Preservative: NoneConstituents: PBS, 50mM Sodium Chloride, 10mM Sodium Phosphate, 0.1mM PMSF. pH 7.2
Store as concentrated solution. Centrifuge briefly prior to opening vial. For short-term storage (1-2 weeks), store at 4ºC. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.
0.34 mg/ml (Please refer to the vial label for the specific concentration.)
TCP1 beta peptide conjugated to purified tuberculin protein derivative (PPD) (Mouse).
Protein G purified
This antibody is affinity purified.
For laboratory use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.
Chaperonin Containing Tcp1, Subunit 2 (Beta),Cctb,Cct2
TCP1 beta is a subunit of a cytosolic hetero-oligomer chaperone (1,2) that is known to be involved in the folding of actin and tubulin. This protein is a member of the chaperonin family, which includes Escherichia coli GroEL, the mitochondrial heat-shock protein Hsp60, the plastid Rubisco-subunit-binding protein and the archaebacterial protein TF55. These chaperonins assist the folding of proteins upon ATP hydrolysis. Nine different subunits of TCP-1 containing chaperonin complexes from mammalian testis and seven different subunits of mouse F9 cells have been identified. The mouse TCP-1 subunits are between 531 and 545 residues in length. Their sequences are 2536% identical to one another, 2735% identical to that of TCP1 alpha and 3239% identical to that of the archaebacterial chaperonin, TF55. The genes for these subunits have been named Cctb, Cctg, Cctd, Ccte, Cctz and Ccth, which encode the CCTb, CCTg, CCTd, CCTe, CCTz, and CCTh subunits, respectively, of the `Chaperonin Containing TCP-1' (CCT). In bovine, CTT has also been referred to as `TRic', TCP-1 ring complex. All the CCT subunits contain motifs that are also shared by all other known chaperonins of prokaryotes and eukaryotic organelles, and that probably relate to their common ATPase function. It has been suggested that each CCT subunit has a specific, independent function, as they are highly diverged from each other but conserved from mammals to yeast. The expansion in the number of types of CCT subunit, compared with other chaperonins, has allowed CCT to carry out more complex functions that are required for the folding and assembly of highly evolved eukaryotic proteins.