Anti-Human Iambda light chain antibody [36-59]
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概述
- 产品描述Constant region of immunoglobulin light chains. 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.
- 产品名称Anti-Human Iambda light chain antibody [36-59]
- 分子量25 kDa
- 种属反应性Human
- 验证应用WB, ELISA
- 抗体类型小鼠单抗
- 免疫原Native protein.
- 偶联Non-conjugated
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性能
- 形态Liquid
- 浓度2 mg/mL.
- 存放说明Store at +4℃ after thawing. Aliquot store at -20℃. Avoid repeated freeze / thaw cycles.
- 存储缓冲液1*TBS (pH7.4), 0.2% BSA, 50% Glycerol. Preservative: 0.05% Sodium Azide.
- 亚型IgG2a
- 纯化方式Protein A purified.
- 亚细胞定位Cell membrane, Immunoglobulin, Membrane, Secreted
- 其它名称
- Bence Jones protein antibody
- BJP antibody
- Constant region of lambda light chains antibody
more
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应用
WB: 1:1000
ELISA: Use at an assay dependent concentration.
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Fig1: Western blot analysis of Human Iambda light chain on human IgG protein lysate. Proteins were transferred to a PVDF membrane and blocked with 5% BSA in PBS for 1 hour at room temperature. The primary antibody was used in 5% BSA at room temperature for 2 hours. Goat Anti-Mouse IgG - HRP Secondary Antibody (HA1006) at 1:5,000 dilution was used for 1 hour at room temperature.
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