Keratin is one of a family of structural fibrous proteins also known as scleroproteins. Alpha-keratin (α-keratin) is a type of keratin found in vertebrates. It is the key structural material making up scales, hair, nails, feathers, horns, claws, hooves, and the outer layer of skin among vertebrates. Keratin also protects epithelial cells from damage or stress. Keratin is extremely insoluble in water and organic solvents. Keratin monomers assemble into bundles to form intermediate filaments, which are tough and form strong unmineralized epidermal appendages found in reptiles, birds, amphibians, and mammals. Excessive keratinization participate in fortification of certain tissues such as in horns of cattle and rhinos, and armadillos' osteoderm. The only other biological matter known to approximate the toughness of keratinized tissue is chitin.
Keratin comes in two types, the primitive, softer forms found in all vertebrates and harder, derived forms found only among sauropsids.
The horns of the impala are made of keratin covering a core of bone.
Protein sequence alignment of human keratin 1, 2A, 3,4, 5, 6A, 7, and 8 (KRT1 – KRT8). Only the first rod domain is shown above. Alignment was created using Clustal Omega.
In zoology, a scale is a small rigid plate that grows out of an animal's skin to provide protection. In lepidopterans, scales are plates on the surface of the insect wing, and provide coloration. Scales are quite common and have evolved multiple times through convergent evolution, with varying structure and function.
Keeled scales of a colubrid snake (banded water snake; Nerodia fasciata)
Placoid scales on a lemon shark (Negaprion brevirostris)
Brightly colored scales on a gold dust day gecko
Scales on talons of a Steller's sea eagle (Haliaeetus pelagicus)