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Official Full Name Phosphatidyl Serine
Background The first study of anti-phospholipid antibodies began in 1906, when Wasserman introduced a serological test for syphilis. In 1942, the active component was found to be a phospholipid, which was designated cardiolipin. In the 1950s it became clear that a number of people had positive tests for syphilis without any evidence of the disease. This phenomenon was referred to as the biological false positive serological test for syphilis. A high prevalence of autoimmune disorders, including systemic lupus erythematosus (SLE) and Sj?gren′s syndrome occurred in this group of patients. The presence of circulating anticoagulants in patients with SLE was first documented in 1952 and was associated with increased risk of paradoxical thrombosis in 1963. The term lupus anticoagulant (LA), first used in 1972, is clearly a misnomer, because LA is more frequently encountered in patients without lupus and is associated with thrombosis rather than abnormal bleeding. During the last years it became clear that the optimal binding of anti-phospholipid antibodies is depending on a cofactor termed beta-2-glycoprotein I (apolipoprotein H) (β2GPI). β2GPI is a 50 kDa beta-2-globulin occurring in plasma at a level of 200 μg/ml. It has been found that beta-2-Glycoprotein I inhibits the intrinsic coagulation pathway and, therefore, it is involved in the regulation of blood coagulation. β2GPI is associated in vivo with negatively-charged substances, e.g. anionic phospholipids, heparin and lipoproteins. The phospholipid binding region is located on its fifth domain. Under the acronym "aPL" (anti-phospholipid antibodies) antibodies against negatively-charged phospholipids, such as CL (cardiolipin), LA (lupus anticoagulant), PS (phosphatidyl serine), PI (phosphatidyl inositol) and PA (phosphatidic acid) are summarised. Of these, cardiolipin is the phospholipid most commonly used as antigen to test for aPL by ELISA. Some antisera which bind cardiolipin-coated ELISA plates can also bind to plates coated with other negatively-charged phospholipids, such as phosphatidyl serine (PS), phosphatidyl inositol and phosphatidic acid (PA). Some investigators have suggested that the use of PS in place of cardiolipin in ELISA tests enables more specific diagnosis. These antigens are less commonly used and their additional use can improve the clinical sensitivity in patient samples with suspected APS (anti-phospholipidsyndrome), but they can't replace the measurement of autoantibodies against cardiolipin. The Scientific and Standardization Committee of the International Society on Thrombosis and Hemostasis has issued consensus criteria that may be used to help laboratory diagnosis.
Synonyms Phosphatidyl Serine; Phosphatidylserine; Ptd-L-Ser; PS
    • Species :
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    Species Cat.# Product name Source (Host) Tag Protein Length Price
    Kit-0740 Phosphatidylserine Apoptosis Kit (Blue Fluorescence 405) N/A
    Kit-0741 Phosphatidylserine Apoptosis Kit (Blue Fluorescence) N/A
    Kit-0742 Phosphatidylserine Apoptosis Kit (Deep Red Fluorescence) N/A
    Kit-0743 Phosphatidylserine Apoptosis Kit (Deep Red Fluorescence) N/A
    Kit-0744 Phosphatidylserine Apoptosis Kit (Green Fluorescence 405) N/A
    Kit-0745 Phosphatidylserine Apoptosis Kit (Green Fluorescence) N/A
    Kit-0746 Phosphatidylserine Apoptosis Kit (Green Fluorescence) N/A
    Kit-0747 Phosphatidylserine Apoptosis Kit (Orange Fluorescence) N/A
    Kit-0748 Phosphatidylserine Apoptosis Kit (Red Fluorescence) N/A

    ps involved in several pathways and played different roles in them. We selected most pathways ps participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with ps were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

    Pathway Name Pathway Related Protein

    ps has several biochemical functions, for example, . Some of the functions are cooperated with other proteins, some of the functions could acted by ps itself. We selected most functions ps had, and list some proteins which have the same functions with ps. You can find most of the proteins on our site.

    Function Related Protein

    ps has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with ps here. Most of them are supplied by our site. Hope this information will be useful for your research of ps.

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