Description
Recombinant Mouse IgG1 Fc/IGHG1 Protein | PKSM041044 | Gentaur US, UK & Europe Disrtribition
Synonyms: g gamma-1 chain C region;IGHG1
Active Protein: N/A
Activity: Recombinant Mouse Immunoglobulin G1 Fc is produced by our Mammalian expression system and the target gene encoding Pro99-Lys324 is expressed.
Protein Construction: Recombinant Mouse Immunoglobulin G1 Fc is produced by our Mammalian expression system and the target gene encoding Pro99-Lys324 is expressed.
Fusion Tag: N/A
Species: Mouse
Expressed Host: Human Cells
Shipping: This product is provided as lyophilized powder which is shipped with ice packs.
Purity: > 95 % as determined by reducing SDS-PAGE.
Endotoxin: < 1.0 EU per μg as determined by the LAL method.
Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.
Molecular Mass: 41.5 kDa
Formulation: Lyophilized from a 0.2 μm filtered solution of PBS, pH7.4.
Reconstitution: Please refer to the printed manual for detailed information.
Background: 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. 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.
Research Area: N/A