Synonyms for scfvs or Related words with scfvs

vhhs              fabs              dabs              nanobodies              vhh              scfv              sdabs              muteins              iggs              tcrs              chimeras              mabs              nanobody              tetramers              sdab              heterodimers              phages              monospecific              diabody              sctcr              chimera              multimers              monoclonals              hybridomas              meganucleases              vnar              transfectants              clones              recombinants              minibody              monobodies              chimaeric              heterodimeric              sfv              abps              subclones              bispecific              homodimers              cdnas              antisera              ectodomains              epitopes              fusions              heterodimer              fab              gpvi              aptamers              surrobodies              adnectins              vlps             

Examples of "scfvs"
"Divalent" (or "bivalent") single-chain variable fragments (di-scFvs, bi-scFvs) can be engineered by linking two scFvs. This can be done by producing a single peptide chain with two V and two V regions, yielding "tandem scFvs". Another possibility is the creation of scFvs with linker peptides that are too short for the two variable regions to fold together (about five amino acids), forcing scFvs to dimerize. This type is known as "diabodies". Diabodies have been shown to have dissociation constants up to 40-fold lower than corresponding scFvs, meaning that they have a much higher affinity to their target. Consequently, diabody drugs could be dosed much lower than other therapeutic antibodies and are capable of highly specific targeting of tumors in vivo. Still shorter linkers (one or two amino acids) lead to the formation of trimers, so-called "triabodies" or "tribodies". "Tetrabodies" have also been produced. They exhibit an even higher affinity to their targets than diabodies.
BiTEs are fusion proteins consisting of two single-chain variable fragments (scFvs) of different antibodies, or amino acid sequences from four different genes, on a single peptide chain of about 55 kilodaltons. One of the scFvs binds to T cells via the CD3 receptor, and the other to a tumor cell via a tumor specific molecule.
Unlike monoclonal antibodies, which are often produced in mammalian cell cultures, scFvs are more often produced in bacteria cell cultures such as "E. coli".
Solitomab (INN) (MT110) is an artificial bispecific monoclonal antibody that is being investigated as an anti-cancer drug. It is a fusion protein consisting of two single-chain variable fragments (scFvs) of different antibodies on a single peptide chain of about 55 kilodaltons. One of the scFvs binds to T cells via the CD3 receptor, and the other to EpCAM as a tumor antigen against gastrointestinal, lung, and other cancers.
Initially the insolubility of anti-herbicide antibody fragments when expressed in E. coli had restricted this work, however work later carried out showed that disulfide linked scFvs, termed SCABS, had improved stability in a range of environments.
These molecules were created to facilitate phage display, where it is highly convenient to express the antigen-binding domain as a single peptide. As an alternative, scFv can be created directly from subcloned heavy and light chains derived from a hybridoma. ScFvs have many uses, e.g., flow cytometry, immunohistochemistry, and as antigen-binding domains of artificial T cell receptors.
There are other bsMabs that lack an Fc region entirely. These include chemically linked Fabs, consisting of only the Fab regions, and various types of bivalent and trivalent single-chain variable fragments (scFvs). There are also fusion proteins mimicking the variable domains of two antibodies. The furthest developed of these newer formats are the bi-specific T-cell engagers (BiTEs).
All of these formats can be composed from variable fragments with specificity for two different antigens, in which case they are types of bispecific antibodies. The furthest developed of these are bispecific tandem di-scFvs, known as bi-specific T-cell engagers (BiTE antibody constructs).
Because antibodies ordinarily are designed to be secreted from the cell, intrabodies require special alterations, including the use of single-chain antibodies (scFvs), modification of immunoglobulin VL domains for hyperstability, selection of antibodies resistant to the more reducing intracellular environment, or expression as a fusion protein with maltose binding protein or other stable intracellular proteins. Such optimizations have improved the stability and structure of intrabodies, allowing the publication of a variety of promising applications against hepatitis B, avian influenza, prion diseases, inflammation, Parkinson's disease, and Huntington's disease.
Janda has also worked creating peptide and antibody molecules for the treatment of cancer. By employing a novel approach, he was able to access and screen a wide range of proteins using both sequence space and conformational space. By panning this library against a B lymphoctye cell line, a unique cell-binding and internalizing peptide was discovered. Further mechanistic studies of this peptide uncovered a dimerization "switch" that modulates the cell-penetrating activity. In addition to these studies, Janda has also examined the development of effective immunotherapies for the treatment of cancer. His group has demonstrated that a synthetically prepared cell-surface glycosphingolipid can be utilized as a panning reagent to identify fully human single chain antibodies (scFvs) that are selective for melanoma and breast tumor cells. The Janda laboratory has also identified a scFv specific for the integrin αβ that is internalized by human pancreatic cancer cells; subsequent studies have employed this antibody conjugated with the potent cytotoxic compound duocarmycin SA for the selective delivery of chemotherapeutic agents.