CCT Epsilon antibody | PK/29/23/8d
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Rat anti CCT Epsilon
- Product Type
- Monoclonal Antibody
- CCT Epsilon
|Rat anti CCT epsilon antibody, clone PK/29/23/8d recognizes the epsilon polypeptide of the CCT chaperonin molecule complex. CCT epsilon, also known as T-complex protein 1 subunit epsilon, CCT5 or CCTε is a 540 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 tumour suppressor protein.
Two isoforms of CCTε produced by alternative splicing have been described. Rat anti CCT epsilon antibody, clone PK/29/23/8d binds to the canonical isoform 1, binding to the truncated isoform 2 has not been evaluated (UniProt : P48643).
Mutations in the CCT5 gene can lead to the development of Neuropathy, hereditary sensory, with spastic paraplegia, autosomal recessive (HSNSP) a disease characterized by spastic paraplegia and progressive neuropathy with limb ulceration (Bouhouche et al. 2006).
- Species Cross-Reactivity
Target Species Cross Reactivity Mouse Rabbit Rat 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 (NaN3)
- 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|
|Gel Super Shift Assays|
- Western Blotting
- Rat anti CCT epsilon antibody, clone PK/29/23/8d detects a band of approximately 60 kDa in lysates of heat shocked Hela cells.
References for CCT Epsilon 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.
Howlett, A.C. et al. (2009) Role of molecular chaperones in G protein beta5/regulator of G protein signaling dimer assembly and G protein betagamma dimer specificity.
J Biol Chem. 284 (24): 16386-99.
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.
Hara, T. et al. (2007) Mass spectrometry analysis of the native protein complex containing actinin-4 in prostate cancer cells.
Mol Cell Proteomics. 6 (3): 479-91.
Tracy, C.M. et al. (2014) Programmed Cell Death Protein 5 Interacts with the Cytosolic Chaperonin Containing Tailless Complex Polypeptide 1 (CCT) to Regulate β-Tubulin Folding.
J Biol Chem. 289: 4490-502.
Gao, X. et al. (2013) Splice isoforms of phosducin-like protein control the expression of heterotrimeric G proteins.
J Biol Chem. 288 (36): 25760-8.
Lai, C.W. et al. (2013) Phosducin-like protein 1 is essential for G-protein assembly and signaling in retinal rod photoreceptors.
J Neurosci. 33 (18): 7941-51.
Mak, W.S. et al. (2021) Novel Binding Partners for CCT and PhLP1 Suggest a Common Folding Mechanism for WD40 Proteins with a 7-Bladed Beta-Propeller Structure
Proteomes 9(4): 40
View The Latest Product References
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.
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