Proteins & Peptides

Bovine Collagen Type III 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, though Type III is the collagen associated with granulation tissues formed during healing.

Bovine Collagen Type IV 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, though Type IV in particular is involved in forming the foundation of cellular basement membranes, the lens of the eye, and within the capillaries of the glomeruli and nephron in the kidneys.

In muscle tissue, collagen serves as a major component of the endomysium. Collagen constitutes one to two percent of muscle tissue, and accounts for 6% of the weight of strong, tendinous muscles. A collagen may be defined as a protein containing sizable domain(s) of triple-helical conformation. Type IV collagen is a major macromolecular constituent of basement membranes and can be readily isolated from basement-membrane-rich tissues or highly vascularized tissues such as the placental villi. This collagen appears to be largely restricted to structures identifiable as basement membranes. In contrast, type VI collagen appears to be prevalent in several tissues even though it has been isolated largely from placental villi preparations. The extent to which type VII and VIII collagens are distributed is not known.

In muscle tissue, collagen serves as a major component of the endomysium. Collagen constitutes one to two percent of muscle tissue, and accounts for 6% of the weight of strong, tendinous muscles. A collagen may be defined as a protein containing sizable domain(s) of triple-helical conformation. Type IV collagen is a major macromolecular constituent of basement membranes and can be readily isolated from basement-membrane-rich tissues or highly vascularized tissues such as the placental villi. This collagen appears to be largely restricted to structures identifiable as basement membranes. In contrast, type VI collagen appears to be prevalent in several tissues even though it has been isolated largely from placental villi preparations. The extent to which type VII and VIII collagens are distributed is not known.

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 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.

Bovine 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. Bovine IgG F(ab')2 molecules lack the Fc portion of Bovine IgG and therefore receptors that bind Bovine IgG Fc will not bind Bovine 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.

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.

Bovine IgG F(c) Fragment 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. This product possesses the F(c) region, recognized by high-affinity Fc receptor proteins followed by agarose conjugation.