About Ig Lambda Light Chain
Immunoglobulins recognize foreign antigens and initiate immune responses such as phagocytosis and the complement system. Each immunoglobulin molecule consists of two identical heavy chains and two identical light chains. There are two classes of light chains, kappa and lambda. This region represents the germline organization of the lambda light chain locus. The locus includes V (variable), J (joining), and C (constant) segments. During B cell development, a recombination event at the DNA level joins a single V segment with a J segment; the C segment is later joined by splicing at the RNA level. Recombination of many different V segments with several J segments provides a wide range of antigen recognition. Additional diversity is attained by junctional diversity, resulting from the random additional of nucleotides by terminal deoxynucleotidyltransferase, and by somatic hypermutation, which occurs during B cell maturation in the spleen and lymph nodes. Several V segments and three C segments are known to be incapable of encoding a protein and are considered pseudogenes. The locus also includes several non-immunoglobulin genes, many of which are pseudogenes or are predicted by automated computational analysis or homology to other species. [provided by RefSeq, Jul 2008]

About PE-Cy7
PE-Cyanine®7 (PE-Cy7, RPE-Cy7) is a far red-emitting tandem fluorophore that combines phycoerythrin (PE) and Cy7. The donor molecule, PE can be excited by the 488-nm blue, 532-nm green, or 561-nm yellow-green laser and and transfers energy to the acceptor molecule, Cy7, which emitts light that can be captured with a 780/60 nm bandpass filter. PE-CY7 has an excitation peak at 565 nm and an emission peak at 778 nm, and is a suitable alternative to PE-Vio®770 and PE-Fire™ 780.