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Urokinase / PLAU (activated by trypsin) Protein (His Tag) PDF Download

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 )

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:
SDS-PAGE

Urokinase / PLAU ( activated by trypsin ) protein

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
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
  1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
  2. Please contact us for any concerns or special requirements.

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

  1. Nagai, M. et al., 1985, Gene. 36:183-188.
  2. Jacobs, P. et al., 1985, DNA. 4:139-146.
  3. Geiger, M. et al., 1989, Blood. 74 (2): 722-728.
  4. Ploug, M. et al., 2002, Biochem. Soc. Trans. 30 (2): 177–183.
  5. Duffy, M.J., 2002, Biochem. Soc. Trans. 30: 207-210.
  6. Alfano, M. et al., 2004, J. Leukoc. Biol. 74 (5): 750–756.

 

uPA/Urokinase related areas, pathways, and other information