Recombinant Human Lambda Light chain protein
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Recombinant Human Lambda Light chain protein is a Human Full Length protein, in the 1 to 232 aa range, expressed in Wheat germ, suitable for ELISA, WB.
View Alternative Names
Immunoglobulin lambda variable 1-51, Ig lambda chain V-I region BL2, Ig lambda chain V-I region EPS, Ig lambda chain V-I region NEW, Ig lambda chain V-I region NIG-64, IGLV1-51
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human Lambda Light chain protein (AB158750)
ab158750 on a 12.5% SDS-PAGE stained with Coomassie Blue.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Lambda Light Chain participates in immunological functions by contributing to the antigen-binding site of antibodies. It exists as a part of the immunoglobulin complex. The lambda chain alongside heavy chains forms the variable part of antibodies allowing specificity in antigen recognition. Its variation leads to a diverse antibody repertoire which is important for recognizing a wide range of pathogens.
Pathways
Lambda Light Chain fits into pathways involving adaptive immune responses. It is important in antigen processing and presentation pathways. In this context it interacts with the heavy chains which together drive the specificity and efficiency of immune response pathways. It also associates with proteins like the major histocompatibility complex (MHC) which facilitates antigen presentation to T cells.
Specifications
Form
Liquid
General info
Function
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).
Target data
Additional targets
Product promise
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