Recombinant human Tissue Plasminogen Activator (mutated ) protein (ab92635)
Key features and details
- Expression system: Insect cells
- Purity: > 95% SDS-PAGE
- Active: Yes
- Suitable for: SDS-PAGE
Description
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Product name
Recombinant human Tissue Plasminogen Activator (mutated ) protein
See all Tissue Plasminogen Activator proteins and peptides -
Biological activity
ab92635 has a double mutation and is permanently single chain and lacks catalytic activity. -
Purity
> 95 % SDS-PAGE. -
Expression system
Insect cells -
Protein length
Full length protein -
Animal free
No -
Nature
Recombinant -
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Species
Human
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Associated products
Specifications
Our Abpromise guarantee covers the use of ab92635 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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Applications
SDS-PAGE
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Form
Liquid -
Concentration information loading...
Preparation and Storage
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Stability and Storage
Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.
pH: 7.40
Constituents: 9.52% HEPES, 0.58% Sodium chlorideThis product is an active protein and may elicit a biological response in vivo, handle with caution.
General Info
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Alternative names
- Alteplase
- DKFZp686I03148
- Plasminogen activator tissue
see all -
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. Play a direct role in facilitating neuronal migration. -
Tissue specificity
Synthesized 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 disease
Note=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 similarities
Belongs 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. -
Domain
Both 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. -
Post-translational
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 localization
Secreted > extracellular space. - Information by UniProt
Protocols
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
Datasheets and documents
References (0)
ab92635 has not yet been referenced specifically in any publications.
