Recombinant Human Apolipoprotein CII/ApoC-II / APOC2 Protein

Name: Recombinant Human Apolipoprotein CII/ApoC-II / APOC2 Protein
Brand: Beta LifeScience
SKU: BLA-0106P
Availability: InStock

Collections: Cytokines and growth factors, Other cytokines, Recombinant proteins

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Product Overview

Host Species	Human
Accession	P02655
Synonym	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
Description	Recombinant Human Apolipoprotein CII/ApoC-II / APOC2 Proteinwas expressed in E.coli. It is a Full length protein
Source	E.coli
AA Sequence	MTQQPQQDEMPSPTLLTQVKESLSSYWESAKTAAQNLYEKTYLPAVDEKL RDLYSKSTAAMSTYTGIFTDQVLSVLKGEELEHHHHHH
Molecular Weight	10 kDa including tags
Purity	>95% SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Formulation	Liquid Solution
Stability	The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution	See related COA
Unit Definition	For Research Use Only
Storage Buffer	Shipped on Dry Ice. Store at -20°C. Avoid freeze / thaw cycle.

Target Details

Target 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.
Subcellular Location	Secreted.
Protein Families	Apolipoprotein C2 family
Database References	HGNC: 609 OMIM: 207750 KEGG: hsa:344 STRING: 9606.ENSP00000466775 UniGene: Hs.75615
Associated Diseases	Hyperlipoproteinemia 1B (HLPP1B)
Tissue Specificity	Liver and intestine.

Gene Functions References

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
Triglyceride-raising variant alleles of the APOC2 encoding apo C-II, associated with clinical Cardiovascular endpoints. PMID: 28534127
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
The results highlight the importance of charge-pair interactions within the apoC-II fibril core PMID: 26196342
Conformational rearrangement of apoC-II at lipoprotein surfaces promotes interaction with LPL. PMID: 26026161
Large deletion in APOC2 caused by Alu-Alu homologous recombination is associated with with apolipoprotein C-II deficiency. PMID: 25172036
No APOC2 mutations were identified in a cohort of patients with diabetic lipemia. PMID: 25131724
STAT1 bound on multienhancer 2 cooperates with RXRalpha located on apoCII promoter and upregulates apoCII expression only in macrophages. PMID: 22808166
Mutations in GPIHBP1 are rare but the associated clinical phenotype of hypertriglyceridaemia is severe PMID: 22239554
These results support a predictive change in the ratio of plasma ApoCIII to ApoCII in pregnancies complicated by severe preeclampsia. PMID: 21321243
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
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
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
Includes the observation of APOC4-APOC2 read-through transcription PMID: 8530039
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
Results describe the functional role of the secondary structure in the lipoprotein lipase-binding portion of apolipoprotein CII. PMID: 20042600
Human apolipoprotein C-II (apoC-II) slowly forms amyloid fibers in lipid-free solutions at physiological pH and salt concentrations PMID: 11751863
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
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
regions of lipoprotein lipase that are responsive to activation by apoC-II PMID: 12682050
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
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
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
No relationship was found between ApoCII polymorphism and coronary disease in the Chinese Han population. PMID: 16459141
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
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
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
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
Both common and rare DNA variants of APOC2 gene were found in 10% patients with severe hypertriglyceridemia PMID: 17717288
Phospholipid interaction induces molecular-level polymorphism in APOC2 amyloid fibrils via alternative assembly pathways. PMID: 18005990
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
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
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

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.