Recombinant Proteins
Product List
IgG Mouse
Immunoglobulin Heavy Chain Constant Region Gamma 2a Mouse Recombinant
IgG is purified by proprietary chromatographic techniques.
IgG Mouse, His
Immunoglobulin Heavy Chain Constant Region Gamma 2a Mouse Recombinant, His Tag
IgG is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
IgG1 Fc Human
Immunoglobulin Heavy Constant Gamma 1 Human Recombinant
IgG1 Fc Human Recombinant produced in HEK is a single polypeptide chain containing 231 amino acids (100-330) and having a molecular mass of 25.9kDa. IgG1 Fc is purified by proprietary chromatographic techniques.
IGJ Human
Immunoglobulin J Human Recombinant
IGLL1 Human
Immunoglobulin Lambda-Like Polypeptide 1 Human Recombinant
IgM Human
Immunoglobulin-M Human
Human Immunoglobulin-M produced in human plasma having a molecular mass of 950kDa.
IGSF8 Human
Immunoglobulin Superfamily Member 8 Human Recombinant
IGSF8 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 561 amino acids (28-579a.a.) and having a molecular mass of 59.6kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). IGSF8 is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Sf9, Baculovirus cells.
LILRB1 Human
Leukocyte Immunoglobulin Like Receptor B1 Human Recombinant
LILRB1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 446 amino acids (24-461 a.a) and having a molecular mass of 48.5kDa.
LILRB1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Sf9, Baculovirus cells.
LILRB2 Human
Leukocyte Immunoglobulin Like Receptor B2 Human Recombinant
LILRB2 Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 444 amino acids (24-461 a.a) and having a molecular mass of 48.3kDa.
LILRB2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Introduction
The Immunoglobulin (Ig) Heavy Chain Constant Region is a part of the antibody molecule that remains constant across different antibodies of the same class. Antibodies, also known as immunoglobulins, are glycoprotein molecules produced by plasma cells. They are composed of two identical heavy chains and two identical light chains. The heavy chains determine the class or isotype of the antibody, which includes IgG, IgA, IgM, IgD, and IgE . Each class has a distinct heavy chain: γ (gamma) for IgG, α (alpha) for IgA, μ (mu) for IgM, δ (delta) for IgD, and ε (epsilon) for IgE .
The constant region of the heavy chain is crucial for the antibody’s effector functions. It is composed of multiple immunoglobulin domains, typically three or four, depending on the class . The expression patterns and tissue distribution of these regions vary. For instance, IgG is the most abundant in serum and extracellular fluid, while IgA is primarily found in mucosal areas such as the gut, respiratory tract, and urogenital tract . IgM is usually the first antibody produced in response to an infection and is found in the blood and lymphatic fluid .
The primary biological functions of the Ig Heavy Chain Constant Region include mediating effector functions such as complement activation, binding to Fc receptors on immune cells, and facilitating phagocytosis . These functions are essential for the immune response, including pathogen recognition and clearance. The constant region also determines the half-life of the antibody and its ability to cross the placenta, providing passive immunity to the fetus .
The constant region interacts with various molecules and cells to exert its functions. It binds to Fc receptors on immune cells, such as macrophages, neutrophils, and natural killer cells, triggering downstream signaling cascades that lead to phagocytosis, antibody-dependent cellular cytotoxicity, and release of inflammatory mediators . The constant region also interacts with complement proteins, leading to the formation of the membrane attack complex and lysis of pathogens .
The expression and activity of the Ig Heavy Chain Constant Region are tightly regulated at multiple levels. Transcriptional regulation involves various enhancers and promoters that control the expression of heavy chain genes . Post-translational modifications, such as glycosylation, are crucial for the stability and function of the antibody . Class switch recombination (CSR) is another regulatory mechanism that allows B cells to switch from producing one class of antibody to another, enabling a more effective immune response .
The Ig Heavy Chain Constant Region has numerous applications in biomedical research, diagnostics, and therapeutics. Monoclonal antibodies, which are engineered to have specific constant regions, are used in the treatment of various diseases, including cancers, autoimmune disorders, and infectious diseases . Diagnostic tools, such as ELISA and Western blot, rely on antibodies to detect specific antigens . Research on the constant region also aids in the development of vaccines and understanding immune mechanisms .
Throughout the life cycle, the Ig Heavy Chain Constant Region plays a critical role in immune defense. During development, it is involved in the maturation of B cells and the establishment of the immune repertoire . In adulthood, it contributes to the immune response against pathogens and the maintenance of immune memory . In aging, changes in the expression and function of the constant region can affect immune competence and susceptibility to infections and autoimmune diseases .
