Product nameRecombinant mouse TPA Tissue Plasminogen Activator (mutated ) protein
See all TPA Tissue Plasminogen Activator proteins and peptides
Biological activityab92720 has a double mutation and is permanently single chain and lacks catalytic activity.
Purity> 95 % SDS-PAGE.
ab92720 is purified by immunoaffinity chromatography and sterile filtered.
Expression systemInsect cells
Protein lengthFull length protein
Our Abpromise guarantee covers the use of ab92720 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Preparation and Storage
Stability and Storage
Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.
Constituents: 9.52% HEPES, 0.58% Sodium chloride
This product is an active protein and may elicit a biological response in vivo, handle with caution.
- Plasminogen activator tissue
FunctionConverts 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. Play a direct role in facilitating neuronal migration.
Tissue specificitySynthesized in numerous tissues (including tumors) and secreted into most extracellular body fluids, such as plasma, uterine fluid, saliva, gingival crevicular fluid, tears, seminal fluid, and milk.
Involvement in diseaseNote=Increased activity of TPA results in increased fibrinolysis of fibrin blood clots that is associated with excessive bleeding. Defective release of TPA results in hypofibrinolysis that can lead to thrombosis or embolism.
Sequence similaritiesBelongs to the peptidase S1 family.
Contains 1 EGF-like domain.
Contains 1 fibronectin type-I domain.
Contains 2 kringle domains.
Contains 1 peptidase S1 domain.
DomainBoth FN1 and one of the kringle domains are required for binding to fibrin.
Both FN1 and EGF-like domains are important for binding to LRP1.
The FN1 domain mediates binding to annexin A2.
The second kringle domain is implicated in binding to cytokeratin-8 and to the endothelial cell surface binding site.
modificationsThe 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.
Cellular localizationSecreted > extracellular space.
- Information by UniProt
ab92720 has not yet been referenced specifically in any publications.