PDF Antibody [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 |
Produced in rabbits immunized with E. coli-derived Human PDF fragment. |
Isotype |
IgG |
Clonality |
Polyclonal |
Host |
Rabbit |
Gene |
PDF |
Purity |
Antigen and protein A Affinity-purified |
Innovator's Reward |
Test in a species/application not listed above to receive a full credit towards a future purchase. |
Applications/Dilutions
Dilutions |
- Immunohistochemistry-Paraffin
|
Application Notes |
Optimal dilution of this antibody should be experimentally determined. |
Packaging, Storage & Formulations
Storage |
Store at 4C in the dark. Do not freeze. |
Buffer |
PBS |
Preservative |
No Preservative |
Purity |
Antigen and protein A Affinity-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 PDF Antibody [CoraFluor™ 1]
Background
Protein synthesis proceeds after formylation of methionine by methionyl-tRNA formyl transferase (FMT) and transfer of the charged initiator f-met tRNA to the ribosome. In eubacteria and eukaryotic organelles the product of this gene, peptide deformylase (PDF), removes the formyl group from the initiating methionine of nascent peptides. In eubacteria, deformylation of nascent peptides is required for subsequent cleavage of initiating methionines by methionine aminopeptidase. The discovery that a natural inhibitor of PDF, actinonin, acts as an antimicrobial agent in some bacteria has spurred intensive research into the design of bacterial-specific PDF inhibitors. In human cells, only mitochondrial proteins have N-formylation of initiating methionines. Protein inhibitors of PDF or siRNAs of PDF block the growth of cancer cell lines but have no effect on normal cell growth. In humans, PDF function may therefore be restricted to rapidly growing cells. [provided by RefSeq]
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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