Recombinant Human Tissue Plasminogen Activator (mutated S478A) protein
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Recombinant Human Tissue Plasminogen Activator (mutated S478A) protein is a Human Full Length protein, expressed in Insect cells, with >95%, suitable for SDS-PAGE.
View Alternative Names
Tissue-type plasminogen activator, t-PA, t-plasminogen activator, tPA, PLAT
Reactivity data
Product details
This Human TPA Tissue Plasminogen Activator (tPA) has the active site mutation S478A which renders it catalytically inactive. It is >90percent single chain and retains exosite binding as well as other properties of wild type TPA.
Produced using non-baculovirus insect cells.
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
TPA plays a critical role in thrombolysis by breaking down blood clots into their soluble components. It regulates plasminogen function by cleaving this zymogen to yield the active protease plasmin. This function makes tPA integral in maintaining hemostasis and it does not form a part of a larger protein complex. The activity and the regulation of tPA are important for preventing pathologic clotting which can lead to cardiovascular complications.
Pathways
TPA is central to the fibrinolytic pathway. This pathway facilitates the conversion of plasminogen to plasmin enabling clot resolution. In addition tPA interacts with other proteins such as urokinase plasminogen activator (uPA) and inhibitors like plasminogen activator inhibitor-1 (PAI-1). The balance between tPA and its inhibitors is important for the regulation of fibrinolytic activity impacting hemostatic and thrombotic events.
Specifications
Form
Liquid
General info
Function
Converts the abundant, but inactive, zymogen plasminogen to plasmin by hydrolyzing a single Arg-Val bond in plasminogen. By controlling plasmin-mediated proteolysis, it plays an important role in tissue remodeling and degradation, in cell migration and many other physiopathological events. During oocyte activation, plays a role in cortical granule reaction in the zona reaction, which contributes to the block to polyspermy (By similarity).
Sequence similarities
Belongs to the peptidase S1 family.
Post-translational modifications
The single chain, almost fully active enzyme, can be further processed into a two-chain fully active form by a cleavage after Arg-310 catalyzed by plasmin, tissue kallikrein or factor Xa.. Differential cell-specific N-linked glycosylation gives rise to two glycoforms, type I (glycosylated at Asn-219) and type II (not glycosylated at Asn-219). The single chain type I glycoform is less readily converted into the two-chain form by plasmin, and the two-chain type I glycoform has a lower activity than the two-chain type II glycoform in the presence of fibrin.. N-glycosylation of Asn-152; the bound oligomannosidic glycan is involved in the interaction with the mannose receptor.. Characterization of O-linked glycan was studied in Bowes melanoma cell line.
Target data
Complementary Products
Product promise
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