Recombinant Human Ig kappa (C-6His)

Recombinant Human Ig kappa (C-6His)

Size1:10μg price1:$136
Size2:50μg price2:$378
Size3:500μg price3:$1890
SKU: PHH2354 Category: Target Proteins Tags: ,

Datasheet

Name

Recombinant Human Ig kappa (C-6His)

Purity

Greater than 95% as determined by reducing SDS-PAGE

Endotoxin level

<1 EU/µg as determined by LAL test.

Construction

Recombinant Human Immunoglobulin Kappa Constant is produced by our Mammalian expression system and the target gene encoding Thr2-Cys107 is expressed with a 6His tag at the C-terminus.

Accession #

P01834

Host

Human Cells

Species

Human

Predicted Molecular Mass

12.4 KDa

Buffer

Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.

Form

Lyophilized

Shipping

The product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.

Stability&Storage

Store at ≤-70°C, stable for 6 months after receipt.Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.

Reconstitution

Always centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.

 

 

 

Alternative Names

Ig kappa chain C region; Ig kappa chain C region AG; Ig kappa chain C region CUM; IGKC; Immunoglobulin Kappa

 

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.

 

Note

For Research Use Only , Not for Diagnostic Use.