Ig Lambda Light Chain Secondary Antibody / APC /
Product Details
| Description | Human immunoglobulins are glycoproteins composed of two disulfide-bonded heavy (H) chain subunits, each of which is linked by interchain disulfide bonds to a light (L) chain forming a tetramolecular complex. There are five classes of immunoglobulins, designated IgG, IgA, IgM, IgD and IgE, which are defined by differences in the constant region of H chains. L chains are divided into kappa or lambda classifications based on structural antigenic differences. All classes of immunoglobulins have been found on the cell surface of B lymphocytes where they function as antigen receptors to elicit antigen-dependent proliferation and secretion of antigen specific soluble circulating antibodies. | |
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| Conjugate | APC | |
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| Target Species | Human | |
| Applications | FC | |
| Supplier | Abbexa | |
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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]
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 APC
Allophycocyanin (APC) is a fluorescent protein derived from cyanobacteria and red algae and a potent donor fluorophore to create tandem dyes that can be excited off the 633-640 nm laser. APC has an excitation peak at 650 nm and a emission peak at 660 nm.
Allophycocyanin (APC) is a fluorescent protein derived from cyanobacteria and red algae and a potent donor fluorophore to create tandem dyes that can be excited off the 633-640 nm laser. APC has an excitation peak at 650 nm and a emission peak at 660 nm.
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444 Ig Lambda Light Chain antibodies from over 21 suppliers available with over 61 conjugates.
