| Patent Number |
Title Of Patent |
Date Issued |
| 5648254 |
Co-expression in eukaryotic cells |
July 15, 1997 |
| A method of producing proteins of interest is disclosed. The method includes the introduction of a first DNA sequence encoding the protein of interest and at least one additional DNA sequence encoding a protein which processes or stabilizes the protein of interest into a eukaryotic host |
| 5486471 |
Tissue plasminogen activator analogs having modified growth factor domains |
January 23, 1996 |
| Tissue plasminogen activator analogs containing the growth factor domain of native t-PA, the domain having at least one cysteine residue replaced with another amino acid. The t-PA analogs may further contain a variety of substitutions and/or modifications. Pharmaceutical compositions con |
| 5403734 |
t-PA with growth factor domain substitutions |
April 4, 1995 |
| A plasminogen activator comprising a growth factor domain, a kringle domain and a serine protease domain is disclosed. The growth factor domain contains a plurality of substitutions of substantially consecutive amino acids as compared to the growth factor domain of native t-PA, the s |
| 5385831 |
Method for producing a mammalian G protein coupled glutamate receptor |
January 31, 1995 |
| Mammalian G protein coupled glutamate receptors are identified, isolated and purified. The receptors have been cloned, sequenced and expressed by recombinant means. The receptors and antibodies thereby may be used to identify agonists and antagonists of G protein coupled glutamate recept |
| 5200340 |
Thrombin-activated tissue plasminogen activators |
April 6, 1993 |
| Zymogens of proteins having fibrinolytic activity are disclosed. The proteins are cleavable by thrombin, the cleavage resulting in the stimulation of fibrinolytic activity. Suitable proteins which may be modified in accordance with the present invention include tissue plasminogen act |
| 5149533 |
Modified t-PA with kringle-/replaced by another kringle |
September 22, 1992 |
| Tissue plasminogen activator analogs exhibiting greater specificity for fibrin than native t-PA are disclosed. The analogs include the K1 domain of native t-PA replaced with another kringle domain mediating the binding of the analog to fibrin. The kringle contains six cysteine residues. |
