ABOUT

TASWEGIANkeritun takes its name from 'keratin' and its REspelling is an attempt to denote a REimaging of the keratin protein – the PREplastic material of the Gods. In the PREplastic era kertin was by and large a useful byproduct of 'the hunt' and animal husbandry and it was valued and useful in tool making and it often had talismanic values attributed to 'horn'.

Keratin is durable, eco-friendly and at the end of its usefulness as a 'tool' it returns to the earth gently. The plastics that displaced keratin given the huge quantities that can be produced quickly and cheaply accumulate in the environment causing great damage. Arguably it is time to reimagine keratin and explore its utility in a 21sr C context

Keratin (/ˈkɛrətɪn/) is one of a family of structural fibrous proteins also known as scleroproteins. It is the key structural material making up scales, hair, nails, feathers, horns, claws, hooves, and the outer layer of skin in tetrapod 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 the harder, derived forms found only among sauropsids (reptiles and birds)

Examples of occurrence

Alpha-keratins (α-keratins) are found in all vertebrates. They form the hair (including wool), the outer layer of skin, horns, nails, claws and hooves of mammals, and the slime threads of hagfish.

The baleen plates of filter-feeding whales are also made of keratin. Keratin filaments are abundant in keratinocytes in the hornified layer of the epidermis; these are proteins which have undergone keratinization. They are also present in epithelial cells in general. 

For example, mouse thymic epithelial cells react with antibodies for keratin 5, keratin 8, and keratin 14. These antibodies are used as fluorescent markers to distinguish subsets of mouse thymic epithelial cells in genetic studies of the thymus.

The harder beta-keratins (β-keratins) are found only in the sauropsids, i.e., all living reptiles and birds. They are found in the nails, scales, and claws of reptiles, in some reptile shells (Testudines), and in the feathers, beaks, and claws of birds.[9] These keratins are formed primarily in beta sheets. However, beta sheets are also found in α-keratins. Recent scholarship has shown that sauropsid β-keratins are fundamentally different from α-keratins at a genetic and structural level. The new term corneous beta protein (CBP) has been proposed to avoid confusion with α-keratins.

Keratins (also described as cytokeratins) are polymers of type I and type II intermediate filaments that have been found only in chordates (vertebrates, amphioxi, urochordates). Nematodes and many other non-chordate animals seem to have only type V intermediate filaments, fibers that structure the nucleus........CLICK HERE TO READ MORE .... READ AND SEE MORE HERE