Human Normal Immunoglobulin

Human Normal Immunoglobulin Uses, Dosage, Side Effects, Food Interaction and all others data.

Intravenous immunoglobulin (IVIg) is a mixture of IgG1 and other antibodies derived from healthy human plasma via Cohn fractionation. The purification process includes cold alcohol fractionation, polyethylene glycol precipitation, and ion exchange chromatography. IVIg contains the same distribution of IgG antibody subclasses as is found in the general human population. IgG subclasses are fully represented in the following proportions: 70.3% IgG1, 24.7% IgG2, 3.1% IgG3, and 1.9% IgG4. IVIg is used in the treatment of immunodeficiencies, as well as autoimmune and inflammatory disorders.

Used as a replacement therapy in inherited humoral immunodeficiency disorders such as severe combined immunodeficiency syndrome, x-linked agammaglobulinemia, and Wiskott-Aldrich Syndrome. The immunoglobulins target, bind and kill bacterial cells as well as viral particles. IgG is the monomeric immunoglobulin of which there are four subclasses (IgG1, IgG2, IgG3 and IgG4) in differing abundances (66%, 23%, 7% and 4%). IgAs represent about 15% of the immunoglobulins in the blood. These target inhaled or ingested pathogens.

Trade Name Human Normal Immunoglobulin
Generic Human immunoglobulin G
Human immunoglobulin G Other Names Human IGG, Human immunoglobulin G, Human normal immunoglobulin, Immune globulin (human), Immune globulin human, Immunoglobulin (human), Immunoglobulin G (human), Immunoglobulin G, human, IVIg
Type
Formula C6332H9826N1692O1980S42
Weight 142682.3 Da
Groups Approved, Investigational
Therapeutic Class
Manufacturer
Available Country
Last Updated: September 19, 2023 at 7:00 am
Human Normal Immunoglobulin
Human Normal Immunoglobulin

Uses

Human Normal Immunoglobulin is a purified form of human immunoglobulin G and other proteins used to treat immunodeficiency and a wide variety of autoimmune disorders.

IVIg is used in the treatment of immunodeficiencies, as well as autoimmune and inflammatory disorders. These indications includes idiopathic thrombocytopenic purpura, Kawasaki disease, hypogammaglobulinemia, B cell chronic lymphocytic leukemia, bone marrow transplant complications, Guillain-Barré syndrome, chronic inflammatory demyelinating polyneuropathy (CIDP), multiple sclerosis, rheumatoid arthritis, myesthenia gravis, Wiskott–Aldrich syndrome and inflammatory skin diseases.

Human Normal Immunoglobulin is also used to associated treatment for these conditions: B-Cell Chronic Lymphocytic Leukemia, Bruton's agammaglobulinemia, Chronic Idiopathic Thrombocytopenic Purpura, Chronic Inflammatory Demyelinating Polyneuropathy (CIDP), Common Variable Immunodeficiency, Congenital Immunodeficiency, Kawasaki Syndrome, Wiskott-Aldrich Syndrome (WAS)

How Human Normal Immunoglobulin works

IVIg interacts with a number of different components of the immune system, including cytokines, complement, Fc receptors and several cell surface immunocompetent molecules. IVIg also impacts different effector cells of the immune system (B and T lymphocytes, dendritic cells, etc.) and regulates a wide range of genes. Its main mechanism of actions are believed to be Fc-dependent and F(ab')2-dependent. IVIg competitively blocks gamma Fc receptors, preventing the binding and ingestion of phagocytes and suppressing platelet depletion. IVIg contains a number of different antobodies, which prevent infection by attaching to the surface of invading pathogens and aiding in their disposal before they can infect cells. Antibodies remove pathogens via complement activation, agglutination or precipitation, pathogen receptor blocking, macrophage “tagging” or neutralization (via binding) of pathogen toxins. Intact IVIg and F(ab′)2 fragments of IVIg can also neutralize the activity of various autoantibodies. By triggering the production of interleukin-1 receptor antagonist, IVIg modulates of the production of cytokines and cytokine antagonists. It also prevents the generation of the C5b-9 membrane attack complex and subsequent complement-mediated tissue damage by binding active complement components.

Food Interaction

No interactions found.

Half Life

>20 hours (mammalian reticulocytes, in vitro).

Innovators Monograph

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