Proteins For Sale

Miniplasminogen and Microplasminogen

Breakdown of a fibrin clot into soluble components depends on plasmin (Plm), a serine protease that is derived from the freely circulating zymogenic proenzyme plasminogen (Plg). The activated Plg is transformed into two separate subunits interconnected by two disulfide bridges. The A chain of the Plm molecule consists of 5 triple-loop disulfide kringle (Kr) domains (approximately 78-80 amino acids each), while the B chain contains a "linker" region of 20 amino acids and a serine protease domain (approximately 228 amino acids) .

Through laboratory manipulations, we have successfully created two des-kringle variants of plasminogen with potential pharmacological applications, miniplasminogen (mini-Plg) and microplasminogen (µPlg). Mini-Plg consists of only kringle 5, the linker, and the serine protease domain, while µPlg consists of only of the linker and serine protease domain itself. µPlg and mini-Plg can also be activated to microplasmin (µPlm) or miniplasmin (mini-Plm) respectively, by digestion at the peptide bond between R561 and V562 by tPA or uPA , again forming two separate subunits interconnected by the same two disulfide bridges.

µPlg and mini-Plg are potentially more potent and fast acting than other thrombolytic therapies. Moreover, they can eliminate the risk of life-threatening intracranial hemorrhage usually associated with plasminogen activators.

For pricing and other information, please contact zhu at proteomtech-inc.com.

Reference:
Refolding, purification, and activation of miniplasminogen and microplasminogen isolated from E. coli inclusion bodies
Dan Medynski, Michael Tuan, Wayne Liu, Shili Wu and Xinli Lin
Proteomtech Inc., 3505 Cadillac Ave., STE F7, Costa Mesa, CA 92626, USA
Protein Expression and Purification Volume 52, Issue 2, April 2007, Pages 395-402

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