Seattle Genova platform is conducted to offer our customers excellent protein production services that keep the bioactivities of your proteins just as they were in nature. To achieve this, we can offer both nature protein purification services and recombinant protein production services. We have developed very specialized protocols to make sure the produced proteins will maintain their biological activities. And our well-developed bioassays can ensure comprehensive activity validations before we release the proteins.
Working with a variety of protein expression systems, we can quickly generate bespoke protein reagents to meet customer requirements. Backed by years of expertise, we have successfully produced a variety of proteins for many biological studies.
Background of IgG Fc
Immunoglobulin G (IgG) is synthesized and emitted by plasma B cells and constitutes 75% of serum immunoglobulins in humans. IgG antibodies conserve the body against pathogens by agglutination and immobilization, complement activation, and toxin neutralization, as well as antibody-dependent cell-mediated cytotoxicity (ADCC). Recombinant IgG Fc is suggested to represent a potential anti-inflammatory drug for the treatment of human autoimmune diseases.
There are five categories of immunoglobulins in humans, which are IgG, IgA, IgM, IgE and IgD. IgG can be further distributed into four subclasses, IgG1, IgG2, IgG3 and IgG4 in humans, and IgG1, IgG2a, IgG2b and IgG3 in mice. IgG is abundant in serum with the biggest half-life, which comprises 75% of immunoglobulins in circulation. IgG has a Y-shaped structure with two identical light chains and two identical heavy polypeptide chains. The fragment crystallizable region (Fc region) illustrates the stem of the Y, which includes two constant domains (CH2 and CH3) of the heavy chain. The Fc region is liable for effector processes through interactions with target molecules and receptors. Fc binding to Fc receptors on immune effector cells, such as natural killers and macrophages, elicits ADCC (antibody-dependent cell-mediated cytotoxicity), which directs to phagocytosis or lysis of the targeted cells. The Fc region can also connect to complement components to mediate CDC (complement-dependent cytotoxicity).
Successful antibody production depends upon careful planning and implementation concerning various important steps and considerations:
•Synthesize or refine the target antigen (e.g., peptide or hapten)
•Choose a reasonable immunogenic carrier protein
•Conjugate the antigen and carrier protein to build the immunogen
•Immunize animals utilizing the appropriate schedule and adjuvant formula
•Screen serum (or hybridoma) for antibody titer and isotype (also called antibody characterization; see below)
Purification techniques vary from very crude to highly specific:
•Crude—precipitation of a subset of total serum proteins that immunoglobulins
•General—affinity purification of specific antibody classes (e.g., IgG) without problem for antigen specificity
•Specific—affinity purification of only those antibodies in a sample that connects to a specific antigen molecule
Which level of purification is essential to obtain usable antibodies depends upon the intended application(s) for the antibody.
It includes three kinds of activities that are usually performed at several stages throughout a whole antibody production and purification project:
•Screening—identifying antibody samples having antigen-binding specificity
•Titering—measuring antibody concentration and functional assay titer
•Isotyping—determining a monoclonal antibody class and subclass individuality
Purified antibodies can be improved for special uses by several methods comprising fragmentation into minor antigen-binding units, conjugation with an enzyme or other detectable markers, and immobilization to solid supports. Most often antibodies are utilized in the whole-molecule form. However, the performance of some techniques and experiments can be improved by utilizing antibodies whose nonessential portions have been removed.
labelling and immobilization
Antibodies are produced and purified for aim as antigen-specific probes. However, their utility in any given technique (ELISA, western blotting, cellular imaging, immunohistochemistry) relies upon having a mechanism to secondarily detect the antibody.
Techniques that utilize antibodies for immunoprecipitation or another form of affinity purification depend upon mechanisms for connecting or immobilizing them to chromatography media (e.g., beaded agarose resin). Strategies for accomplishing this include the same considerations and chemical methods as antibody labelling.
•Guaranteed package! No success no fee for the bacterial technique.
•Risk-Free. To date, we have successfully provided 3,000+ recombinant proteins with a very high success rate.
•Various types of proteins. Enzymes, cytokines, growth components, hormones, receptors, transcription factors, antibodies, etc.
•Advance your project. From codon optimization, and sequence analysis, to expression and purification, actual stable cell line construction.
•Rich customizable selections. Four expression systems, fed-batch fermentation (1-100 L), protein-protein interaction examinat
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