IGKV1-5 antibody

V segment of the variable domain of immunoglobulins light chain that participates to the antigen recognition. 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:20176268, PubMed:17576170).

Immunoglobulin kappa variable 1-5|Ig kappa chain V-I region CAR|Ig kappa chain V-I region EU|Ig kappa chain V-I region HK102|Ig kappa chain V-I region Kue|IGKV1-5

P01602

Rabbit

Human, Mouse

immunoglobulin kappa variable 1-5

IGKV1-5

Polyclonal

IgG

ELISA, WB

Immunology

Immunogen affinity purified

WB: 1:500-1:2000

≥95% as determined by SDS-PAGE

Liquid

PBS with 0.02% sodium azide and 50% glycerol pH 7.3, -20°C for 12 months(Avoid repeated freeze / thaw cycles.)

Primary Antibodies

https://www.fn-test.com/product/FNab04188/

human plasma tissue were subjected to SDS PAGE followed by western blot with FNab04188 (IGKV1-5 antibody) at dilution of 1:1000