IgG2 Fc Protein, Human (228a.a, V161M, S257A, HEK293)

The IgG2 Fc protein is the constant region of the immunoglobulin heavy chain and acts as an antigen receptor, triggering the expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. IgG2 Fc Protein, Human (228a.a, V161M, S257A, HEK293) is the recombinant human-derived IgG2 Fc protein, expressed by HEK293 , with tag free. The total length of IgG2 Fc Protein, Human (228a.a, V161M, S257A, HEK293) is 228 a.a., with molecular weight of ~32 kDa.

The constant region of immunoglobulin heavy chains, referred to as antibodies, comprises membrane-bound or secreted glycoproteins synthesized by B lymphocytes. In the recognition phase of humoral immunity, these membrane-bound immunoglobulins act as receptors, triggering clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells upon binding specific antigens. The effector phase, mediated by secreted immunoglobulins, leads to the elimination of bound antigens. The antigen binding site is shaped by the variable domain of one heavy chain, along with that of its associated light chain, resulting in each immunoglobulin possessing two antigen binding sites with remarkable affinity for a particular antigen. Variable domains undergo V-(D)-J rearrangement and subsequent somatic hypermutations, facilitating affinity maturation for a specific antigen following exposure and selection. Immunoglobulins consist of two identical heavy chains and two identical light chains, interconnected by disulfide linkages.

Human

HEK293

Tag Free

P01859 (E99-K326, V161M, S257A)

3501  [NCBI]

ERKCCVECPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVQFNWYVDGMEVHNAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKEYKCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPMLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK

Approximately 32 kDa

Greater than 95% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.