Proteins & Peptides

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.

Bovine Serum Albumin (BSA) is used for various biochemical applications including ELISA (Enzyme-Linked Immunosorbent Assay), high content screening assays, western blotting, FACS Buffer and immunohistochemistry. BSA as a blocking reagent is particularly useful with casein-sensitive antibodies, such as phospho-specific antibodies. Also used as a nutrient in cell and microbial culture. In restriction digests, BSA is used to stabilize some enzymes during digestion of DNA and to prevent adhesion of the enzyme to reaction tubes and other vessels. Bovine Serum Albumin can also be used to determine the quantity of other proteins, by comparing an unknown quantity of protein to known amounts of BSA.

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.

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 antibody 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) region possessing the epitope-recognition site, both heavy and light chains of the antibody molecule are present.

Bovine Serum Albumin (BSA) is used for various biochemical applications including ELISA (Enzyme-Linked Immunosorbent Assay), high content screening assays, western blotting, FACS Buffer and immunohistochemistry. BSA as a blocking reagent is particularly useful with casein-sensitive antibodies, such as phospho-specific antibodies. Also used as a nutrient in cell and microbial culture. In restriction digests, BSA is used to stabilize some enzymes during digestion of DNA and to prevent adhesion of the enzyme to reaction tubes and other vessels. Bovine Serum Albumin can also be used to determine the quantity of other proteins, by comparing an unknown quantity of protein to known amounts of BSA.

Bovine Collagen Type I is one of a family of proteins found particularly in the flesh and connective tissues of mammals (approximately one-third of the body's total protein). Over two dozen types of collagen have been described; Type I is the most abundant form in the body. Collagen Type I is found in scar tissue, tendons, the skin, arterial walls, the corneas, muscles, cartilage, and in the organic parts of bones and teeth. Bovine Collagen Type I is ideal for investigators involved in extracellular matrix proteins and osteoporosis.

Bovine Collagen Type I is one of a family of proteins found particularly in the flesh and connective tissues of mammals (approximately one-third of the body's total protein). Over two dozen types of collagen have been described; Type I is the most abundant form in the body. Collagen Type I is found in scar tissue, tendons, the skin, arterial walls, the corneas, muscles, cartilage, and in the organic parts of bones and teeth. Bovine Collagen Type I is ideal for investigators involved in extracellular matrix proteins and osteoporosis.

Bovine Collagen Type I is one of a family of proteins found particularly in the flesh and connective tissues of mammals (approximately one-third of the body's total protein). Over two dozen types of collagen have been described; Type I is the most abundant form in the body. Collagen Type I is found in scar tissue, tendons, the skin, arterial walls, the corneas, muscles, cartilage, and in the organic parts of bones and teeth. Bovine Collagen Type I is ideal for investigators involved in extracellular matrix proteins and osteoporosis.