V region of the variable domain of immunoglobulin light chains that participates in 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 . 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 . .

Immunoglobulin lambda variable 3-21 (Ig lambda chain V-III region LOI) (Ig lambda chain V-V region DEL) (Ig lambda chain V-VII region MOT),IGLV3-21

P80748

Human,Rat,Mouse

WB

WB 1:500-2000

This antibody detects endogenous levels of human LV302

12kDa

Rabbit

Synthesized peptide derived from human LV302.

Polyclonal

Rabbit,IgG

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.

Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% New type preservative N.

1 mg/ml

Store at -20℃. Stable for 12 months from date of receipt.