Recombinant Human Apolipoprotein C-Ii (APOC2) Protein (His)

Name: Recombinant Human Apolipoprotein C-Ii (APOC2) Protein (His)
Brand: Beta LifeScience
SKU: BLC-06096P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality cytokines for advanced research, High-quality recombinant proteins

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Product Overview

Description	Recombinant Human Apolipoprotein C-Ii (APOC2) Protein (His) is produced by our Yeast expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P02655
Target Symbol	APOC2
Synonyms	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 System	Yeast
Tag	N-6His
Target Protein Sequence	TQQPQQDEMPSPTFLTQVKESLSSYWESAKTAAQNLYEKTYLPAVDEKLRDLYSKSTAAMSTYTGIFTDQVLSVLKGEE
Expression Range	23-101aa
Protein Length	Full Length of Mature Protein
Mol. Weight	10.9kDa
Research Area	Metabolism
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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: 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.