Trichohyalin and transglutaminase-3 and methods of using same

Chemistry: molecular biology and microbiology – Vector – per se

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435 691, 435193, 435325, 435348, 536 221, 536 231, 536 232, 536235, 536 243, 536 2431, 536 2433, C12N 1500, C12P 2106, C12H 910, C07H 1900

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active

056165005

ABSTRACT:
The sequences of a pair of human proteins, trichohyalin and transglutaminase-3, in addition to the sequence of the mouse transglutaminase-3 protein, have been discovered. The enzyme transglutaminase-3 is used to cross-link the structural protein trichohyalin in order to form a gel.

REFERENCES:
Kim et al. "The Deduced Sequence of the Novel Protransglutaminase . . . " J.B.C. 268:17 pp. 12682-12690 1993.
Kim et al. "The Complete Amino Acid Sequence . . . " J.B.C. 266:1 pp. 536-539 1991.
Kim et al. "Protransglutaminase E . . . " J.B.C. 265:35 pp. 21971-21978 1990.
Lee et al. "Generation of cDNA Probes . . . " Science 239:1288-1291 1988.
Park, et al., "Expression of Transglutaminase E in Cultured Human Keratinocytes and Skin Tissues", Progress in Clinical Biochemistry, pp. 275-278, 1992.
Kim, et al., "The Deduced Sequence of the Novel Protransglutaminase E (TGase3) of Human and Mouse", Journal of Biological Chemistry, vol. 268, No. 17, pp. 12682-12690, Jun. 15, 1993.
Lee, et al., "The Structure of Human Trichohyalin", Journal of Biological Chemistry, vol. 268, No. 16, pp. 12164-12178, Jun. 5, 1993.

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