Description
Recombinant Human IgG2-Fc Protein (aa 99-326, Val161Met) | PKSH033652 | Gentaur US, UK & Europe Disrtribition
Synonyms: Ig gamma-2 chain C region, IgG2 Fc
Active Protein: N/A
Activity: Recombinant Human IgG2-Fc is produced by our Mammalian expression system and the target gene encoding Glu99-Lys326(Val161Met) is expressed.
Protein Construction: Recombinant Human IgG2-Fc is produced by our Mammalian expression system and the target gene encoding Glu99-Lys326(Val161Met) is expressed.
Fusion Tag: N/A
Species: Human
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: 25.7 kDa
Formulation: Lyophilized from a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, 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; 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. Protein G or Protein A on the surface of certain Staphylococcal and Streptococcal strains specifically binds with the Fc region of IgGs; and has numerous applications in biotechnology as a reagent for affinity purification. Recombinant IgG Fc Region is suggested to represent a potential anti-inflammatory drug for treatment of human autoimmune diseases.
Research Area: immunology
