Antibodies Ideal for Targeting
1. What are antibodies and why are antibodies ideal for targeting?
An antibody, also known as an immunoglobulin, is a large Y-shaped protein used by the immune system to identify and neutralize foreign objects such as bacteria and viruses. The antibody recognizes a unique part of the foreign target, termed an antigen.[1][2] Each tip of the "Y" of an antibody contains a paratope (a structure analogous to a lock) that is specific for one particular epitope (similarly analogous to a key) on an antigen, allowing these two structures to bind together with precision. Using this binding mechanism, an antibody can tag a microbe or an infected cell for attack by other parts of the immune system, or can neutralize its target directly (for example, by blocking a part of a microbe that is essential for its invasion and survival). The production of antibodies is the main function of the humoral immune system.[3]
Antibodies are produced by a type of white blood cell called a plasma cell.
Antibodies are typically made of basic structural units—each with two large heavy chains and two small light chains. There are several different types
The specificity of an antibody is its ability to discriminate between two different epitopes.
The specificity of antibodies can be so precise that they are able to discriminate between enantiomers of the same molecule
http://users.rcn.com/jkimball.ma.ultranet/BiologyPages/A/Affinity.html#Antibody_Specificity
http://www-users.med.cornell.edu/~jawagne/Antibody_Approaches.html#Uses%20of%20antibodies
2. What are bispecific antibodies, bispecific complexes? Why are these complexes superior to conventional antibody for diagnosis and therapy?
Bispecific antibodies recognize two distinct targets at the same time. These antibodies might bridge two targets together and present a high-value opportunity for therapeutic gains (such as bringing cancer cells within striking distance of cytotoxic T lymphocytes).
An antibody, also known as an immunoglobulin, is a large Y-shaped protein used by the immune system to identify and neutralize foreign objects such as bacteria and viruses. The antibody recognizes a unique part of the foreign target, termed an antigen.[1][2] Each tip of the "Y" of an antibody contains a paratope (a structure analogous to a lock) that is specific for one particular epitope (similarly analogous to a key) on an antigen, allowing these two structures to bind together with precision. Using this binding mechanism, an antibody can tag a microbe or an infected cell for attack by other parts of the immune system, or can neutralize its target directly (for example, by blocking a part of a microbe that is essential for its invasion and survival). The production of antibodies is the main function of the humoral immune system.[3]
Antibodies are produced by a type of white blood cell called a plasma cell.
Antibodies are typically made of basic structural units—each with two large heavy chains and two small light chains. There are several different types
The specificity of an antibody is its ability to discriminate between two different epitopes.
The specificity of antibodies can be so precise that they are able to discriminate between enantiomers of the same molecule
http://users.rcn.com/jkimball.ma.ultranet/BiologyPages/A/Affinity.html#Antibody_Specificity
http://www-users.med.cornell.edu/~jawagne/Antibody_Approaches.html#Uses%20of%20antibodies
2. What are bispecific antibodies, bispecific complexes? Why are these complexes superior to conventional antibody for diagnosis and therapy?
Bispecific antibodies recognize two distinct targets at the same time. These antibodies might bridge two targets together and present a high-value opportunity for therapeutic gains (such as bringing cancer cells within striking distance of cytotoxic T lymphocytes).