Goat Polyclonal KVD16 antibody. Suitable for Ie and reacts with Human samples.
Preservative: 0.1% Sodium azide
Constituents: Tris buffered saline
| Ie | |
|---|---|
| Human | Expected |
| Species | Dilution info | Notes |
|---|---|---|
Species Human | Dilution info Use at an assay dependent concentration. | Notes - |
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V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition (PubMed:24600447). Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268).
Immunoglobulin kappa variable 1D-16, Ig kappa chain V-I region HK146, Ig kappa chain V-I region HK189, IGKV1D-16
Goat Polyclonal KVD16 antibody. Suitable for Ie and reacts with Human samples.
Preservative: 0.1% Sodium azide
Constituents: Tris buffered saline
Delipidation and ion exchange chromatography. Product is 0.2um filtered.
The kappa light chain alternatively known as Ig kappa chain is a component of immunoglobulins which are important for immune response. This protein has a molecular mass of roughly 25 kDa. It predominantly expresses in B lymphocytes where it pairs with heavy chains to form antibodies. Its expression is indicative of mature B cell functions serving as a marker for certain types of immune cells. The kappa light chain can also be detected outside of cells circulating in the blood and other bodily fluids.
Kappa light chains are integral to the structure and function of antibodies. As part of the immunoglobulin molecule these chains contribute to antigen specificity by combining with heavy chains. Together they form the antigen-binding site. The kappa light chain is not part of a multiprotein complex; rather it directly participates in the antibody response. The presence of either kappa or lambda light chains can determine the particularities of antibody characteristics.
Kappa light chains are elements of the immunological pathways notably the adaptive immune response. They interact with other proteins like immunoglobulin heavy chains to neutralize pathogens. The constant region of the kappa chain plays a role in determining the isotype of immunoglobulins which affects how antibodies mediate immune effector functions. Cross-linking of surface immunoglobulin by antigens can trigger B cell activation an essential step in the adaptive immune system.
Kappa light chains associate closely with multiple myeloma and certain types of lymphomas. Overproduction of kappa light chains in these diseases results in high levels detectable in the serum or urine which can be used diagnostically as markers. Also dysregulation of kappa chains correlates with autoimmune disorders whereby the immune system incorrectly targets its tissues. In disorders like these the interplay between kappa and lambda chains often arises showing imbalance between the two as a sign of abnormal B cell activity.
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