Gelatin is a hydrocolloid and is rich in glycine, proline and hydroxyproline, which impart structural stability. It is synthesised from the alkaline digestion of collagen from bovine skin and is referred as type B. It has wide applications in food industry.

• Sterility: sterile
• Type: type B
• Gel strength: ~225 g bloom

Gelatin takes up random coil structure after digestion from the triple helical collagen. The most common source for industrial production of gelatin is slaughter byproducts. The type A gelatin from porcine and type B differ in their isoelectric pH. The N-terminal sequence of bovine gelatin is unique for its identification. It has gelling property and displays surface behaviour for use in foams and adhesions.

Gelatin has been used in many applications. It has use in coating cell culture to improve attachment of cells, being added to PCR to stabilise Taq DNA, as a blocking reagent in Western blotting, ELISA, and immunochemistry, and as a component of media for species differentiation in bacteriology. As a biocompatible polymer, it has been used as a delivery vehicle for release of active biomolecules and in the generation of scaffolds for tissue engineering applications. It has also been used to study long-chain fatty acid-induced changes in gene expression in neonatal cardiac monocytes and to study to test mobilisation of capillary endothelium in-vitro induced by effectors of angiogenesis in vivo. This product is recommended for use as a cell culture substratum at 1 to 5 μg/cm² or 0,5 to 50 μg/ml. The optimal concentration does depend on cell type as well as the application and research objectives.

Gelatin is a heterogeneous mixture of water-soluble proteins of high average molecular masses, present in collagen. Proteins are extracted by boiling the relevant skin, tendons, ligaments, bones, etc. in water. Type A gelatin is derived from acid-cured tissue. Type B is derived from lime-cured tissue.