| Product name: |
Recombinant Human IgG4 Fc (224AA) |
| Description: |
Recombinant Human Ig Gamma-4 Chain C Region is produced by our Mammalian expression system and the target gene encoding Pro104-Lys327(Leu325Pro) is expressed. |
| Accession: |
P01861 |
| Molecular weight: |
25.1 KDa |
| Apparent molecular weight: |
30 KDa, reducing conditions |
| Purity: |
Greater than 95% as determined by reducing SDS-PAGE. |
| Endotoxin: |
Less than 0.1 ng/μg (1 EU/μg) as determined by LAL test. |
| Redissolve: |
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.? |
| Storage: |
Lyophilized protein should be stored at < -20°C, though stable at room temperature for 3 weeks.
Reconstituted protein solution can be stored at 4-7°C for 2-7 days.
Aliquots of reconstituted samples are stable at < -20°C for 3 months. |
| Delivery condition: |
The product is shipped at ambient temperature.
Upon receipt, store it immediately at the temperature listed below. |
| 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. |
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