Immunoglobulin Kappa is 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.
パッケージサイズ | 在庫状況 | 単価(税別) |
---|---|---|
10 μg | 約5 days | ¥ 27,000 |
50 μg | 約5 days | ¥ 81,500 |
500 μg | 約5 days | ¥ 461,500 |
1 mg | 約5 days | ¥ 693,000 |
説明 | Immunoglobulin Kappa is 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. |
Species | Human |
Expression Host | HEK293 Cells |
Tag | C-6xHis |
Accession Number | P01834 |
別名 | Ig κ chain C region AG, Ig κ, Ig kappa chain C region AG, Ig kappa chain C region, IGKC, Ig κ chain C region, Immunoglobulin Kappa, Ig kappa chain C region CUM, Ig κ chain C region CUM, Immunoglobulin κ |
Amino Acid | Thr2-Cys107 |
Construction | Thr2-Cys107 |
Protein Purity | Greater than 95% as determined by reducing SDS-PAGE. (QC verified) |
分子量 | 14 KDa (reducing condition) |
Endotoxin | < 0.1 ng/µg (1 EU/µg) as determined by LAL test. |
Formulation | Lyophilized from a solution filtered through a 0.22 μm filter, containing PBS, pH 7.4. |
Reconstitution | Reconstitute the lyophilized protein in distilled water. The product concentration should not be less than 100 μg/ml. Before opening, centrifuge the tube to collect powder at the bottom. After adding the reconstitution buffer, avoid vortexing or pipetting for mixing. |
Stability & Storage |
Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at-80℃. For reconstituted proteinsolutions, the solution can be stored at -20°c to -80'c for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots. |
Shipping |
In general, Lyophilized powders are shipping with blue ice. Solutions are shipping with dry ice. |
Research Background | Immunoglobulin Kappa is 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. |
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Ig kappa Protein, Human, Recombinant (His) Ig κ chain C region AG Ig κ Ig kappa chain C region AG Ig kappa chain C region Ig k chain C region IGKC Ig k chain C region AG Ig k chain C region CUM Ig κ chain C region Immunoglobulin Kappa Immunoglobulin k Ig kappa chain C region CUM Ig κ chain C region CUM Immunoglobulin κ recombinant recombinant-proteins proteins protein