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From Wikipedia, the free
encyclopedia Antibodies (also
known as immunoglobulins[1], abbreviated Ig) are gamma globulin proteins
that are found in blood or other bodily fluids of vertebrates, and are used
by the immune system to identify and neutralize foreign objects, such as
bacteria and viruses. They are typically made of basic structural units—each
with two large heavy chains and two small light chains—to form, for example,
monomers with one unit, dimers with two units or pentamers with five units.
Antibodies are produced by a kind of white blood cell called a plasma cell.
There are several different types of antibody heavy chains, and several
different kinds of antibodies, which are grouped into different isotypes
based on which heavy chain they possess. Five different antibody isotypes
are known in mammals, which perform different roles, and help direct the
appropriate immune response for each different type of foreign object they
encounter.[2]
Though the general structure of all antibodies is very similar, a small
region at the tip of the protein is extremely variable, allowing millions of
antibodies with slightly different tip structures, or antigen binding sites,
to exist. This region is known as the hypervariable region. Each of these
variants can bind to a different target, known as an antigen.[3] This huge
diversity of antibodies allows the immune system to recognize an equally
wide diversity of antigens. The unique part of the antigen recognized by an
antibody is called an epitope. These epitopes bind with their antibody in a
highly specific interaction, called induced fit, that allows antibodies to
identify and bind only their unique antigen in the midst of the millions of
different molecules that make up an organism. Recognition of an antigen by
an antibody tags it for attack by other parts of the immune system.
Antibodies can also neutralize targets directly by, for example, binding to
a part of a pathogen that it needs to cause an infection.[4]
The large and diverse population of antibodies is generated by random
combinations of a set of gene segments that encode different antigen binding
sites (or paratopes), followed by random mutations in this area of the
antibody gene, which create further diversity.[2][5] Antibody genes also
re-organize in a process called class switching that changes the base of the
heavy chain to another, creating a different isotype of the antibody that
retains the antigen specific variable region. This allows a single antibody
to be used by several different parts of the immune system. Production of
antibodies is the main function of the humoral immune system.[6] |
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Antibody
Engineering - December 6-10, 2009 - Sheraton San Diego Hotel and Marina
... Celebrating the 20th Annual
Antibody
Engineering Conference: ...
www.ibclifesciences.com/antibodyeng/overview.xml
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Straightforward procedures for conjugation
of proteins (mainly
antibodies) to fluorescent dyes.
www.drmr.com/abcon/
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Read about antinuclear
antibodies (ANAs),
unusual antibodies
that can bind to certain structures within the nucleus of the cells, are
found in patients ...
www.medicinenet.com ›
... ›
antinuclear antibody index
Search
Antibodies |
monoclonal, polyclonal, primary, secondary and therapeutic |
Antibodies for
research | Find and compare
antibodies,
...
www.antibodydirectory.com/
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Signalway
Antibody(SAB)
develops rabbit polyclonal phospho-specific
antibodies,rabbit
monoclonal,mouse monoclonal for studying protein phosphorylation in
...
www.signalwayantibody.com/
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Here are some online educational resources
about antibodies.
This page is divided into sections for those interested in research
(with an emphasis on ...
www.antibodyresource.com/educational.html
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