Company Filing History:
Years Active: 1989-1999
Title: The Innovative Contributions of Lars Bjorck
Introduction
Lars Bjorck is a notable inventor based in Sodra Sandby, Sweden. He has made significant contributions to the field of immunology through his innovative inventions. With a total of 6 patents, Bjorck has focused on developing proteins that enhance our understanding of immunoglobulin interactions.
Latest Patents
One of Bjorck's latest patents is titled "Protein L and hybrid proteins thereof." This invention relates to sequences of protein L that bind to light chains of immunoglobulins. It also includes hybrid proteins capable of binding to both light and heavy chains of immunoglobulin G, particularly protein LG. Additionally, the patent covers DNA sequences coding for these proteins, vectors containing such DNA sequences, and host cells transformed with these vectors. The invention further encompasses methods for producing the proteins, reagent appliances for the separation and identification of immunoglobulins, and pharmaceutical compositions containing these proteins. Another significant patent is for a gene encoding a novel protein H capable of binding to IgG. This gene was isolated from Streptococcus sp. AP1 and expressed in E. coli to produce Protein H, which binds specifically to human IgG of all subclasses.
Career Highlights
Throughout his career, Lars Bjorck has worked with several prominent companies, including Hightech Receptor Ab and Pharmacia Ab. His work has significantly advanced the field of immunology and has implications for therapeutic applications.
Collaborations
Bjorck has collaborated with notable individuals in his field, including Goran Kronvall and Hideyuki Gomi. These collaborations have contributed to the development of his innovative patents and research.
Conclusion
Lars Bjorck's contributions to immunology through his patents and collaborations highlight his role as a significant inventor in the field. His work continues to influence the understanding and application of immunoglobulin interactions.