Other Proteins

Isotype controls are important for Flow Cytometry and have no specificity for target cells within a particular experiment. Their purpose is to confirm the specificity of primary antibody binding that it is not a result of non-specific Fc receptor binding to cells or other cellular protein interactions. Isotype controls need to be matched to the specific primary Abs (species and isotype, including heavy and light chains) being used.

Mouse IgG whole molecule Agarose Conjugated product is made from IgG, 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.

Mouse IgG F(ab')2 Fragment Agarose Conjugated is a proteolytic fragment of immunoglobulin G (IgG) obtained by limited digestion with the enzyme pepsin under controlled conditions of temperature, time and pH. Mouse IgG F(ab')2 molecules lack the Fc portion of Mouse IgG and therefore receptors that bind Mouse IgG Fc will not bind Mouse 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 followed by agarose conjugation.

Mouse IgG purified protein (Immunoglobulin G) are antibody molecules. Mouse IgG is composed of four peptide chains — two heavy chains and two light chains. Mouse IgG has two antigen binding sites. Other Immunoglobulins may be described in terms of polymers with the IgG structure considered the monomer. Mouse IgG typically constitutes 75% of serum immunoglobulins. Mouse IgG molecules are synthesized and secreted by plasma B cells. Ideal as a negative control for Flow Cytometry, Western blotting, immunoprecipitation and immunohistochemistry applications.

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. This product possesses the F(c) region, recognized by high-affinity Fc receptor proteins.

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. 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.

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. This product possesses the F(ab) region possessing the epitope-recognition site, both heavy and light chains of the antibody molecule are present.

Mouse IgM, or mouse Immunoglobulin M, purified protein is a basic antibody that is produced by B cells. Mouse IgM is by far the physically largest antibody in the human circulatory system. Mouse IgM is the first antibody to appear in response to initial exposure to antigen. IgM is predominantly produced in the spleen. Mouse IgM is formed from covalently linking 5 immunoglobulins together, the approximate molecular weight of IgM is 900kDa and possesses 10 binding sites.

Mouse Transferrin is a blood plasma glycoprotein which binds iron and regulates the amount of available iron in circulation. Mouse Transferrin has a high affinity for iron, but this binding is reversible. Mouse Transferrin has a molecular weight of approximately 80kDa. Mouse Transferrin also plays a role in the immune system, creating environments low in iron for which many pathogenic bacteria are unable to thrive. This product is holo-transferrin and is loaded with iron prior to use and can be added directly to iron poor or iron-free cell culture media.