Pro-Urokinase, human recombinant protein
Single chain Urokinase-type plasminogen activator (scuPA), Urokinase-type Plasminogen Activator uPA,
|Calculated MW||49.3 kDa|
|Other Names||Single chain Urokinase-type plasminogen activator (scuPA), Urokinase-type Plasminogen Activator uPA, PLAU.|
|Results||>1200 mU/mg (1 U = Digestion of 1 µmole of Z-GGR-AMC substrate in 1 min at 37ºC.)|
|Application Notes||Briefly spin down the vial and reconstitute in water to 0.5-1 mg/ml and store at –80°C.|
|Storage||-20°C; Lyophilized from proprietary buffer.|
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Provided below are standard protocols that you may find useful for product applications.
Urokinase or Urokinase-type plasminogen activator (uPA) is a serine protease (EC 18.104.22.168). It is secreted as a single-chain zymogen, pro-Urokinase, possessing little or no intrinsic enzymatic activity. The single chain zymogen is converted into the active two chain enzyme (tcuPA) by cleavage of the bond between Lys157 and Ile158. After activation, Urokinase specifically cleaves the proenzyme plasminogen to form the active enzyme plasmin. The active plasmin then catalyzes the breakdown of fibrin polymers of blood clots. Urokinase is involved in a number of biological functions including fibrinolysis, embryogenesis, cell migration, tissue remodeling, ovulation, and wound healing. Additionally, it is a potent marker of invasion and metastasis in a variety of human cancers associated with breast, stomach, colon, bladder, ovary, brain and endometrium.
Holmes W.E.,et al.Biotechnology (N.Y.) 3:923-929(1985).
Jacobs P.,et al.DNA 4:139-146(1985).
Nagai M.,et al.Gene 36:183-188(1985).
Riccio A.,et al.Nucleic Acids Res. 13:2759-2771(1985).
Kalnine N.,et al.Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
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