Other Proteins

Human IgM Fab mu Peroxidase is ideal for investigators involved in serum protein component research. IgM is by far the physically largest antibody in the human circulatory system. It is the first antibody to appear in response to initial exposure to antigen. The spleen is the major site of specific IgM production. Distinct heavy chains differ in size and composition; alpha and gamma contain approximately 450 amino acids, while μ and ε have approximately 550 amino acids.

Human IgM (myeloma) Fc5µ fragment Peroxidase conjugate consists of only the µ (mu) chain of the Fc fragment. Immunoglobulin M is the largest antibody isotype and the first to be secreted against an initial exposure to antigen. IgM is predominantly produced in the spleen. IgM is formed from covalently linking 5 immunoglobulins together. Due to this large size, IgM is typically isolated to the serum.

Human serum albumin is the most abundant protein in human blood plasma. It is produced in the liver. Albumin constitutes about half of the blood serum protein. It is soluble and monomeric. Albumin transports hormones, fatty acids, and other compounds, buffers pH, and maintains osmotic pressure, among other functions. Human Albumin is ideal for investigators involved in serum protein component research.

Human transferrin is encoded by the TF gene and is an iron-binding blood plasma glycoprotein that controls the level of free iron in biological fluids. Human transferrin binds iron very tightly but reversibly. Human transferrin is the most important iron pool in mammals. Human transferrin has a molecular weight of around 80 kDa and contains 2 specific high-affinity Fe(III) binding sites. The affinity of Human transferrin for Fe(III) is extremely high but decreases progressively with decreasing pH below neutrality. Human Transferrin also plays a role in the immune system, creating environments low in iron for which many pathogenic bacteria are unable to thrive.

Human IgG purified protein (Immunoglobulin G) are antibody molecules. Human IgG is composed of four peptide chains — two heavy chains gamma and two light chains. Human IgG has two antigen binding sites. Other Immunoglobulins may be described in terms of polymers with the IgG structure considered the monomer. Human IgG typically constitutes 75% of serum immunoglobulins. Human IgG molecules are synthesized and secreted by plasma B cells.

Secreted as part of the adaptive immune response by plasma B cells, immunoglobulin G constitutes 75% of serum immunoglobulins. Immunoglobulin G binds to viruses, bacteria, as well as fungi and facilitates their destruction or neutralization via agglutination (and thereby immobilizing them), activation of the compliment cascade, and opsonization for phagocytosis. The whole IgG molecule possesses both the F(c) region, recognized by high-affinity Fc receptor proteins, as well as the F(ab) region possessing the epitope-recognition site. Both heavy and light chains of the antibody molecule are present. This Human IgG whole molecule is conjugated to biotin (Vitamin H), a small biomolecule that has a large affinity for avidin and streptavidin.

Human IgG Fc purified protein is a proteolytic fragment of immunoglobulin G (IgG) obtained by limited digestion with the enzyme papain under controlled conditions of temperature, time and pH. Receptors bind the Fc portion of Human IgG and often this fragment is removed from immunoglobulins to minimize receptor binding and lower background reactivity.

Human IgG F(ab')2 purified protein is a proteolytic fragment of immunoglobulin G (IgG) obtained by limited digestion with the enzyme pepsin under controlled conditions of temperature, time and pH. Human IgG F(ab')2 molecules lack the Fc portion of Human IgG and therefore receptors that bind Human IgG Fc will not bind Human IgG F(ab')2 molecules. This product possesses the F(ab')2 fragment, recognized by the two F(ab) fragments yielded from the digestion of the antibody below the disulfide bond hinge region.

Human IgG Fab Fragment Biotin Conjugate - secreted as part of the adaptive immune response by plasma B cells, immunoglobulin G constitutes 75% of serum immunoglobulins. Immunoglobulin G binds to viruses, bacteria, as well as fungi and facilitates their destruction or neutralization via agglutination (and thereby immobilizing them), activation of the compliment cascade, and opsonization for phagocytosis. The F(ab) fragment is the portion of the antibody that binds to the antigen target. The immunoglobulin Fab also possesses one constant and one variable region of both the heavy and light chain.