit monoclonal antibody against Human Apolipoprotein C3. The antibody can be used for immunoassay techniques, such as ICC, IF, WB.
See all APOC3 antibodies
Published Data

Summary

Host Animal
Rabbit
Specificity
Human
Clone
SR1078
Antibody Isotype
IgG
Application
IHC, WB

Basic Information

Immunogen
A synthesized peptide derived from human Apolipoprotein CIII.
Host Species
Rabbit
Specificity
Human
Antibody Isotype
IgG
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:500-1:2,000
IHC1:50-1:200

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, pH 7.4, 150mM NaCl, 50% glycerol
Preservative
0.02% sodium azide
Concentration
Batch dependent
Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Apolipoprotein C3
Introduction
APOC3 is a protein component of triglyceride (TG)-rich lipoproteins (TRLs) including very low density lipoproteins (VLDL), high density lipoproteins (HDL) and chylomicrons. The encoded protein plays a role in role in the metabolism of these TRLs through m
Entrez Gene ID
Human345
Rat24207
UniProt ID
HumanP02656
RatP06759
Alternative Names
Apolipoprotein C3; Apolipoprotein C-III; Apo-CIII; ApoC-III; APOCIII;
Function
Component of triglyceride-rich very low density lipoproteins (VLDL) and high density lipoproteins (HDL) in plasma (PubMed:18201179, PubMed:22510806). Plays a multifaceted role in triglyceride homeostasis (PubMed:18201179, PubMed:22510806). Intracellularly, promotes hepatic very low density lipoprotein 1 (VLDL1) assembly and secretion; extracellularly, attenuates hydrolysis and clearance of triglyceride-rich lipoproteins (TRLs) (PubMed:18201179, PubMed:22510806). Impairs the lipolysis of TRLs by inhibiting lipoprotein lipase and the hepatic uptake of TRLs by remnant receptors (PubMed:18201179, PubMed:22510806). Formed of several curved helices connected via semiflexible hinges, so that it can wrap tightly around the curved micelle surface and easily adapt to the different diameters of its natural binding partners (PubMed:18408013).
Biological Process
Cholesterol efflux Source: BHF-UCL
Cholesterol homeostasis Source: BHF-UCL
Chylomicron assembly Source: Reactome
Chylomicron remnant clearance Source: BHF-UCL
Chylomicron remodeling Source: Reactome
G protein-coupled receptor signaling pathway Source: BHF-UCL
High-density lipoprotein particle remodeling Source: BHF-UCL
Lipoprotein metabolic process Source: InterPro
Negative regulation of cholesterol import Source: BHF-UCL
Negative regulation of fatty acid biosynthetic process Source: BHF-UCL
Negative regulation of high-density lipoprotein particle clearance Source: BHF-UCL
Negative regulation of lipid catabolic process Source: BHF-UCL
Negative regulation of lipid metabolic process Source: BHF-UCL
Negative regulation of lipoprotein lipase activity Source: BHF-UCL
Negative regulation of low-density lipoprotein particle clearance Source: BHF-UCL
Negative regulation of receptor-mediated endocytosis Source: BHF-UCL
Negative regulation of triglyceride catabolic process Source: BHF-UCL
Negative regulation of very-low-density lipoprotein particle clearance Source: BHF-UCL
Negative regulation of very-low-density lipoprotein particle remodeling Source: BHF-UCL
Phospholipid efflux Source: BHF-UCL
Regulation of Cdc42 protein signal transduction Source: BHF-UCL
Retinoid metabolic process Source: Reactome
Reverse cholesterol transport Source: BHF-UCL
Triglyceride catabolic process Source: BHF-UCL
Triglyceride homeostasis Source: BHF-UCL
Triglyceride metabolic process Source: HGNC-UCL
Very-low-density lipoprotein particle assembly Source: BHF-UCL
Cellular Location
Secreted
Involvement in disease
Hyperalphalipoproteinemia 2 (HALP2): A condition characterized by high levels of high density lipoprotein (HDL) and increased HDL cholesterol levels.
PTM
The most abundant glycoforms are characterized by an O-linked disaccharide galactose linked to N-acetylgalactosamine (Gal-GalNAc), further modified with up to 3 sialic acid residues. Less abundant glycoforms are characterized by more complex and fucosylated glycan moieties. O-glycosylated on Thr-94 with a core 1 or possibly core 8 glycan.

Buckner, T., Shao, B., Eckel, R. H., Heinecke, J. W., Bornfeldt, K. E., & Snell-Bergeon, J. (2021). Association of apolipoprotein C3 with insulin resistance and coronary artery calcium in patients with type 1 diabetes. Journal of Clinical Lipidology, 15(1), 235-242.

Xu, Q. Y., Li, H., Cao, H. X., Pan, Q., & Fan, J. G. (2020). APOC3 rs2070667 Associates with Serum Triglyceride Profile and Hepatic Inflammation in Nonalcoholic Fatty Liver Disease. BioMed Research International, 2020.

Zewinger, S., Reiser, J., Jankowski, V., Alansary, D., Hahm, E., Triem, S., ... & Speer, T. (2020). Apolipoprotein C3 induces inflammation and organ damage by alternative inflammasome activation. Nature immunology, 21(1), 30-41.

Morze, J., Koch, M., Aroner, S. A., Budoff, M., McClelland, R. L., Mukamal, K. J., & Jensen, M. K. (2020). Associations of HDL Subspecies Defined by ApoC3 with Non-Alcoholic Fatty Liver Disease: The Multi-Ethnic Study of Atherosclerosis. Journal of clinical medicine, 9(11), 3522.

Kanter, J. E., Shao, B., Kramer, F., Barnhart, S., Shimizu-Albergine, M., Vaisar, T., ... & Bornfeldt, K. E. (2019). Increased apolipoprotein C3 drives cardiovascular risk in type 1 diabetes. The Journal of clinical investigation, 129(10), 4165-4179.

Dai, W., Zhang, Z., Yao, C., & Zhao, S. (2019). Emerging evidences for the opposite role of apolipoprotein C3 and apolipoprotein A5 in lipid metabolism and coronary artery disease. Lipids in health and disease, 18(1), 1-7.

Wang, Y., Shen, L., & Xu, D. (2019). Aerobic exercise reduces triglycerides by targeting apolipoprotein C3 in patients with coronary heart disease. Clinical cardiology, 42(1), 56-61.

Ginsberg, H. N., & Reyes-Soffer, G. (2019). Is APOC3 the driver of cardiovascular disease in people with type I diabetes mellitus?. The Journal of clinical investigation, 129(10), 4074-4076.

Zvintzou, E., Lhomme, M., Chasapi, S., Filou, S., Theodoropoulos, V., Xapapadaki, E., ... & Kypreos, K. E. (2017). Pleiotropic effects of apolipoprotein C3 on HDL functionality and adipose tissue metabolic activity [S]. Journal of lipid research, 58(9), 1869-1883.

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For research use only. Not intended for any clinical use.

Custom Antibody Labeling

We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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