Antibody producing cells of the immune system require multiple rearrangements of immunoglobulin (antibody, Ig) genes. Immunoglobulins are four-chain, Y-shaped, monomeric structures of two identical heavy chains and two identical light chains held together through interchain disulfide bonds. Immunoglobulins in vertebrates help to remove non-self molecules or cells (antigens) by recognizing and binding to the antigen and carrying out effector functions that activate the immune system. Variable genetic combinations of the five heavy chain classes (M, D, G, E and A) and the two light chain isotypes, ˚ and ¬, confer the role of an antibody. The variable region genes encoding immunoglobulin ˚ and ¬ chains are assembled from three DNA segments, the V, C and J genes. Human ˚ light chain genes map to chromosome 2 and the human ¬ light chain genes map to chromosome 22. ˚ gene recombination can precede ¬ gene recombination during B cell ontogeny and only a single light chain type is expressed in individual B cells. Antibodies in camels and sharks can lack light chain, suggesting that light chain may not be essential for antigen binding in some vertebrates.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of Ig &lambda Chain of mouse and rat origin by WB, IP, IF and ELISA
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 1-110 representing full length Ig &lambda chain of mouse origin
Tissue Specificity
epitope corresponding to amino acids 1-110 representing full length Ig λ chain of mouse origin