PCYT1B Antibody (F39 P7 F11) [CoraFluor™ 1] Summary
Description |
CoraFluor(TM) 1 is a high performance terbium-based TR-FRET (Time-Resolved Fluorescence Resonance Energy Transfer) or TRF (Time-Resolved Fluorescence) donor for high throughput assay development. CoraFluor(IM) 1 absorbs UV light at approximately 340 nm, and emits at approximately 490 nm, 545 nm, 585 nm and 620 nm. It is compatible with common acceptor dyes that absorb at the emission wavelengths of CoraFluor(TM) 1. CoraFluor(TM) 1 can be used for the development of robust and scalable TR-FRET binding assays such as target engagement, ternary complex, protein-protein interaction and protein quantification assays. |
Immunogen |
Synthetic Peptide corresponding to the C-Terminus of Human CCT-beta. |
Specificity |
CCT-beta. |
Isotype |
IgG2a Kappa |
Clonality |
Monoclonal |
Host |
Mouse |
Gene |
PCYT1B |
Purity |
Protein A or G purified |
Innovator's Reward |
Test in a species/application not listed above to receive a full credit towards a future purchase. |
Applications/Dilutions
Dilutions |
|
Application Notes |
Optimal dilution of this antibody should be experimentally determined. |
Reactivity Notes
Packaging, Storage & Formulations
Storage |
Store at 4C in the dark. Do not freeze. |
Buffer |
PBS |
Preservative |
No Preservative |
Purity |
Protein A or G purified |
Notes
CoraFluor (TM) is a trademark of Bio-Techne Corp. Sold for research purposes only under agreement from Massachusetts General Hospital. US patent 2022/0025254
Alternate Names for PCYT1B Antibody (F39 P7 F11) [CoraFluor™ 1]
Background
TCP1 beta is a subunit of a cytosolic hetero-oligomer chaperon 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. 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.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are
guaranteed for 1 year from date of receipt.
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