Purified from human plasma that has been tested and found to be negative for HIV, HCV and HBsAg antibodies. After coating onto ELISA plates the product will bind autoantibodies to β2-glycoprotein 1.
Target
APOH
Purity
The β2-glycoprotein 1 autoantigen (54 kDa) is more than 95% pure, as assessed by SDS gel electrophoresis.
Concentration
0.5-2.0 mg/ml
Preservative
None
Storage
The product is stabilised with 20% glycerol and 0.1% Micr-O-protect TM. Store at -20°C or below (long term) or at +4°C (short term). Avoid repeated freezing and thawing. Mix thoroughly before use.
Apolipoprotein H (Apo-H), previously known as (β2-glycoprotein I, beta-2 glycoprotein I), is a multifunctional apolipoprotein. One of its functions is to bind cardiolipin. When bound the structure of cardiolipin and Apo-H both undergo large changes in structure. Within the structure of Apo-H is a stretch of positively charged amino acids, (protein sequence positions 282-287) Lys-Asn-Lys-Glu-Lys-Lys, are involved in phospholipid binding (See image on right). Apo-H has a complex involvement in agglutination, it appears to alter ADP mediated agglutination of platelets. Normally Apo-H assumes an anti-coagulation activity in serum (by inhibiting coagulation factors), however changes in blood factors can result of a reversal of that activity.
Have you cited DAG-T1240 in a publication? Let us know and earn a reward for your research.
Background
Beta-2-glycoprotein-I (β2GPI, apolipoprotein H, Apo H) is a glycoprotein produced by liver cells and is a glycoprotein produced by hepatocytes. It exists in plasma in either a free or lipoprotein variant depending on its purpose. Anti-Beta-2GPI antibodies are the most prevalent antiphospholipid syndrome antibodies, which along with phospholipids or phospholipid complexes (anticardiolipin antibodies, lupus anticoagulants) make up antiphospholipid antibodies (aPL). There are low-titer, low affinity natural Beta-2GPI antibodies in most healthy plasma.
β2GPI belongs to the complement control protein superfamily and consists of five highly homologous complement control domains in tandem. β2GPI has at least two conformations in plasma, and in the free state, domain I and domain V interact to form a closed 'O' shape. When encountering the exposed surface of the negative phospholipid, due to the strong affinity of domain V for the negative phospholipid, the closed loop will open and form a fishhook-like structure 'J' anchored to the surface of the negative phospholipid. β2GPI conformational changes can be caused by molecular interactions, post-translational modifications, genetic alterations, or changes in the internal environment. That conformational switch reveals an obscure domain I epitope to which the anti-β2GPI antibody binds. When β2GPI antigen-antibody complexes are formed, autoimmune patients are more susceptible to thrombosis. Other researchers speculated that there are many intermediate types of β2GPI, which account for β2GPI's many reactive functions in the body.
Figure 1. Proposed structural states of β2GPI and the transition to cellular binding (Source: McDonnell T, et al. 2020)
It turns out that β2GPI is critical for controlling bleeding/coagulation, complement, angiogenesis and immunity. β2GPI works as an anticoagulant by preventing the production of coagulation factors and thrombospondin complexes and endogenous adenosine diphosphate-induced platelet aggregation. In addition, β2GPI has the ability to bind anionic substances such as lipoproteins, phospholipids, and heparin. The negative charge of lipoprotein molecules increased significantly after oxidation by Cu2+, and the affinity with β2GPI was also enhanced, and a more stable complex could be formed with β2GPI. The study of the function of β2GPI may be of great value in aiding the diagnosis, treatment and prognosis of a wide range of hematological disorders in clinical practice.
Alternative Names
β2GPI Antigen Beta-2GPI Antigen β2GP1 Antigen
References
1. Brusch A. The Significance of Anti-Beta-2-Glycoprotein I Antibodies in Antiphospholipid Syndrome. Antibodies (Basel). 2016 Jun 8;5(2):16.
2. McDonnell T, et al. The role of beta-2-glycoprotein I in health and disease associating structure with function: More than just APS. Blood Rev. 2020 Jan;39:100610.
Creative Diagnostics products are for RESEARCH USE ONLY, please make sure your review is research based.
Required fields are marked with *
Terms and conditions:
We will select high-quality review customers and offer a $30 coupon for your next purchase.
All product reviews must be submitted in the English language.
Creative Diagnostics will not share any personal information of applicants, and all information will be treated with strict confidentiality and will not be sold or disclosed to a third party.
References
Plasmodium berghei EXP-1 interacts with host Apolipoprotein H during Plasmodium liver-stage development
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Authors: Sa e Cunha, Claudia; Nyboer, Britta; Heiss, Kirsten; Sanches-Vaz, Margarida; Fontinha, Diana; Wiedtke, Ellen; Grimm, Dirk; Przyborski, Jude Marek; Mota, Maria M.; Prudencio, Miguel; Mueller, Ann-Kristin
The first, obligatory replication phase of malaria parasite infections is characterized by rapid expansion and differentiation of single parasites in liver cells, resulting in the formation and release of thousands of invasive merozoites into the bloodstream. Hepatic Plasmodium development occurs inside a specialized membranous compartment termed the parasitophorous vacuole (PV). Here, we show that, during the parasite's hepatic replication, the C-terminal region of the parasitic PV membrane protein exported protein 1 (EXP-1) binds to host Apolipoprotein H (ApoH) and that this molecular interaction plays a pivotal role for successful Plasmodium liver-stage development. Expression of a truncated EXP-1 protein, missing the specific ApoH interaction site, or down-regulation of ApoH expression in either hepatic cells or mouse livers by RNA interference resulted in impaired intrahepatic development. Furthermore, infection of mice with sporozoites expressing a truncated version of EXP-1 resulted in both a significant reduction of liver burden and delayed blood-stage patency, leading to a disease outcome different from that generally induced by infection with wildtype parasites. This study identifies a host-parasite protein interaction during the hepatic stage of infection by Plasmodium parasites. The identification of such vital interactions may hold potential toward the development of novel malaria prevention strategies.
Population distributions of APOE, APOH, and APOA4 polymorphisms and their relationships with quantitative plasma lipid levels among the Evenki herders of Siberia
We examined the distributions of seven polymorphic sites in three apolipoprotein genes (APOE, APOA4, and APOH) and their relationships with quantitative lipid levels (total cholesterol, LDL cholesterol, HDL cholesterol, and triglycerides) among the Evenki reindeer herders of central Siberia. The polymorphism data reveal several distinctive features that differentiate the Evenki from white populations: the near absence of the APOE*2 allele, the highest ever recorded frequency of the APOH*3 allele, the complete absence of the APOA*2 allele at codon 360, and significantly different frequencies at three other APOA4 polymorphic sites. Our analyses of the relationships of common apolipoprotein polymorphism and plasma lipid levels also revealed interesting results, The well-established positive association between the APOE*4 allele and LDL cholesterol level reported in white populations was not seen in the Evenki despite a comparable frequency of the APOE*4 allele. Because the Evenki have significantly lower cholesterol levels than Westernized whites, this difference in allelic effect probably reflects gene-diet interaction, which modulates the effect of APOE polymorphism on LDL cholesterol. At the APOA4 locus the HincII polymorphism at codon 127 shows a significant impact on plasma triglyceride variation in the Evenki sample: The HincII - allele was associated with higher triglyceride levels than the HincII + allele. Our data indicate that both the genetic and the environmental factors conventionally associated with cardiovascular disease risk in Western societies are different in the Evenki.
COA
Publication 
Figure 1. Proposed structural states of β2GPI and the transition to cellular binding
Loading ......
