Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation
Lyophilized from a 0.2μm filtered concentrated solution in 20mM Tris-HCl, pH 8.0, 150mM NaCl, with 0.02% Tween-20.
Endotoxin
Less than 0.1EU/μg of rHuVaspin as determined by LAL method.
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0mg/ml. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.
Category
Enzymes
Background
The human serpin superfamily consists of at least 35 members that target not only serine proteases, but also selected cysteine proteases and non-protease proteins. Serpins bind the protease active site resulting in a major conformational rearrangement that traps the enzyme in a covalent acyl-enzyme intermediate. As protease inhibitors, serpins have an array of functions including regulating blood clotting, the complement pathway, extracellular matrix remodeling, and cell motility. They are also involved in activities that extend beyond their ability to inhibit proteases. For instance, they may also regulate blood pressure, angiogenesis, or act as storage/transport proteins.