||Recombinant Human IGHG1 (Glu 99-Lys 330) was expressed in Human cells.
||As a monomeric immunoglobulin that is predominately involved in the secondary antibody response and the only isotype that can pass through the human placenta, Immunoglobulin G (IgG) is synthesized and secreted by plasma B cells, and constitutes 75% of serum immunoglobulins in humans. IgG antibodies protect the body against the pathogens by agglutination and immobilization, complement activation, toxin neutralization, as well as the antibody-dependent cell-mediated cytotoxicity (ADCC). IgG tetramer contains two heavy chains (50 kDa ) and two light chains (25 kDa) linked by disulfide bonds, that is the two identical halves form the Y-like shape. IgG is digested by pepsin proteolysis into Fab fragment (antigen-binding fragment) and Fc fragment ("crystallizable" fragment). IgG1 is most abundant in serum among the four IgG subclasses (IgG1, 2, 3 and 4) and binds to Fc receptors (FcγR ) on phagocytic cells with high affinity. Fc fragment is demonstrated to mediate phagocytosis, trigger inflammation, and target Ig to particular tissues.
||> 95 % as determined by SDS-PAGE.
||< 1.0 EU per 1μg of the protein as determined by the LAL method.
||Samples are stable for up to twelve months from date of receipt at -70°C
|Predicted N terminal :
|Molecular Mass :
||The recombinant human IgG1 Fc consists of 232 amino acids and has a predicted molecular mass of 26 kDa. As a result of glycosylation, the apparent molecular mass of rhFc is approximately 32 kDa in SDS-PAGE under reducing conditions.
||Lyophilized from sterile PBS, pH 7.4. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA
||Store it under sterile conditions at -70°C. It is recommended that the protein be aliquoted for optimal storage and usage. Avoid repeated freeze-thaw cycles.