Urokinase Human - 1mg

enzyme
enzymeenzyme
Catalog #: ENZ-264Description:Urokinase is a two-chain glycoprotein containing 411 amino acids with 12 disulfide bonds. Its molecular weight is 54,000 Dalton.Synonyms:Urokinase, Abbokinase, Urokinase-type Plasminogen Activator,uPA, EC 3.4.21.73, UK.Source:Human urine.Purity:Greater than 90.0% as det ...Read more
Catalog # ENZ-264 $200.00 each


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  • Description
  • Specifications

Catalog #: ENZ-264

Description:
Urokinase is a two-chain glycoprotein containing 411 amino acids with 12 disulfide bonds. Its molecular weight is 54,000 Dalton.

Synonyms:
Urokinase, Abbokinase, Urokinase-type Plasminogen Activator,uPA, EC 3.4.21.73, UK.

Source:
Human urine.

Purity:
Greater than 90.0% as determined by SDS-PAGE.

Free of: Hepatitis B surface antigen, Hepatitis C antibody and HIV I and II.

Solubility:
It is recommended to reconstitute the lyophilized Urokinase in sterile 18MΩ–cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

Formulation:
The Urokinase was lyophilized from a concentrated (1mg/ml) solution containing phosphate buffer.

Stability:
Lyophilized Urokinase although stable at room temperature for 3 weeks, should be stored desiccated below -18 °C. Upon reconstitution Urokinase should be stored at 4 °C between 2-7 days and for future use below -18 °C.
Please prevent freeze-thaw cycles.

Activity:
1nM UK will cause a change in absorbance of 0.001 at 405nm in 1 minute at R/T in 100 ul 0.05M Tris-HCl, 0.1M NaCl, pH 7.4, using S2444 (0.6mM) as the substrate.

Specific Activity:
83,700IU/mg.

Physical Appearance:
Sterile Filtered White lyophilized (freeze-dried) powder.

Usage:
Denovo Biotechnology's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

References:
1. Title:Transient ?-catenin stabilization modifies lineage output from human thymic CD34+CD1a– progenitors.
Publication:Published online before print December 1, 2009, doi: 10.1189/jlb.0509344 March 2010 Journal of Leukocyte Biology vol. 87 no. 3 405-414 .
Link:http://www.jleukbio.org/content/87/3/405.full
2.Title:Activation of human pro-urokinase by unrelated proteases secreted by Pseudomonas aeruginosa.
Publication:Received 26 November 2009/18 March 2010; accepted 2
Link:http://www.biochemj.org/bj/428/0473/bj4280473.htm

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