Recombinant Human Apolipoprotein C-II (APOC2)

Code CSB-BP001932HU
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Source Baculovirus
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Code CSB-EP001932HU-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-MP001932HU
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
APOC2
Uniprot No.
Research Area
Metabolism
Alternative Names
APC 2; APC2; Apo CII; Apo-CII; APOC 2; ApoC II; ApoC-II; APOC2; APOC2 protein; APOC2_HUMAN; ApoCII; Apolipoprotein C II; Apolipoprotein C II precursor; Apolipoprotein C2; ApolipoproteinCII; MGC75082; ProapoC-II; Proapolipoprotein C-II
Species
Homo sapiens (Human)
Expression Region
23-101aa
Target Protein Sequence
TQQPQQDEMPSPTFLTQVKESLSSYWESAKTAAQNLYEKTYLPAVDEKLRDLYSKSTAAMSTYTGIFTDQVLSVLKGEE
Mol. Weight
24.9kD
Protein Length
Full Length of Mature Protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Datasheet
Please contact us to get it.

Customer Reviews and Q&A

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Target Background

Function
Component of chylomicrons, very low-density lipoproteins (VLDL), low-density lipoproteins (LDL), and high-density lipoproteins (HDL) in plasma. Plays an important role in lipoprotein metabolism as an activator of lipoprotein lipase. Both proapolipoprotein C-II and apolipoprotein C-II can activate lipoprotein lipase. In normolipidemic individuals, it is mainly distributed in the HDL, whereas in hypertriglyceridemic individuals, predominantly found in the VLDL and LDL.
Gene References into Functions
  1. Results from this exploratory analysis suggest that regulatory element methylation levels within the larger TOMM40-APOE-APOC2 gene region correlate with AD-related biomarkers and TOMM40 or APOE gene expression in AD. PMID: 29371683
  2. Triglyceride-raising variant alleles of the APOC2 encoding apo C-II, associated with clinical Cardiovascular endpoints. PMID: 28534127
  3. The results demonstrate the important role of both intra- and inter-subunit charge interactions in stabilizing apoC-II amyloid fibrils, a process that may be a key factor in determining the general ability of proteins to form amyloid fibrils. PMID: 28229588
  4. The results highlight the importance of charge-pair interactions within the apoC-II fibril core PMID: 26196342
  5. Conformational rearrangement of apoC-II at lipoprotein surfaces promotes interaction with LPL. PMID: 26026161
  6. Large deletion in APOC2 caused by Alu-Alu homologous recombination is associated with 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 apoCII promoter and upregulates apoCII expression only in macrophages. PMID: 22808166
  9. Mutations in GPIHBP1 are rare but the associated clinical phenotype of hypertriglyceridaemia is severe PMID: 22239554
  10. These results 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 experienced 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 the local classical NMR constraints, define the 3D structure of the apoCII-SDS micelle complex and give 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 PMID: 12682050
  21. Hydrolysis activated by APOC2 was faster compared with the LPL-mediated lipolysis of emulsion triolein. The binding density of APOC2 was less for small emulsion surfaces than for large ones. PMID: 12782148
  22. Different levels of secreted apoC-II had little effect on LDL and HDL protein degradation by HepG2 cells. Compared to controls, cells under-expressing apoC-II showed 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 relationship was found between ApoCII polymorphism and coronary disease in the Chinese Han population. PMID: 16459141
  25. Decrease of 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. Taken together these data demonstrate an interaction between antichymotrypsin and apolipoprotein C-II that accelerates fibrillogenesis and indicates a specific role for accessory proteins in protein aggregation. PMID: 17174330
  27. These results suggested that T-->A substitution at position -190 in the apoC-II gene promoter only partly affected transcriptional activity of the apoC-II promoter, leading to decrease of apoC-II expression in quantity. 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 APOC2 gene were found in 10% 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 correlated this 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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Involvement in disease
Hyperlipoproteinemia 1B (HLPP1B)
Subcellular Location
Secreted.
Protein Families
Apolipoprotein C2 family
Tissue Specificity
Liver and intestine.
Database Links

HGNC: 609

OMIM: 207750

KEGG: hsa:344

STRING: 9606.ENSP00000466775

UniGene: Hs.75615

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