Recombinant Human Apolipoprotein A-Ii (APOA2) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-00823P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.

Recombinant Human Apolipoprotein A-Ii (APOA2) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-00823P
Regular price $456.00 Sale price $349.00Save $107
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Product Overview

Description Recombinant Human Apolipoprotein A-Ii (APOA2) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 85% as determined by SDS-PAGE.
Uniprotkb P02652
Target Symbol APOA2
Species Homo sapiens (Human)
Expression System E.coli
Tag N-6His-SUMO
Target Protein Sequence QAKEPCVESLVSQYFQTVTDYGKDLMEKVKSPELQAEAKSYFEKSKEQLTPLIKKAGTELVNFLSYFVELGTQPATQ
Expression Range 24-100aa
Protein Length Full Length of Mature Protein
Mol. Weight 21.7 kDa
Research Area Cancer
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.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
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 May stabilize HDL (high density lipoprotein) structure by its association with lipids, and affect the HDL metabolism.
Subcellular Location Secreted.
Protein Families Apolipoprotein A2 family
Database References
Tissue Specificity Plasma; synthesized in the liver and intestine.

Gene Functions References

  1. Weight loss resulted from a reduction of HDL in both APOE-II genotypes. However, in C homozygote carriers, it was shown that HDL3 reduced significantly and leads to a general shift toward larger size HDL subfractions after intervention, while in T allele carriers HDL2 decreased significantly and weight loss leads to shift toward smaller size HDL subfractions. PMID: 28545455
  2. There was a statistically significant interaction between APOA2 polymorphism and dietary fatty acids intake on oxidative stress n patients with type 2 diabetes PMID: 27271094
  3. This study detected a reduced level of heterodimer apoA2-ATQ/AT and a specific apoA2 isoform hypo-processing pattern in the sera of autoimmune pancreatitis patients. PMID: 29481802
  4. In type 2 diabetes mellitus patients, the dietary intake of antiinflammatory fatty acids, such as omega-3 PUFAs and MUFAs, could reduce the inflammatory effects associated with the Apolipoprotein A2 CC genotype. In addition, proinflammatory fatty acids, such as SFAs, could overcome the antiinflammatory effect of the T-allele. PMID: 28359369
  5. data support an SR-B1 nibbling mechanism that is similar to that of streptococcal serum opacity factor, which also selectively removes CE and releases apoAI, leaving an apoAII-rich remnant. PMID: 28373285
  6. A new missense mutation in an Iranian population has a significant association with high-density lipoprotein cholesterol levels. PMID: 26590203
  7. ApoAII-ATQ/AT not only distinguished the early stages of pancreatic cancer from healthy controls but also identified patients at high risk for pancreatic malignancy. PMID: 26549697
  8. Plasma apoB pool size of VLDL containing apoA-II is much smaller than that of VLDL without apoA-II, and this was caused by a very low rate of secretion of this VLDL type into plasma. PMID: 26071654
  9. APOA-II polymorphism and oxidative stress is associated with poor prognosis in patients with type 2 diabetes. PMID: 26104730
  10. Apolipoprotein AII was detected as a protein associated with the urinary protein/urinary creatinine levels in pediatric idiopathic steroid-sensitive nephrotic syndrome PMID: 24633472
  11. Apolipoprotein A-II/B significantly improves risk prediction of overall survival, also in carotid surgery patients with lower LDL levels PMID: 25953375
  12. Apolipoprotein A-II and the regulation of high density lipoproteins in cardiovascular disease. [Review] PMID: 24012775
  13. We have cloned the cDNA encoding human ApoA-II and achieved its high-level secreting expression with a yield of 65 mg/L of yeast culture PMID: 24116940
  14. identified a statistically significant interaction between the APOA2 -265T > C variant and higher-fat dairy food intake in the Boston Puerto Ricans and replicated this relation in the GOLDN study PMID: 24108135
  15. Clinical studies demonstrate that apoA-II is a strong predictor of risk for CVD. There is no evidence, however, that selective therapeutic modification of apoA-II impacts on atherosclerosis and clinical outcomes.[review] PMID: 21501035
  16. These data suggest Apo-AII-containing high-density lipoproteins (HDL) formed intrahepatically are likely cholesterol-rich compared to the smaller intracellular lipid-poor Apo A-I HDL. PMID: 23025327
  17. Enrichment of apo A-II in high-density lipoprotein particles has atheroprotective effects and apo A-II may become a target for the treatment of atherosclerosis. PMID: 23241412
  18. We conclude that apoA-II plays a significant role in apoE-associated risk of incident CVD in women with high levels of HDL-C and CRP. PMID: 22723940
  19. APOA2 m265 genotype may be associated with eating behaviours and dietary modulation of plasma ghrelin. PMID: 21386805
  20. a gene-diet interaction involving the APOA2 -265T>C SNP and saturated fat intake determines body weight in a Mediterranean and an Asian populations PMID: 20975728
