CCT Beta antibody | PK/8/4/4i/2F
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|Rat anti Human CCT beta antibody recognizes human T-complex protein 1 subunit beta, also known as CCT beta, CCT2 or TCP-1-beta. CCT beta is a 535 amino acid cytoplasmically expressed chaperonin molecule involved in protein folding and has been shown to be involved in actin interaction (Llorca et al. 1999). Two isoforms of CCT beta have been described, arising from alternative splicing. It is not clear whether this Rat anti Human CCT beta antibody recognizes the shorter isoform 2, lacking the N-terminal 47 amino acids seen in isoform 1.
Rat anti Human CCT beta antibody recognizes CCT beta as a single band of ~ 57 kDa in multiple human cell line lysates by western blotting under reducing conditions and is cross reactive with both mouse and rat cell line lysates.
- Target Species
- Western Blotting
- Anti CCT beta antibody detects a band of approximately 57 kDa in Jurkat cell lysates.
- Species Cross-Reactivity
Target Species Cross Reactivity Rat Mouse
- N.B. Antibody reactivity and working conditions may vary between species.
- Product Form
- Purified IgG - liquid
- Rat monoclonal antibody purified by affinity chromatography on Protein G from tissue culture supernatant.
- Buffer Solution
- Phosphate buffered saline.
- Preservative Stabilisers
- 0.09% Sodium Azide (NaN3).
- Mouse CCT beta peptide conjugated to purified tuberculin protein derivative
- 0.5 mg/ml
- For research purposes only.
- 12 months from date of despatch.
- PrecisionAb is a trademark of Bio-Rad Laboratories.
|Application Name||Verified||Min Dilution||Max Dilution|
References for CCT Beta antibody
Satish, L. et al. (2010) Cloning and expression of rabbit CCT subunits eta and beta in healing cutaneous wounds.
Cell Stress Chaperones. 15 (6): 819-26.
Fislová, T. et al. (2010) Association of the influenza virus RNA polymerase subunit PB2 with the host chaperonin CCT.
J Virol. 84 (17): 8691-9.
Satish, L. et al. (2010) Chaperonin containing T-complex polypeptide subunit eta (CCT-eta) is a specific regulator of fibroblast motility and contractility.
PLoS One. 5 (4): e10063.
Plimpton, R.L. et al. (2015) Structures of the Gβ-CCT and PhLP1-Gβ-CCT complexes reveal a mechanism for G-protein β-subunit folding and Gβγ dimer assembly.
Proc Natl Acad Sci U S A. 112 (8): 2413-8.
Satish, L. et al. (2011) Chaperonin containing T-complex polypeptide (CCT) subunit expression in oral mucosal wounds and fibroblasts.
Cell Stress Chaperones. 16 (6): 675-80.
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