CCT Theta antibody | PK/13/72/8k

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WB ResetRat anti CCT Theta
- Product Type
- Monoclonal Antibody
- Clone
- PK/13/72/8k
- Isotype
- IgG2a
- Specificity
- CCT Theta
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
- Preparation
- Purified IgG prepared by affinity chromatography on Protein G from tissue culture supernatant
- Buffer Solution
- Phosphate buffered saline
- Preservative Stabilisers
- 0.09% sodium azide (NaN3)
- Carrier Free
- Yes
- Approx. Protein Concentrations
- IgG concentration 1.0 mg/ml
- Regulatory
- For research purposes only
- Guarantee
- 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 |
---|---|---|---|
Immunoprecipitation | ![]() |
||
Western Blotting | ![]() |
1/250 | 1/500 |
- Western Blotting
- Rat anti CCT antibody, clone PK/13/72/8k detects a band of approximately 60 kDa 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.
- RRID
- AB_2228910
- UniProt
- Q3ZCI9
- Entrez Gene
- CCT8
- GO Terms
- GO:0051082 unfolded protein binding
- GO:0006457 protein folding
- GO:0005524 ATP binding
- GO:0005815 microtubule organizing center
Please Note: All Products are "FOR RESEARCH PURPOSES ONLY"
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