  21. Human apolipoprotein A-II inhibits the production of interferon-gamma by concanavalin A-stimulated mouse and human CD4-positive T cells. PMID: 21300819
  22. Low apolipoprotein-A2 is associated with metastatic renal cell cancer. PMID: 20022911
  23. ApoA-II plays a crucial role in triglyceride catabolism by regulating lipoprotein lipase activity, at least in part, through HDL proteome modulation. PMID: 19910634
  24. The serum apoA-II concentrations confer risk for MetS and diabetes and exhibit evidence of anti-inflammatory properties among Turks. PMID: 19817643
  25. In metabolic syndrome, fenofibrate, but not atorvastatin, influences high density lipoprotein metabolism by increasing the transport of APOA2 particles. PMID: 19651918
  26. when expressed in transgenic mice, HDL shows antioxidant properties PMID: 11971944
  27. Overexpression in transgenic mice does not increase their susceptibility to insulin resistance and obesity PMID: 12032642
  28. Evaluated as a positional candidate gene for familial Type II diabetes, altered lipid concentrations, and insulin resistance PMID: 12136402
  29. Crystallographic studies of apo A-II and its complex with lipid surrogate beta-octyl glucoside show that disulfide-linked dimers of apo A-II form amphipathic alpha-helices which aggregate into tetramers. PMID: 12269810
  30. Carriers of a novel splice-site mutation in the LDL-receptor gene were simultaneously homozygous for the -265C variant of apoA-II thus concluding that one variant of the apoA-II gene was associated with reduced plasma LDL cholesterol in FH patients PMID: 12522687
  31. This protein inhibits high density lipoprotein remodeling and lipid-poor apolipoprotein A-I formation PMID: 12690114
  32. Genetic association of plasma apolipoprotein A-II levels with familial combined hyperlipidemia. PMID: 12738753
  33. Analysis of trancription factors that bind response elements in the apoA-II promotor and modulate transcription. PMID: 12959642
  34. apoA-II affects both the structure and the dynamic behavior of HDL particles and selectively modifies lipid metabolism PMID: 14967812
  35. In transgenic mice overexpressing the human apoA-II gene, plasma human apoA-II concentration was positively correlated with blood glucose levels. PMID: 14988251
  36. this protein-exonic splicing enhancer interaction is able to promote the incorporation of exon 3 in mRNA and suggest that they can rescue the splicing despite the noncanonical 3' splice site. PMID: 15247216
  37. Overexpressed human apoA-II in mice impairs HDL protection of apoB-lipoproteins from oxidation. Displacement of PON1 by apoA-II may explain why PON1 is found in HDL particles with apoA-I, not apoA-II, & apo-A-II-rich HDL's poor antiatherogenic properties. PMID: 15388641
  38. results indicate a significant association between the T265C APOA-II polymorphism and levels of visceral adipose tissue in premenopausal women present in white but not African-American women PMID: 15833935
  39. Characterization of regulatory elements found in the apoA-II exon 3 and its flanking introns that are involved in the control of apoA-II exon 3 splicing. PMID: 16254078
  40. the association of apoA-II with triglyceride-rich lipoproteins occurs in the circulation and induces postprandial hypertriglyceridemia PMID: 16990646
  41. ApoA-II adopts a beltlike structure in which the protein helices wrap around the lipid- bilayer reconstituted high density lipoprotein (rHDL) disc. PMID: 17264082
  42. ApoAII is efficiently reabsorbed in kidney proximal tubules in relation to its plasma concentration PMID: 17652309
  43. carriers of the minor allele for Apo A-II -265T/C (CC/TC) have a lower postprandial response compared with TT homozygotes PMID: 17709437
  44. ApoA-II is associated with a decreased risk of future coronary artery disease in apparently healthy people, implying that apoA-II itself exerts effects on specific antiatherogenic pathways. PMID: 17923573
  45. APOAII rs5082 polymorphism may have a role in reducing risk of coronary artery disease in an Australian male population PMID: 18179799
  46. results for dimeric apolipoprotein AII are similar to those we have reported for the monomeric apolipoprotein CI, which has a similar secondary structure but a different peptide sequence and net charge PMID: 18652418
  47. procoagulant activities of plasma factor VIIc and factor Xc are positively and independently associated with concentrations of the high-density lipoprotein apolipoprotein, apo A-II PMID: 18766253
  48. small sizes (i. e., number of kringle-4 repeats in the gene) of apolipoprotein (a) are risk factors for the development of atherothrombosis. (review) PMID: 19069164
  49. Results indicate that CETP inhibition increases plasma concentrations of apoA-II by delaying HDL apoA-II catabolism and significantly alters the remodeling of apoA-II-containing HDL subpopulations. PMID: 19193611
  50. The available data does not support a role for common variants in APOA2 on type 2 diabetes susceptibility or related quantitative traits in Northern Europeans PMID: 19216768

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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.

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