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This protein is found as a pentamer and is a major substrate for the cAMP-dependent protein kinase in cardiac muscle.In the unphosphorylated state, phospholamban is an inhibitor of cardiac muscle sarcoplasmic reticulum Ca 2+-ATPase [7] which transports calcium from cytosol into the sarcoplasmic reticulum.
Five sub-units come together to form a channel. Each channel consist of two alpha chain, one beta, one gamma and one delta chain.These five chains assemble together (along with certain receptors like protons or acetylcholine) forming the structure of the channel. [1]
Immunoglobulin M (IgM) is the largest of several isotypes of antibodies (also known as immunoglobulin) that are produced by vertebrates.IgM is the first antibody to appear in the response to initial exposure to an antigen; [1] [2] causing it to also be called an acute phase antibody.
A pentamer is an entity composed of five subunits. In chemistry, it applies to molecules made of five monomers . In biochemistry, it applies to macromolecules, particularly pentameric proteins , made of five protein sub-units.
The J chain regulates the multimerization of IgM and IgA in mammals. When expressed in cells, it favors the formation of a pentameric IgM and an IgA dimer. IgM pentamers are most commonly found with a single J chain, but some studies have seen as many as 4 J chains associated to a single IgM pentamer.
sdAb: single-domain antibody; BsAb: bispecific monoclonal antibody: 3funct: trifunctional antibody; BiTE: bi-specific T-cell engager; This list of over 500 monoclonal antibodies includes approved and investigational drugs as well as drugs that have been withdrawn from market; consequently, the column Use does not necessarily indicate clinical ...
Polyclonal antibodies (pAbs) are antibodies that are secreted by different B cell lineages within the body (whereas monoclonal antibodies come from a single cell lineage). ). They are a collection of immunoglobulin molecules that react against a specific antigen, each identifying a different ep
mAbs is a peer-reviewed multi-disciplinary scientific journal established in 2009, published by Taylor & Francis and dedicated to the art and science of antibody research and development. Its editor-in-chief is Janice M. Reichert [1] and it is affiliated with The Antibody Society.