CCT Theta antibody | PK/13/72/8k
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|Rat anti CCT theta antibody, clone PK/13/72/8k recognizes the theta polypeptide of the CCT chaperonin molecule complex, also known as T-complex protein 1 subunit theta, CCT8 or CCTθ, a 547 amino acid ~:60 kDa molecular chaperone.
The intact CCT complex is composed of eight polypeptides in a double-ring structure. CCT is important within cells in aiding the folding of proteins including actin, tubulin and the VHL tumor suppressor protein.
- Species Cross-Reactivity
Target Species Cross Reactivity Mouse Rabbit Human Bovine
- N.B. Antibody reactivity and working conditions may vary between species.
- Product Form
- Purified IgG - liquid
- Purified IgG prepared by affinity chromatography on Protein G from tissue culture supernatant
- Buffer Solution
- Phosphate buffered saline
- Preservative Stabilisers
0.09% Sodium Azide
- Carrier Free
- Approx. Protein Concentrations
- IgG concentration 1.0 mg/ml
- For research purposes only
- 12 months from date of despatch
Avoid repeated freezing and thawing as this may denature the antibody. Storage in frost-free freezers is not recommended.
|Application Name||Verified||Min Dilution||Max Dilution|
- Western Blotting
- MCA2180 detects a band of approximately 60kD in lysates of heat shocked Hela cells.
References for CCT Theta antibody
Hynes, G. et al. (1996) Analysis of chaperonin-containing TCP-1 subunits in the human keratinocyte two-dimensional protein database: further characterisation of antibodies to individual subunits.
Electrophoresis. 17 (11): 1720-7.
Llorca, O. et al. (2000) Eukaryotic chaperonin CCT stabilizes actin and tubulin folding intermediates in open quasi-native conformations.
EMBO J. 19 (22): 5971-9.
Hynes, G.M. & Willison, K.R. (2000) Individual subunits of the eukaryotic cytosolic chaperonin mediate interactions with binding sites located on subdomains of beta-actin.
J Biol Chem. 275 (25): 18985-94.
Plimpton, R.L. et al. (2015) Structures of the Gβ-CCT and PhLP1-G&beta-CCT complexes reveal a mechanism for G-protein β-subunit folding and Gβγγ dimer assembly.
Proc Natl Acad Sci U S A. 112 (8): 2413-8.
Slater, L.H. et al. (2013) CCT chaperonin complex is required for efficient delivery of anthrax toxin into the cytosol of host cells.
Proc Natl Acad Sci U S A. 110 (24): 9932-7.
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