Clone: F39 P7 F11.
Background: The protein TCP-1 (t-complex polypeptide 1) is a subunit of the hetero-oligomeric complex CCT (chaperonin containing TCP-1) present in the eukaryotic cytosol. The CCT of eukaryotic cytosol is composed of eight different subunit species that are proposed to have independent functions in folding its in vivo substrates, the Actins and Tubulins. TCP-1 was first identified in the mouse as relevant for tail-less and embryonic lethal phenotypes. Sequences homologous to TCP-1 have been isolated in several other species, and the yeast TCP-1 has been shown to encode a molecular chaperone for Actin and Tubulin. TCP-1 found in mammalian cells and yeast plays an important role in the folding of cytosolic proteins.
Positive Control: Colorectal cancer tissue, Calu6 and HT29 cell lysates.
Immunogen: Hybridoma produced by the fusion of splenocytes from BALB/c mice immunized with a synthetic peptide derived from the C-terminal of the TCP-1 protein and mouse myeloma Ag8563 cells. Sequence common in human, frog, mouse, rat.
Purification Method: Protein A/G Chromatography.
Formulation: Provided as solution in phosphate buffered saline with 0.08% sodium azide.
References: 1. Kubota, H., et al. (1999). Structures and co-regulated expression of the genes encoding mouse cytosolic chaperonin CCT subunits. Eur. J. Biochem. 262(2):492-500
2. Joly, E.C., et al. (1994). cDNA encoding a novel TCP1-related protein. Biochm. Biophys. Acta. 1217(2):224-226.
UniProt: P47207.
Caution: This product is intended FOR RESEARCH USE ONLY, and FOR TESTS IN VITRO, not for use in diagnostic or therapeutic procedures involving humans or animals.
English
Deutsch
