Our services include quantitative polymerase chain reaction (qPCR), reverse transcription polymerase chain reaction (RT-qPCR ), circular dichroism (CD) spectroscopy and electron paramagnetic resonance (EPR; a.k.a. electron spin resonance- ESR) spectroscopy, as well as sample preparation and data analysis.
Polymerase chain reaction (PCR) is a widely used laboratory technique for the amplification of specific DNA segments. PCR involves using short synthetic DNA fragments called primers to select a segment of the genome to be amplified, and then multiple rounds of DNA synthesis to further amplify that segment. We focus on reverse transcription quantitative PCR (RT-qPCR), using our 384-well QuantStudio 5 qPCR machine, which provides real-time detection of nucleotide sequence amplification at any sample concentration. qPCR uses fluorescence-based imaging to measure the amount of amplified DNA in real time. In RT-qPCR, total RNA is isolated and converted into cDNA via reverse transcription (RT). The cDNA is then used in the qPCR analysis. We can assist you at any step along the PCR process, from sample processing to data analysis. We offer quick turnaround with results delivered back to you within 2 weeks. After completion of the requested assay, a written report will be delivered back to you with the raw data and analysis that one of our PCR experts has analyzed.
qPCR Services
Circular Dichroism (CD) spectra are highly sensitive to distortions within chiral centers of biopolymers and is therefore especially useful in analyzing the secondary structure of biopolymers, especially proteins/peptides and nucleic acids (Rogers et al., 2019). CD spectroscopy is the most common approach for studying the overall conformation of biopolymers, such as proteins and peptides. CD is a spectroscopic method based on the interaction of chiral centers in the polymer with circular polarized light, which is very sensitive to levels of regular order in the polymer backbone. CD offers a convenient method for identifying changes in the structure of proteins and peptides.
CW-EPR spectroscopy provides a highly sensitive and specific method for probing the local structure, dynamics and environment of proteins (Garcia-Rubio, 2020) and lipid assemblies (Guzzi and Bartucci, 2015). The Site Directed Spin Labeling Electron Paramagnetic Resonance (SDSL-EPR) spectroscopy offers a unique approach to elucidate the structure and dynamics of biomolecules in solution. The approach combines protein chemistry/molecular genetics to target spin probes into biomolecules (most commonly peptides and proteins) with EPR analysis using modifications that can accommodate small biological samples under a variety of conditions (pure protein, tissue, live cells, etc.).
The EPR instrument services are categorized under three different service types, depending on the mode of data collection.
References
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