Description_x000D_ General description_x000D_ Ubiquitin is a highly conserved, 8.6kDa, eukaryotic cellular protein containing 76 amino acid residues. Ubiquitin is absent in prokaryotes._x000D_ Specificity_x000D_ By immunoblotting, the antibody recognizes 1-3 protein bands using bovine red blood cell ubiquitin._x000D_ Immunogen_x000D_ bovine red blood cell ubiquitin._x000D_ Application_x000D_ Anti-Ubiquitin antibody produced in rabbit is used in:_x000D_ • immunostaining in neuropathology_x000D_ • immunohistochemistry_x000D_ • western blotting_x000D_ Target description_x000D_ Ubiquitin, present in both prokaryotes and eukaryotes, is a highly conserved 8.6 kDa protein. It is involved in the selective degradation of many short-lived proteins by the proteasome, an ATP-dependent protease. Proteins are targeted for degradation by covalent ligation to ubiquitin. This ubiquitin-mediated degradation of regulatory proteins plays important roles in the control of numerous processes, including cell-cycle progression, signal transduction, transcriptional regulation, receptor down-regulation, and endocytosis. It has also been implicated in immune response, metabolism, development, protein quality control, and apoptosis._x000D_ Physical form_x000D_ Lyophilized from 0.01 M phosphate buffer, containing 1% lactose._x000D_ Reconstitution_x000D_ Reconstitute the contents of the vial with 10 mL of Tris buffered saline. Since the antisera is preservative free, it is recommended that it be reconstituted in the presence of a preservative or aliquoted and frozen. Avoid repeated freeze/thaw cycles._x000D_ Disclaimer_x000D_ Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals._x000D_ Biochem/physiol Actions_x000D_ Ubiquitin is involved in the selective degradation of many short-lived proteins by 26S proteasome. Proteins are targeted for degradation by covalent ligation to ubiquitin. This ubiquitin-mediated degradation of regulatory proteins plays crucial roles in the regulation of various processes, such as cell-cycle progression, signal transduction, transcriptional regulation, receptor down-regulation, stress response, protein trafficking and endocytosis. Ubiquitin protein also aids in immune response, metabolism, development, normal protein turnover, protein quality control by degrading misfolded and damaged proteins and apoptosis. Variation in the ubiquitin-mediated processes results in carcinogenesis.