Search results
Results from the WOW.Com Content Network
18821 Ensembl ENSG00000198523 ENSMUSG00000038583 UniProt P26678 P61014 RefSeq (mRNA) NM_002667 NM_001141927 NM_023129 RefSeq (protein) NP_002658 NP_001135399 NP_075618 Location (UCSC) Chr 6: 118.55 – 118.56 Mb Chr 10: 53.21 – 53.22 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Phospholamban, also known as PLN or PLB, is a micropeptide protein that in humans is encoded by the ...
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.
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.
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.
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This list of over 500 monoclonal antibodies includes approved and investigational drugs as well as drugs that have been withdrawn from market; consequently, the column Use does not necessarily indicate clinical ...
Complement-dependent cytotoxicity (CDC) is an effector function of IgG and IgM antibodies.When they are bound to surface antigen on target cell (e.g. bacterial or viral infected cell), the classical complement pathway is triggered by bonding protein C1q to these antibodies, resulting in formation of a membrane attack complex (MAC) and target cell lysis.
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.