tPA and PAI-1 Deficient – Depleted Plasma
tPA and PAI-1 Deficient – Depleted Plasma is manufactured from normal citrated human plasma that has been depleted of both tPA (Tissue Plasminogen Activator) and PAI-1 (Plasminogen Activator Inhibitor – type 1) by selective affinity immuno-adsorption using antibodies directed towards tPA and PAI-1.
Only the highest quality citrated plasma is used as starting material and in many cases the parent plasma is available as control material. Plasma products are typically buffered with the addition of HEPES to 20mM final concentration and are available in 1ml vials to litre quantities. Our tPA/PAI deficient – depleted plasma can be used for further manufacturing or research use only applications.
Product Code: TPA/PAI-DP
Presentation: Frozen tPA and PAI-1 Deficient – Depleted Plasma
Preparation/Handling: Thaw 1 ml vials in 37oC water bath for 5 minutes; for bulk volumes, thawing time will be dependent on bottle size.
Storage and Stability: Plasma is shipped frozen and should be stored below -60oC. Product is stable until date stated on vial label when stored at -60oC. Once thawed, plasma is stable for 4 hours at 2-8oC in original vial.
Specifications: Plasma is deficient of tPA antigen to ≤0.5 ng/mL and deficient of PAI-1 to <0.5ng/mL – normal for PT, APTT and Fibrinogen levels.
Description of Tissue Plasminogen Activator (tPA)
Tissue-type plasminogen activator (tPA) is one of two major physiologic activators of plasminogen in plasma. It is a serine protease of 68 kDa produced primarily in endothelial cells but is also present in monocytes and megakaryocytes. Normal plasma tPA antigen concentrations have been reported from 20 ng/ml to 5 μg/ml, depending on the assay used, but typically most of the tPA (> 90%) is in complex with it’s primary inhibitor, plasminogen activator inhibitor-1 (PAI-1). Structurally, tPA is a single-chain enzyme that consists of a catalytic domain followed by two kringle structures, an EGF domain and a finger domain. The activation of plasminogen by tPA is dependent on the presence of a fibrin cofactor. The binding of both tPA and plasminogen to fibrin is mediated in part through lysine binding sites within the kringle structures of both enzyme and substrate, but also through the finger domain of tPA. Activation of plasminogen by tPA occurs by cleavage after residue Arg560 to produce the two-chain active serine protease plasmin. The activity of tPA is regulated in part by a very short half life in circulation (t½ of ~4 minutes) and by circulating protease inhibitors PAI-1 and to a lesser extent α2macroglobulin1-3.