Reconstitute with 20mM Tris and 150mM NaCl to 0.1-1.0mg/ml. Do not vortex. Lyophilized from 20mM Tris, 150mM NaCl, 1mM EDTA, 1mM DTT, 0.01% SKL, 5% Trehalose, ProClin 300.
Expression System:
E. coli
Form:
Lyophilized powder
Sequence:
N-terminal His-Tag, confidential (NP_000292.1)
Application Notes:
Plasmin is an important enzyme present in blood that degrades many blood plasma proteins, including fibrin clots. It is released as a zymogen called plasminogen (PLG) from the liver into the systemic circulation. Plasmin is a serine protease that acts to dissolve fibrin blood clots. Apart from fibrinolysis, plasmin proteolyses proteins in various other systems: It activates collagenases, some mediators of the complement system and weakens the wall of the Graafian follicle (leading to ovulation). It cleaves fibrin, fibronectin, thrombospondin, laminin, and von Willebrand factor. Plasmin, like trypsin, belongs to the family of serine proteases. Besides, Actin Beta (ACTb) has been identified as an interactor of PLG, thus a binding ELISA assay was conducted to detect the interaction of recombinant human PLG and recombinant human ACTb. Briefly, PLG were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100 µl were then transferred to ACTb-coated microtiter wells and incubated for 2h at 37C. Wells were washed with PBST and incubated for 1h with anti-PLG pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody, wells were aspirated and washed 3 times. With the addition of substrate solution , wells were incubated 15-25 minutes at 37C. Finally, add 50 µl stop solution to the wells and read at 450nm immediately. The binding activity of PLG and ACTb was in a dose dependent manner.
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