APOC2 Antibody, Biotin conjugated

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Description

What is APOC2 Antibody, Biotin Conjugated?

APOC2 (Apolipoprotein C-II) Antibody, Biotin Conjugated, is a specialized immunoassay reagent designed to detect and quantify the APOC2 protein in biological samples. APOC2 is a 79–101 amino acid protein critical for lipid metabolism, primarily activating lipoprotein lipase to hydrolyze triglycerides . The biotin conjugation enables high-sensitivity detection through streptavidin-HRP or fluorescent streptavidin conjugates, facilitating applications like ELISA, Western blot (WB), and immunohistochemistry (IHC) .

Key characteristics include:

  • Host species: Primarily rabbit-derived polyclonal antibodies .

  • Clonality: Polyclonal formulations dominate, offering broad epitope recognition .

  • Immunogen: Typically recombinant human APOC2 fragments or peptides (e.g., residues 20–38 or Thr23-Glu101) .

  • Conjugate: Biotin linked via covalent bonding, ensuring stable binding to streptavidin .

Key Applications

ApplicationDescriptionExample Data
ELISAQuantifies APOC2 in serum/plasma using paired antibodies (capture and biotinylated detection) .Standard curves with sensitivity down to 0.5 µg/mL .
Western BlotDetects APOC2 at ~8–11 kDa in human plasma, liver, or intestine lysates .Band observed under reducing conditions .
Immunohistochemistry (IHC)Localizes APOC2 in cytoplasmic regions of hepatocytes (human liver) .Positive staining in THP-1 cells, negative in MCF-7 .
Immunocytochemistry (ICC)Visualizes APOC2 in fixed cells using fluorescent secondary antibodies .Cytoplasmic staining in monocytic leukemia cells .

Research Insights

  • Molecular Weight Variability: APOC2 is detected at 8–11 kDa across studies, likely due to post-translational processing or gel electrophoresis conditions .

  • Disease Relevance: APOC2 dysregulation links to cardiovascular diseases, amyloidosis, and lipid metabolism disorders .

  • Cross-Reactivity: Validated specificity for human APOC2, with no significant cross-reactivity to analogues reported .

Technical Performance

  • Sensitivity: ELISA kits detect APOC2 concentrations as low as 0.5 µg/mL with inter-assay CV <12% .

  • Buffer Compatibility: Formulated in PBS with glycerol (50%) and sodium azide (0.02%) for long-term stability .

  • Biotinylation Efficiency: Validated via streptavidin-HRP binding in Western blots and ELISA .

Protocols and Best Practices

  • ELISA Protocol:

    1. Coat plates with capture antibody (e.g., MAB4497) .

    2. Incubate samples with biotinylated detection antibody (e.g., MAB44971) .

    3. Add streptavidin-HRP and TMB substrate for signal development .

  • Western Blot: Use 0.25–0.5 µg/mL antibody with HRP-conjugated streptavidin .

  • Storage: Avoid freeze-thaw cycles; store at -20°C or lower .

Product Specs

Buffer
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
Form
Liquid
Lead Time
Typically, we can ship the products within 1-3 business days after receiving your order. Delivery times may vary depending on the chosen purchasing method and destination. For specific delivery times, please consult your local distributor.
Synonyms
APC 2 antibody; APC2 antibody; Apo CII antibody; Apo-CII antibody; APOC 2 antibody; ApoC II antibody; ApoC-II antibody; APOC2 antibody; APOC2 protein antibody; APOC2_HUMAN antibody; ApoCII antibody; Apolipoprotein C II antibody; Apolipoprotein C II precursor antibody; Apolipoprotein C2 antibody; ApolipoproteinCII antibody; MGC75082 antibody; ProapoC-II antibody; Proapolipoprotein C-II antibody
Target Names
Uniprot No.

