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> Recombinant Protein > Human Cell Expressed > Urokinase / PLAU (activated by trypsin) Protein (His Tag) Urokinase / PLAU (activated by trypsin) Protein (His Tag)
| Catalog | Size (Price) | Quantity | In Stock | Operation | Other Information |
| 10815-H08H-A |
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Plasminogen activator, urokinase Protein Datasheet
Urokinase / PLAU ( activated by trypsin ) Protein Price Inquiry ( Available Sizes )
- 50μg: Inquiring Price;
- 200μg: Inquiring Price;
- ≥1mg Bulk: Inquiring Price
Urokinase / PLAU ( activated by trypsin ) Protein Product Information
| Synonym : | PLAU ,ATF, UPA, URK, u-PA |
| Protein Construction: | A DNA sequence encoding the human PLAU (NP_002649.1) ( Met 1-Leu 431 ) with a C-terminal polyhistidine tag was expressed. The purified protein was activated by trypsin in vitro. |
| Source: | Human |
| Expression Host: | Human Cells |
Urokinase / PLAU ( activated by trypsin ) Protein QC Testing
| Purity: | > 97 % as determined by SDS-PAGE. | SDS-PAGE:![]() Urokinase / PLAU ( activated by trypsin ) protein |
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Bio-activity: |
Measured by its ability to cleave a peptide substrate, N-carbobenzyloxy-Gly-Gly-Arg-7-amido-4-methylcoumarin (Z-GGR-AMC). The specific activity is > 2000 pmoles/min/μg |
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| Endotoxin: | < 1.0 EU per μg of the protein as determined by the LAL method | |
| Stability: | Samples are stable for up to twelve months from date of receipt at -70℃ | |
| Predicted N terminal: | Ser 21 | |
| Molecular Mass: | The secreted recombinant human PLAU comprises 422 amino acids with a predicted molecular mass of 46 kDa. As a result of glycosylation and cleavage, rhPLAU migrates as three bands corresponding to the long α chain, β chain and unprocessed full-length PLAU with the molecular mass of 18, 32 and 50 kDa respectively in SDS-PAGE under reducing conditions. | |
| Formulation: | Lyophilized from sterile PBS, pH7.4
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Urokinase / PLAU ( activated by trypsin ) Protein Usage Guide
| Storage: | Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles. |
| Reconstitution: | A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information. |
Urokinase / PLAU ( activated by trypsin ) Protein Related Products & Topics
Related Areas:
Enzyme>>Protease & Regulator>>Serine Protease & Regulator>>Urokinase/PLAU/u-PA
Cancer>>Cancer Biomarkers>>Urokinase/PLAU/u-PA
Immunology>>Innate Immunity>>Coagulation>>Urokinase/PLAU/u-PA
Cardiovascular>>Coagulation>>Urokinase/PLAU/u-PA
Proteins:
| Urokinase/PLAU/u-PA | Human | Urokinase/PLAU/u-PA Protein, Recombinant![]() |
10815-H08H |
Antibodies:
| Human Urokinase/PLAU/u-PA | WB | Mouse Monoclonal Antibody | 10815-MM01 |
| Human Urokinase/PLAU/u-PA | WB | Mouse Monoclonal Antibody | 10815-MM02 |
| Human Urokinase/PLAU/u-PA | ELISA | Mouse Monoclonal Antibody | 10815-MM03 |
Urokinase / PLAU ( activated by trypsin ) Protein Description
Plasminogen activator, urokinase, also known as?PLAU and UPA, is a serine protease involved in degradation of the extracellular matrix and possibly tumor cell migration and proliferation. The human PLAU is initially synthesized as 431 amino acid precursor with a N-terminal signal peptide (20 residues). The single chain molecule is processed into a disulfide-linked two-chain molecule of different molecular weights. Two forms of the A chain exist, starting at Ser21 (the long form) and Lys156 (the short form). The long and short A chains are unique to the high and low molecular weight forms, respectively. The long A chain contains an EGF-like domain, responsible for binding of the PLAU receptor. The B chain corresponds to the catalytic domain. PLAU is a potent marker of invasion and metastasis in a variety of human cancers associated with breast, stomach, colon, bladder, ovary, brain and endometrium. A specific polymorphism in PLAU gene is implicated in late-onset Alzheimer disease and also with decreased affinity for fibrin-binding.
References
- Nagai, M. et al., 1985, Gene. 36:183-188.
- Jacobs, P. et al., 1985, DNA. 4:139-146.
- Geiger, M. et al., 1989, Blood. 74 (2): 722-728.
- Ploug, M. et al., 2002, Biochem. Soc. Trans. 30 (2): 177–183.
- Duffy, M.J., 2002, Biochem. Soc. Trans. 30: 207-210.
- Alfano, M. et al., 2004, J. Leukoc. Biol. 74 (5): 750–756.
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