1-832-868-1888
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Catalog Number: |
78185 |
other_names: | AGM1, MU, VH |
Amount: |
100μg |
calculated_mw: | 75kDa |
host_species: | Rabbit |
Price: |
$318 |
Swiss-Prot No: |
P01871 |
Form of Antibody: |
|
Storage/Stability: |
|
Immunogen: |
A synthesized peptide derived from human Human IgM |
Purification: |
Affinity purification |
Specificity/Sensitivity: |
|
Applications: |
WB,IHC |
Background: |
Immunoglobulins (Ig) are the antigen recognition molecules of B cells. An Ig molecule is made up of 2 identical heavy chains and 2 identical light chains joined by disulfide bonds so that each heavy chain is linked to a light chain and the 2 heavy chains are linked together. Each Ig heavy chain has an N-terminal variable (V) region containing the antigen-binding site and a C-terminal constant (C) region, encoded by an individual C region gene, that determines the isotype of the antibody and provides effector or signaling functions. The heavy chain V region is encoded by 1 each of 3 types of genes: V genes, joining (J) genes, and diversity (D) genes. The C region genes are clustered downstream of the V region genes within the heavy chain locus on chromosome 14. The IGHM gene encodes the C region of the mu heavy chain, which defines the IgM isotype. Naive B cells express the transmembrane forms of IgM and IgD on their surface. During an antibody response, activated B cells can switch to the expression of individual downstream heavy chain C region genes by a process of somatic recombination known as isotype switching. In addition, secreted Ig forms that act as antibodies can be produced by alternative RNA processing of the heavy chain C region sequences. Although the membrane forms of all Ig isotypes are monomeric, secreted IgM forms pentamers, and occasionally hexamers, in plasma. |
References: |
|
appl_detail: |
WB 1:500 - 1:2000 |
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