Target Background

Function
Apolipoprotein C-II is a component of chylomicrons, very low-density lipoproteins (VLDL), low-density lipoproteins (LDL), and high-density lipoproteins (HDL) in plasma. It plays a crucial role in lipoprotein metabolism as an activator of lipoprotein lipase. Both proapolipoprotein C-II and apolipoprotein C-II can activate lipoprotein lipase. In individuals with normal lipid levels, apolipoprotein C-II is primarily found in HDL, while in individuals with hypertriglyceridemia, it is predominantly located in VLDL and LDL.
Gene References Into Functions
  1. An exploratory analysis suggests that regulatory element methylation levels within the larger TOMM40-APOE-APOC2 gene region correlate with Alzheimer's disease (AD)-related biomarkers and TOMM40 or APOE gene expression in AD. PMID: 29371683
  2. Triglyceride-raising variant alleles of the APOC2 gene, which encodes apo C-II, have been associated with clinical cardiovascular endpoints. PMID: 28534127
  3. Research findings demonstrate the significant role of both intra- and inter-subunit charge interactions in stabilizing apoC-II amyloid fibrils. This process may be a key factor in determining the general ability of proteins to form amyloid fibrils. PMID: 28229588
  4. The results underscore the importance of charge-pair interactions within the apoC-II fibril core. PMID: 26196342
  5. Conformational rearrangement of apoC-II at lipoprotein surfaces facilitates interaction with lipoprotein lipase (LPL). PMID: 26026161
  6. A large deletion in APOC2 caused by Alu-Alu homologous recombination has been associated with apolipoprotein C-II deficiency. PMID: 25172036
  7. No APOC2 mutations were identified in a cohort of patients with diabetic lipemia. PMID: 25131724
  8. STAT1 bound on multienhancer 2 cooperates with RXRalpha located on the apoCII promoter and upregulates apoCII expression specifically in macrophages. PMID: 22808166
  9. Mutations in GPIHBP1 are uncommon, but the associated clinical phenotype of hypertriglyceridaemia is severe. PMID: 22239554
  10. These findings support a predictive change in the ratio of plasma ApoCIII to ApoCII in pregnancies complicated by severe preeclampsia. PMID: 21321243
  11. Substoichiometric concentrations of cyc[60-70] significantly delayed fibril formation by the fibrillogenic, linear peptides apoC-II[60-70] and apoC-II[56-76]. PMID: 22244853
  12. Activation of apoC-II fibrils by submicellar lipid (NBD-lyso-12-phosphocholine) is catalytic with release of monomer- and tetramer-bound lipid accompanying fibril elongation and growth. PMID: 21985034
  13. Physiological shear flow conditions and conditions encountered during apoC-II manufacturing exert significant effects on apoC-II conformation, leading to protein misfolding, aggregation, and amyloid fibril formation. PMID: 21476595
  14. Includes the observation of APOC4-APOC2 read-through transcription. PMID: 8530039
  15. Our structural model for apoC-II fibrils suggests that apoC-II monomers fold and self-assemble to form a stable cross-beta-scaffold containing relatively unstructured connecting loops. PMID: 21146539
  16. Results describe the functional role of the secondary structure in the lipoprotein lipase-binding portion of apolipoprotein CII. PMID: 20042600
  17. Human apolipoprotein C-II (apoC-II) slowly forms amyloid fibers in lipid-free solutions at physiological pH and salt concentrations. PMID: 11751863
  18. During amyloidosis under oxidizing conditions, cysteine-containing apolipoprotein C-II (apoC-II) derivatives form fibrils more rapidly and become extensively tangled compared to wild-type apoC-II. PMID: 12450397
  19. Three categories of global constraints, together with local classical NMR constraints, define the 3D structure of the apoCII-SDS micelle complex and provide important clues toward a possible mechanism for the activation of lipoprotein lipase by apoCII. PMID: 12590574
  20. Regions of lipoprotein lipase that are responsive to activation by apoC-II have been identified. PMID: 12682050
  21. Hydrolysis activated by APOC2 was faster compared with LPL-mediated lipolysis of emulsion triolein. The binding density of APOC2 was lower for small emulsion surfaces than for large ones. PMID: 12782148
  22. Different levels of secreted apoC-II had minimal effect on LDL and HDL protein degradation by HepG2 cells. Compared to controls, cells under-expressing apoC-II exhibited a 160% higher capacity to selectively take up HDL-CE. PMID: 15778093
  23. Results show that purified human HDL and recombinant apolipoprotein A-I lipid particles bind directly to amyloid beta and apolipoprotein C-II amyloid fibrils. PMID: 16432277
  24. No association was found between ApoCII polymorphism and coronary disease in the Chinese Han population. PMID: 16459141
  25. A decrease in LPL activity in the heart, along with the inhibitory effects of excess apolipoprotein C-II, may contribute to the hypertriglyceridemia observed in apolipoprotein c-ii transgenic mice. PMID: 17018885
  26. These data demonstrate an interaction between antichymotrypsin and apolipoprotein C-II that accelerates fibrillogenesis, indicating a specific role for accessory proteins in protein aggregation. PMID: 17174330
  27. These results suggest that the T-->A substitution at position -190 in the apoC-II gene promoter only partially affected the transcriptional activity of the apoC-II promoter, leading to a decrease in apoC-II expression. PMID: 17222387
  28. The ozone oxidation product of cholesterol, 3beta-hydroxy-5-oxo-5,6-secocholestan-6-al, rapidly promotes human apolipoprotein (apo) C-II amyloid fibril formation in vitro. PMID: 17429947
  29. Both common and rare DNA variants of the APOC2 gene were found in 10% of patients with severe hypertriglyceridemia. PMID: 17717288
  30. Phospholipid interaction induces molecular-level polymorphism in APOC2 amyloid fibrils via alternative assembly pathways. PMID: 18005990
  31. The concentration-dependent kinetics of apolipoprotein C-II amyloid fibril formation and its correlation with the final size distribution of the fibrils determined by sedimentation velocity experiments, is studied. PMID: 18206908
  32. Lipids promote on-pathway intermediates of apoC-II fibril assembly, and the accumulation of a discrete tetrameric intermediate depends on the molecular state of the lipid. PMID: 18852267
  33. No significant differences were found between the acute hypertriglyceridaemic pancreatitis cases and controls with severe hypertriglyceridaemia in terms of LPL activity and mass, hepatic lipase activity, CII and CIII mass, or apo E polymorphisms. PMID: 19534808

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Database Links

HGNC: 609

OMIM: 207750

KEGG: hsa:344

STRING: 9606.ENSP00000466775

UniGene: Hs.75615

Involvement In Disease
Hyperlipoproteinemia 1B (HLPP1B)
Protein Families
Apolipoprotein C2 family
Subcellular Location
Secreted.
Tissue Specificity
Liver and intestine.

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